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1. The Concise Guide to PHARMACOLOGY 2023/24: G protein-coupled receptors

Author: Alexander, SPH, Christopoulos, A, Davenport, AP, Kelly, E, Mathie, AA, Peters, JA, Veale, EL, Armstrong, JF, Faccenda, E, Harding, SD, Davies, JA, Abbracchio, MP, Abraham, G, Agoulnik, A, Alexander, W, Al-hosaini, K, Back, M, Baker, JG, Barnes, NM, Bathgate, R, Beaulieu, J-M, Beck-Sickinger, AG, Behrens, M, Bernstein, KE, Bettler, B, Birdsall, NJM, Blaho, V, Boulay, F, Bousquet, C, Brauner-Osborne, H, Burnstock, G, Calo, G, Castano, JP, Catt, KJ, Ceruti, S, Chazot, P, Chiang, N, Chini, B, Chun, J, Cianciulli, A, Civelli, O, Clapp, LH, Couture, R, Cox, HM, Csaba, Z, Dahlgren, C, Dent, G, Douglas, SD, Dournaud, P, Eguchi, S, Escher, E, Filardo, EJ, Fong, T, Fumagalli, M, Gainetdinov, RR, Garelja, ML, de Gasparo, M, Gerard, C, Gershengorn, M, Gobeil, F, Goodfriend, TL, Goudet, C, Gratz, L, Gregory, KJ, Gundlach, AL, Hamann, J, Hanson, J, Hauger, RL, Hay, DL, Heinemann, A, Herr, D, Hollenberg, MD, Holliday, ND, Horiuchi, M, Hoyer, D, Hunyady, L, Husain, A, Ijzerman, AP, Inagami, T, Jacobson, KA, Jensen, RT, Jockers, R, Jonnalagadda, D, Karnik, S, Kaupmann, K, Kemp, J, Kennedy, C, Kihara, Y, Kitazawa, T, Kozielewicz, P, Kreienkamp, H-J, Kukkonen, JP, Langenhan, T, Larhammar, D, Leach, K, Lecca, D, Lee, JD, Leeman, SE, Leprince, J, Li, XX, Lolait, SJ, Lupp, A, Macrae, R, Maguire, J, Malfacini, D, Mazella, J, McArdle, CA, Melmed, S, Michel, MC, Miller, LJ, Mitolo, V, Mouillac, B, Mueller, CE, Murphy, PM, Nahon, J-L, Ngo, T, Norel, X, Nyimanu, D, O'Carroll, A-M, Offermanns, S, Panaro, MA, Parmentier, M, Pertwee, RG, Pin, J-P, Prossnitz, ER, Quinn, M, Ramachandran, R, Ray, M, Reinscheid, RK, Rondard, P, Rovati, GE, Ruzza, C, Sanger, GJ, Schoeneberg, T, Schulte, G, Schulz, S, Segaloff, DL, Serhan, CN, Singh, KD, Smith, CM, Stoddart, LA, Sugimoto, Y, Summers, R, Tan, VP, Thal, D, Thomas, WW, Timmermans, PBMWM, Tirupula, K, Toll, L, Tulipano, G, Unal, H, Unger, T, Valant, C, Vanderheyden, P, Vaudry, D, Vaudry, H, Vilardaga, J-P, Walker, CS, Wang, JM, Ward, DT, Wester, H-J, Willars, GB, Williams, TL, Woodruff, TM, Yao, C, Ye, RD, Alexander, SPH, Christopoulos, A, Davenport, AP, Kelly, E, Mathie, AA, Peters, JA, Veale, EL, Armstrong, JF, Faccenda, E, Harding, SD, Davies, JA, Abbracchio, MP, Abraham, G, Agoulnik, A, Alexander, W, Al-hosaini, K, Back, M, Baker, JG, Barnes, NM, Bathgate, R, Beaulieu, J-M, Beck-Sickinger, AG, Behrens, M, Bernstein, KE, Bettler, B, Birdsall, NJM, Blaho, V, Boulay, F, Bousquet, C, Brauner-Osborne, H, Burnstock, G, Calo, G, Castano, JP, Catt, KJ, Ceruti, S, Chazot, P, Chiang, N, Chini, B, Chun, J, Cianciulli, A, Civelli, O, Clapp, LH, Couture, R, Cox, HM, Csaba, Z, Dahlgren, C, Dent, G, Douglas, SD, Dournaud, P, Eguchi, S, Escher, E, Filardo, EJ, Fong, T, Fumagalli, M, Gainetdinov, RR, Garelja, ML, de Gasparo, M, Gerard, C, Gershengorn, M, Gobeil, F, Goodfriend, TL, Goudet, C, Gratz, L, Gregory, KJ, Gundlach, AL, Hamann, J, Hanson, J, Hauger, RL, Hay, DL, Heinemann, A, Herr, D, Hollenberg, MD, Holliday, ND, Horiuchi, M, Hoyer, D, Hunyady, L, Husain, A, Ijzerman, AP, Inagami, T, Jacobson, KA, Jensen, RT, Jockers, R, Jonnalagadda, D, Karnik, S, Kaupmann, K, Kemp, J, Kennedy, C, Kihara, Y, Kitazawa, T, Kozielewicz, P, Kreienkamp, H-J, Kukkonen, JP, Langenhan, T, Larhammar, D, Leach, K, Lecca, D, Lee, JD, Leeman, SE, Leprince, J, Li, XX, Lolait, SJ, Lupp, A, Macrae, R, Maguire, J, Malfacini, D, Mazella, J, McArdle, CA, Melmed, S, Michel, MC, Miller, LJ, Mitolo, V, Mouillac, B, Mueller, CE, Murphy, PM, Nahon, J-L, Ngo, T, Norel, X, Nyimanu, D, O'Carroll, A-M, Offermanns, S, Panaro, MA, Parmentier, M, Pertwee, RG, Pin, J-P, Prossnitz, ER, Quinn, M, Ramachandran, R, Ray, M, Reinscheid, RK, Rondard, P, Rovati, GE, Ruzza, C, Sanger, GJ, Schoeneberg, T, Schulte, G, Schulz, S, Segaloff, DL, Serhan, CN, Singh, KD, Smith, CM, Stoddart, LA, Sugimoto, Y, Summers, R, Tan, VP, Thal, D, Thomas, WW, Timmermans, PBMWM, Tirupula, K, Toll, L, Tulipano, G, Unal, H, Unger, T, Valant, C, Vanderheyden, P, Vaudry, D, Vaudry, H, Vilardaga, J-P, Walker, CS, Wang, JM, Ward, DT, Wester, H-J, Willars, GB, Williams, TL, Woodruff, TM, Yao, C, and Ye, RD
Abstract: The Concise Guide to PHARMACOLOGY 2023/24 is the sixth in this series of biennial publications. The Concise Guide provides concise overviews, mostly in tabular format, of the key properties of approximately 1800 drug targets, and about 6000 interactions with about 3900 ligands. There is an emphasis on selective pharmacology (where available), plus links to the open access knowledgebase source of drug targets and their ligands (https://www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. Although the Concise Guide constitutes almost 500 pages, the material presented is substantially reduced compared to information and links presented on the website. It provides a permanent, citable, point-in-time record that will survive database updates. The full contents of this section can be found at http://onlinelibrary.wiley.com/doi/bph.16177. G protein-coupled receptors are one of the six major pharmacological targets into which the Guide is divided, with the others being: ion channels, nuclear hormone receptors, catalytic receptors, enzymes and transporters. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. The landscape format of the Concise Guide is designed to facilitate comparison of related targets from material contemporary to mid-2023, and supersedes data presented in the 2021/22, 2019/20, 2017/18, 2015/16 and 2013/14 Concise Guides and previous Guides to Receptors and Channels. It is produced in close conjunction with the Nomenclature and Standards Committee of the International Union of Basic and Clinical Pharmacology (NC-IUPHAR), therefore, providing official IUPHAR classification and nomenclature for human drug targets, where appropriate.
Published: 2023

2. THE CONCISE GUIDE TO PHARMACOLOGY 2021/22: G protein-coupled receptors

Author: Alexander, SPH, Christopoulos, A, Davenport, AP, Kelly, E, Mathie, A, Peters, JA, Veale, EL, Armstrong, JF, Faccenda, E, Harding, SD, Pawson, AJ, Southan, C, Davies, JA, Abbracchio, MP, Alexander, W, Al-hosaini, K, Baeck, M, Barnes, NM, Bathgate, R, Beaulieu, J-M, Bernstein, KE, Bettler, B, Birdsall, NJM, Blaho, V, Boulay, F, Bousquet, C, Braeuner-Osborne, H, Burnstock, G, Calo, G, Castano, JP, Catt, K, Ceruti, S, Chazot, P, Chiang, N, Chini, B, Chun, J, Cianciulli, A, Civelli, O, Clapp, LH, Couture, R, Csaba, Z, Dahlgren, C, Dent, G, Singh, KD, Douglas, SD, Dournaud, P, Eguchi, S, Escher, E, Filardo, EJ, Fong, T, Fumagalli, M, Gainetdinov, RR, de Gasparo, M, Gerard, C, Gershengorn, M, Gobeil, F, Goodfriend, TL, Goudet, C, Gregory, KJ, Gundlach, AL, Hamann, J, Hanson, J, Hauger, RL, Hay, DL, Heinemann, A, Hollenberg, MD, Holliday, ND, Horiuchi, M, Hoyer, D, Hunyady, L, Husain, A, IJzerman, AP, Inagami, T, Jacobson, KA, Jensen, RT, Jockers, R, Jonnalagadda, D, Karnik, S, Kaupmann, K, Kemp, J, Kennedy, C, Kihara, Y, Kitazawa, T, Kozielewicz, P, Kreienkamp, H-J, Kukkonen, JP, Langenhan, T, Leach, K, Lecca, D, Lee, JD, Leeman, SE, Leprince, J, Li, XX, Williams, TL, Lolait, SJ, Lupp, A, Macrae, R, Maguire, J, Mazella, J, McArdle, CA, Melmed, S, Michel, MC, Miller, LJ, Mitolo, V, Mouillac, B, Mueller, CE, Murphy, P, Nahon, J-L, Ngo, T, Norel, X, Nyimanu, D, Ocarroll, A-M, Offermanns, S, Panaro, MA, Parmentier, M, Pertwee, RG, Pin, J-P, Prossnitz, ER, Quinn, M, Ramachandran, R, Ray, M, Reinscheid, RK, Rondard, P, Rovati, GE, Ruzza, C, Sanger, GJ, Schoeneberg, T, Schulte, G, Schulz, S, Segaloff, DL, Serhan, CN, Stoddart, LA, Sugimoto, Y, Summers, R, Tan, VP, Thal, D, Thomas, WW, Timmermans, PMWM, Tirupula, K, Tulipano, G, Unal, H, Unger, T, Valant, C, Vanderheyden, P, Vaudry, D, Vaudry, H, Vilardaga, J-P, Walker, CS, Wang, JM, Ward, DT, Wester, H-J, Willars, GB, Woodruff, TM, Yao, C, Ye, RD, Alexander, SPH, Christopoulos, A, Davenport, AP, Kelly, E, Mathie, A, Peters, JA, Veale, EL, Armstrong, JF, Faccenda, E, Harding, SD, Pawson, AJ, Southan, C, Davies, JA, Abbracchio, MP, Alexander, W, Al-hosaini, K, Baeck, M, Barnes, NM, Bathgate, R, Beaulieu, J-M, Bernstein, KE, Bettler, B, Birdsall, NJM, Blaho, V, Boulay, F, Bousquet, C, Braeuner-Osborne, H, Burnstock, G, Calo, G, Castano, JP, Catt, K, Ceruti, S, Chazot, P, Chiang, N, Chini, B, Chun, J, Cianciulli, A, Civelli, O, Clapp, LH, Couture, R, Csaba, Z, Dahlgren, C, Dent, G, Singh, KD, Douglas, SD, Dournaud, P, Eguchi, S, Escher, E, Filardo, EJ, Fong, T, Fumagalli, M, Gainetdinov, RR, de Gasparo, M, Gerard, C, Gershengorn, M, Gobeil, F, Goodfriend, TL, Goudet, C, Gregory, KJ, Gundlach, AL, Hamann, J, Hanson, J, Hauger, RL, Hay, DL, Heinemann, A, Hollenberg, MD, Holliday, ND, Horiuchi, M, Hoyer, D, Hunyady, L, Husain, A, IJzerman, AP, Inagami, T, Jacobson, KA, Jensen, RT, Jockers, R, Jonnalagadda, D, Karnik, S, Kaupmann, K, Kemp, J, Kennedy, C, Kihara, Y, Kitazawa, T, Kozielewicz, P, Kreienkamp, H-J, Kukkonen, JP, Langenhan, T, Leach, K, Lecca, D, Lee, JD, Leeman, SE, Leprince, J, Li, XX, Williams, TL, Lolait, SJ, Lupp, A, Macrae, R, Maguire, J, Mazella, J, McArdle, CA, Melmed, S, Michel, MC, Miller, LJ, Mitolo, V, Mouillac, B, Mueller, CE, Murphy, P, Nahon, J-L, Ngo, T, Norel, X, Nyimanu, D, Ocarroll, A-M, Offermanns, S, Panaro, MA, Parmentier, M, Pertwee, RG, Pin, J-P, Prossnitz, ER, Quinn, M, Ramachandran, R, Ray, M, Reinscheid, RK, Rondard, P, Rovati, GE, Ruzza, C, Sanger, GJ, Schoeneberg, T, Schulte, G, Schulz, S, Segaloff, DL, Serhan, CN, Stoddart, LA, Sugimoto, Y, Summers, R, Tan, VP, Thal, D, Thomas, WW, Timmermans, PMWM, Tirupula, K, Tulipano, G, Unal, H, Unger, T, Valant, C, Vanderheyden, P, Vaudry, D, Vaudry, H, Vilardaga, J-P, Walker, CS, Wang, JM, Ward, DT, Wester, H-J, Willars, GB, Woodruff, TM, Yao, C, and Ye, RD
Abstract: The Concise Guide to PHARMACOLOGY 2021/22 is the fifth in this series of biennial publications. The Concise Guide provides concise overviews, mostly in tabular format, of the key properties of nearly 1900 human drug targets with an emphasis on selective pharmacology (where available), plus links to the open access knowledgebase source of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. Although the Concise Guide constitutes over 500 pages, the material presented is substantially reduced compared to information and links presented on the website. It provides a permanent, citable, point-in-time record that will survive database updates. The full contents of this section can be found at http://onlinelibrary.wiley.com/doi/bph.15538. G protein-coupled receptors are one of the six major pharmacological targets into which the Guide is divided, with the others being: ion channels, nuclear hormone receptors, catalytic receptors, enzymes and transporters. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. The landscape format of the Concise Guide is designed to facilitate comparison of related targets from material contemporary to mid-2021, and supersedes data presented in the 2019/20, 2017/18, 2015/16 and 2013/14 Concise Guides and previous Guides to Receptors and Channels. It is produced in close conjunction with the Nomenclature and Standards Committee of the International Union of Basic and Clinical Pharmacology (NC-IUPHAR), therefore, providing official IUPHAR classification and nomenclature for human drug targets, where appropriate.
Published: 2021

3. THE CONCISE GUIDE TO PHARMACOLOGY 2019/20: G protein-coupled receptors

Author: Alexander, SPH, Christopoulos, A, Davenport, AP, Kelly, E, Mathie, A, Peters, JA, Veale, EL, Armstrong, JF, Faccenda, E, Harding, SD, Pawson, AJ, Sharman, JL, Southan, C, Davies, JA, Arumugam, TV, Bennett, A, Sjogren, B, Sobey, C, Wong, SS, Abbracchio, MP, Alexander, W, Al-hosaini, K, Back, M, Beaulieu, J-M, Bernstein, KE, Bettler, B, Birdsall, NJM, Blaho, V, Bousquet, C, Brauner-Osborne, H, Burnstock, G, Calo, G, Castano, JP, Catt, KJ, Ceruti, S, Chazot, P, Chiang, N, Chun, J, Cianciulli, A, Clapp, LH, Couture, R, Csaba, Z, Dent, G, Singh, KD, Douglas, SD, Dournaud, P, Eguchi, S, Escher, E, Filardo, E, Fong, TM, Fumagalli, M, Gainetdinov, RR, de Gasparo, M, Gershengorn, M, Gobeil, F, Goodfriend, TL, Goudet, C, Gregory, KJ, Gundlach, AL, Hamann, J, Hanson, J, Hauger, RL, Hay, D, Heinemann, A, Hollenberg, MD, Holliday, ND, Horiuchi, M, Hoyer, D, Hunyady, L, Husain, A, Ijzerman, AP, Inagami, T, Jacobson, KA, Jensen, RT, Jockers, R, Jonnalagadda, D, Karnik, S, Kaupmann, K, Kemp, J, Kennedy, C, Kihara, Y, Kozielewicz, P, Kreienkamp, H-J, Kukkonen, JP, Langenhan, T, Leach, K, Lecca, D, Lee, JD, Leeman, SE, Leprince, J, Lolait, SJ, Lupp, A, Macrae, R, Maguire, J, Mazella, J, McArdle, CA, Melmed, S, Michel, MC, Miller, L, Mitolo, V, Mouillac, B, Murphy, PM, Nahon, J-L, Norel, X, Nyimanu, D, O'Carroll, A-M, Offermanns, S, Panaro, MA, Pertwee, RG, Pin, J-P, Prossnitz, E, Ramachandran, R, Reinscheid, RK, Rondard, P, Rovati, GE, Ruzza, C, Sanger, G, Schoeneberg, T, Schulte, G, Schulz, S, Segaloff, DL, Serhan, CN, Stoddart, LA, Sugimoto, Y, Summers, R, Tan, V, Thomas, W, Timmermans, PBMWM, Tirupula, K, Tulipano, G, Unal, H, Unger, T, Vanderheyden, P, Vaudry, D, Vaudry, H, Vilardaga, J-P, Walker, CS, Ward, DT, Wester, H-J, Willars, GB, Williams, TL, Woodruff, TM, Yao, C, Aldrich, RW, Becirovic, E, Biel, M, Catterall, WA, Conner, AC, Davies, P, Delling, M, Di Virgilio, F, Falzoni, S, George, C, Goldstein, SAN, Grissmer, S, Ha, K, Hammelmann, V, Hanukoglu, I, Jarvis, M, Jensen, AA, Kaczmarek, LK, Kellenberger, S, King, B, Lynch, JW, Perez-Reyes, E, Plant, LD, Rash, LD, Ren, D, Sivilotti, LG, Smart, TG, Snutch, TP, Tian, J, Van den Eynde, C, Vriens, J, Wei, AD, Winn, BT, Wulff, H, Xu, H, Yue, L, Zhang, X, Zhu, M, Coons, L, Fuller, P, Korach, KS, Young, M, Bryant, C, Farndale, RW, Hobbs, A, Jarvis, GE, MacEwan, D, Monie, TP, Waldman, S, Beuve, A, Boison, D, Brouckaert, P, Burnett, JC, Burns, K, Dessauer, C, Friebe, A, Garthwaite, J, Gertsch, J, Helsby, N, Izzo, AA, Koesling, D, Kuhn, M, Ostrom, R, Papapetropoulos, A, Potter, LR, Pyne, NJ, Pyne, S, Russwurm, M, Schmidt, HHHW, Seifert, R, Stasch, J-P, Szabo, C, van der Stelt, M, van der Vliet, A, Watts, V, Anderson, CMH, Broer, S, Dawson, P, Hagenbuch, B, Hammond, JR, Hancox, J, Inui, K-I, Kanai, Y, Kemp, S, Thwaites, DT, Verri, T, Alexander, SPH, Christopoulos, A, Davenport, AP, Kelly, E, Mathie, A, Peters, JA, Veale, EL, Armstrong, JF, Faccenda, E, Harding, SD, Pawson, AJ, Sharman, JL, Southan, C, Davies, JA, Arumugam, TV, Bennett, A, Sjogren, B, Sobey, C, Wong, SS, Abbracchio, MP, Alexander, W, Al-hosaini, K, Back, M, Beaulieu, J-M, Bernstein, KE, Bettler, B, Birdsall, NJM, Blaho, V, Bousquet, C, Brauner-Osborne, H, Burnstock, G, Calo, G, Castano, JP, Catt, KJ, Ceruti, S, Chazot, P, Chiang, N, Chun, J, Cianciulli, A, Clapp, LH, Couture, R, Csaba, Z, Dent, G, Singh, KD, Douglas, SD, Dournaud, P, Eguchi, S, Escher, E, Filardo, E, Fong, TM, Fumagalli, M, Gainetdinov, RR, de Gasparo, M, Gershengorn, M, Gobeil, F, Goodfriend, TL, Goudet, C, Gregory, KJ, Gundlach, AL, Hamann, J, Hanson, J, Hauger, RL, Hay, D, Heinemann, A, Hollenberg, MD, Holliday, ND, Horiuchi, M, Hoyer, D, Hunyady, L, Husain, A, Ijzerman, AP, Inagami, T, Jacobson, KA, Jensen, RT, Jockers, R, Jonnalagadda, D, Karnik, S, Kaupmann, K, Kemp, J, Kennedy, C, Kihara, Y, Kozielewicz, P, Kreienkamp, H-J, Kukkonen, JP, Langenhan, T, Leach, K, Lecca, D, Lee, JD, Leeman, SE, Leprince, J, Lolait, SJ, Lupp, A, Macrae, R, Maguire, J, Mazella, J, McArdle, CA, Melmed, S, Michel, MC, Miller, L, Mitolo, V, Mouillac, B, Murphy, PM, Nahon, J-L, Norel, X, Nyimanu, D, O'Carroll, A-M, Offermanns, S, Panaro, MA, Pertwee, RG, Pin, J-P, Prossnitz, E, Ramachandran, R, Reinscheid, RK, Rondard, P, Rovati, GE, Ruzza, C, Sanger, G, Schoeneberg, T, Schulte, G, Schulz, S, Segaloff, DL, Serhan, CN, Stoddart, LA, Sugimoto, Y, Summers, R, Tan, V, Thomas, W, Timmermans, PBMWM, Tirupula, K, Tulipano, G, Unal, H, Unger, T, Vanderheyden, P, Vaudry, D, Vaudry, H, Vilardaga, J-P, Walker, CS, Ward, DT, Wester, H-J, Willars, GB, Williams, TL, Woodruff, TM, Yao, C, Aldrich, RW, Becirovic, E, Biel, M, Catterall, WA, Conner, AC, Davies, P, Delling, M, Di Virgilio, F, Falzoni, S, George, C, Goldstein, SAN, Grissmer, S, Ha, K, Hammelmann, V, Hanukoglu, I, Jarvis, M, Jensen, AA, Kaczmarek, LK, Kellenberger, S, King, B, Lynch, JW, Perez-Reyes, E, Plant, LD, Rash, LD, Ren, D, Sivilotti, LG, Smart, TG, Snutch, TP, Tian, J, Van den Eynde, C, Vriens, J, Wei, AD, Winn, BT, Wulff, H, Xu, H, Yue, L, Zhang, X, Zhu, M, Coons, L, Fuller, P, Korach, KS, Young, M, Bryant, C, Farndale, RW, Hobbs, A, Jarvis, GE, MacEwan, D, Monie, TP, Waldman, S, Beuve, A, Boison, D, Brouckaert, P, Burnett, JC, Burns, K, Dessauer, C, Friebe, A, Garthwaite, J, Gertsch, J, Helsby, N, Izzo, AA, Koesling, D, Kuhn, M, Ostrom, R, Papapetropoulos, A, Potter, LR, Pyne, NJ, Pyne, S, Russwurm, M, Schmidt, HHHW, Seifert, R, Stasch, J-P, Szabo, C, van der Stelt, M, van der Vliet, A, Watts, V, Anderson, CMH, Broer, S, Dawson, P, Hagenbuch, B, Hammond, JR, Hancox, J, Inui, K-I, Kanai, Y, Kemp, S, Thwaites, DT, and Verri, T
Abstract: The Concise Guide to PHARMACOLOGY 2019/20 is the fourth in this series of biennial publications. The Concise Guide provides concise overviews of the key properties of nearly 1800 human drug targets with an emphasis on selective pharmacology (where available), plus links to the open access knowledgebase source of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. Although the Concise Guide represents approximately 400 pages, the material presented is substantially reduced compared to information and links presented on the website. It provides a permanent, citable, point-in-time record that will survive database updates. The full contents of this section can be found at http://onlinelibrary.wiley.com/doi/10.1111/bph.14748. G protein-coupled receptors are one of the six major pharmacological targets into which the Guide is divided, with the others being: ion channels, nuclear hormone receptors, catalytic receptors, enzymes and transporters. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. The landscape format of the Concise Guide is designed to facilitate comparison of related targets from material contemporary to mid-2019, and supersedes data presented in the 2017/18, 2015/16 and 2013/14 Concise Guides and previous Guides to Receptors and Channels. It is produced in close conjunction with the International Union of Basic and Clinical Pharmacology Committee on Receptor Nomenclature and Drug Classification (NC-IUPHAR), therefore, providing official IUPHAR classification and nomenclature for human drug targets, where appropriate.
Published: 2019

4. First In human study of a novel biased apelin receptor ligand, MM54, a G-alpha(i) agonist/beta-arrestin antagonist

Author: Davenport, AP, Brame, AL, Kuc, RE, Cheriyan, J, Glen, RR, Wilkinson, IB, and Maguire, JJ
Subjects: Science & Technology, Cardiac & Cardiovascular Systems, Peripheral Vascular Disease, Cardiovascular System & Hematology, Vascular, Cardiovascular System & Cardiology, Apelin, 1103 Clinical Sciences, Hematology, Peptides, Ligands, Life Sciences & Biomedicine, 1102 Cardiorespiratory Medicine and Haematology
Abstract: Introduction: The peptide apelin acts via G proteins to cause beneficial vasodilation and potent positive inotropy to ameliorate pulmonary arterial hypertension in humans and animal models. Apelin is internalised via β-arrestin. In contrast, with loss of endogenous apelin, its receptor acts as a mechanosensor, stimulating β-arrestin to induce detrimental cardiac hypertrophy. Our aim was to characterise the action of our apelin ligand, MM54 that in cell based assays blocks β-arrestin but activates the Gαi protein pathway, in this first in human study. Method: Competition binding in human heart (n=3) used [I125] [Pyr1]apelin-13 (0.1nmol/L). β-arrestin recruitment, receptor internalization and forskolin-induced cAMP inhibition were measured in CHO-K1 cells expressing human apelin receptor. Forearm blood flow was measured in 9 volunteers using venous occlusion plethysmography at baseline and at 4 incremental doses (1, 10, 30, 100 nmol/min) of MM54, each for eight minutes. The Aellig hand vein technique was used to measure the effect of 3 incremental doses (3, 30, 300 nmol/min) of MM54 for 15 min on veins pre-constricted with noradrenaline in 6 individuals compared with 8 controls. Data are mean+SEM, n≥3. Results: MM54 had an affinity of pKi = 6.50±0.03. In β-arrestin (pKB 6.93±0.15) and receptor internalization assays (pKB 5.89±0.06) MM54 was an antagonist, but activated the G protein pathway (pD2±SEM 5.86+0.23). At the highest concentration (100 nmol/min), MM54 caused a significant absolute increase in forearm blood flow compared to control arm, representing a 76 % change from baseline (P
Published: 2018

5. International Union of Basic and Clinical Pharmacology: Chemerin Receptors CMKLR1 (ChemerinWell1) and GPR1 (Chemerin2) Nomenclature, Pharmacology and Function

Author: Davenport, AP, Kennedy, A, Davenport, Anthony [0000-0002-2096-3117], and Apollo - University of Cambridge Repository
Subjects: Terminology as Topic, Animals, Humans, Receptors, Chemokine, Amino Acid Sequence, Receptors, G-Protein-Coupled
Abstract: Chemerin, a chemoattractant protein and adipokine, has been identified as the endogenous ligand for a G protein-coupled receptor encoded by the gene CMKLR1 (also known as ChemR23) and as a consequence the receptor protein was renamed the chemerin receptor in 2013. Since then, chemerin has been identified as the endogenous ligand for a second G protein-coupled receptor, encoded by the gene GPR1. Therefore, the International Union of Basic and Clinical Pharmacology Committee on Receptor Nomenclature and Drug Classification recommends that the official name of the receptor protein for CMKLR1 is chemerin receptor 1 and GPR1 is chemerin receptor 2 to follow the convention of naming the receptor protein after the endogenous ligand. Chemerin receptor 1 and chemerin receptor 2 can be abbreviated to Chemerin1 and Chemerin2 respectively. Chemerin requires C-terminal processing for activity and human chemerin21-157 is reported to be the most active form, with peptide fragments derived from the C-terminus biologically active at both receptors. Small molecule antagonist, CCX832, selectively blocks CMKLR1, and resolvin E1 activation of CMKLR1 is discussed. Activation of both receptors by chemerin is via coupling to Gi/o causing inhibition of adenylyl cyclase and increased Ca2+ flux. Receptors and ligand are widely expressed in human, rat and mouse, and both receptors share ~80% identity across these species. CMKLR1 knock-out mice highlight the role of this receptor in inflammation and obesity and similarly GPR1 knock-out mice exhibit glucose intolerance. In addition, the chemerin receptors have been implicated in cardiovascular disease, cancer, steroidogenesis, HIV replication and neurogenerative disease.
Published: 2018

6. IS ENDOTHELIN CONVERTING ENZYME ACTIVITY INCREASED IN CHRONIC HEART FAILURE?

Author: Love, Plumpton, C, Webb, DJ, Davenport, AP, and McMurray, JJV
Published: 1997

7. Detection of Atherosclerotic Inflammation by $^{68}$Ga-DOTATATE PET Compared to [$^{18}$F]FDG PET Imaging

Author: Tarkin, JM, Joshi, FR, Evans, NR, Chowdhury, MM, Figg, NL, Shah, AV, Starks, LT, Martin-Garrido, A, Manavaki, R, Yu, E, Kuc, RE, Grassi, L, Kreuzhuber, R, Kostadima, MA, Frontini, M, Kirkpatrick, PJ, Coughlin, PA, Gopalan, D, Fryer, TD, Buscombe, JR, Groves, AM, Ouwehand, WH, Bennett, MR, Warburton, EA, Davenport, AP, Rudd, JHF, Tarkin, Jason [0000-0002-9132-120X], Evans, Nicholas [0000-0002-7640-4701], Manavaki, Roido [0000-0002-4384-6626], Grassi, Luigi [0000-0002-6308-7540], Frontini, Mattia [0000-0001-8074-6299], Ouwehand, Willem [0000-0002-7744-1790], Bennett, Martin [0000-0002-2565-1825], Davenport, Anthony [0000-0002-2096-3117], Rudd, James [0000-0003-2243-3117], and Apollo - University of Cambridge Repository
Subjects: somatostatin receptor, positron emission tomography, inflammation, atherosclerosis, molecular imaging, macrophages
Abstract: $\textbf{Background}$ Inflammation drives atherosclerotic plaque rupture. Although inflammation can be measured using fluorine-18-labeled fluorodeoxyglucose positron emission tomography ([$^{18}$F]FDG PET), [$^{18}$F]FDG lacks cell specificity, and coronary imaging is unreliable because of myocardial spillover. $\textbf{Objectives}$ Objectives This study tested the efficacy of gallium-68-labeled DOTATATE ($^{68}$Ga-DOTATATE), a somatostatin receptor subtype-2 (SST2)-binding PET tracer, for imaging atherosclerotic inflammation. $\textbf{Methods}$ We confirmed $^{68}$Ga-DOTATATE binding in macrophages and excised carotid plaques. $^{68}$Ga-DOTATATE PET imaging was compared to [$^{18}$F]FDG PET imaging in 42 patients with atherosclerosis. $\textbf{Results}$ Target $\textit{SSTR2}$ gene expression occurred exclusively in “proinflammatory” M1 macrophages, specific $^{68}$Ga-DOTATATE ligand binding to SST$_{2}$ receptors occurred in CD68-positive macrophage-rich carotid plaque regions, and carotid $\textit{SSTR2}$ mRNA was highly correlated with in vivo $^{68}$Ga-DOTATATE PET signals (r = 0.89; 95% confidence interval [CI]: 0.28 to 0.99; p = 0.02). $^{68}$Ga-DOTATATE mean of maximum tissue-to-blood ratios (mTBR$_{max}$) correctly identified culprit versus nonculprit arteries in patients with acute coronary syndrome (median difference: 0.69; interquartile range [IQR]: 0.22 to 1.15; p = 0.008) and transient ischemic attack/stroke (median difference: 0.13; IQR: 0.07 to 0.32; p = 0.003). $^{68}$Ga-DOTATATE mTBR$_{max}$ predicted high-risk coronary computed tomography features (receiver operating characteristics area under the curve [ROC AUC]: 0.86; 95% CI: 0.80 to 0.92; p < 0.0001), and correlated with Framingham risk score (r = 0.53; 95% CI: 0.32 to 0.69; p
Published: 2017

8. [Pyr¹]Apelin-13(₁-₁₂) Is a Biologically Active ACE2 Metabolite of the Endogenous Cardiovascular Peptide [Pyr¹]Apelin-13

Author: Yang, P, Kuc, RE, Brame, AL, Dyson, A, Singer, M, Glen, RC, Cheriyan, J, Wilkinson, IB, Davenport, AP, Maguire, JJ, Glen, Robert [0000-0003-1759-2914], Cheriyan, Joseph [0000-0001-6921-1592], Wilkinson, Ian [0000-0001-6598-9399], Davenport, Anthony [0000-0002-2096-3117], Maguire, Janet [0000-0002-9254-7040], and Apollo - University of Cambridge Repository
Subjects: apelin, forearm plethysmography, [Pyr1]apelin-13(1–12), pulmonary arterial hypertension, fungi, ACE2, human heart, apelin receptor, biased signaling
Abstract: Aims: Apelin is a predicted substrate for ACE2, a novel therapeutic target. Our aim was to demonstrate the endogenous presence of the putative ACE2 product [Pyr(1)]apelin-13(1-12) in human cardiovascular tissues and to confirm it retains significant biological activity for the apelin receptor in vitro and in vivo. The minimum active apelin fragment was also investigated. Methods and Results: [Pyr(1)]apelin-13 incubated with recombinant human ACE2 resulted in de novo generation of [Pyr(1)]apelin-13(1-12) identified by mass spectrometry. Endogenous [Pyr(1)]apelin-13(1-12) was detected by immunostaining in human heart and lung localized to the endothelium. Expression was undetectable in lung from patients with pulmonary arterial hypertension. In human heart [Pyr(1)]apelin-13(1-12) (pKi = 8.04 ± 0.06) and apelin-13(F13A) (pKi = 8.07 ± 0.24) competed with [(125)I]apelin-13 binding with nanomolar affinity, 4-fold lower than for [Pyr(1)]apelin-13 (pKi = 8.83 ± 0.06) whereas apelin-17 exhibited highest affinity (pKi = 9.63 ± 0.17). The rank order of potency of peptides to inhibit forskolin-stimulated cAMP was apelin-17 (pD2 = 10.31 ± 0.28) > [Pyr(1)]apelin-13 (pD2 = 9.67 ± 0.04) ≥ apelin-13(F13A) (pD2 = 9.54 ± 0.05) > [Pyr(1)]apelin-13(1-12) (pD2 = 9.30 ± 0.06). The truncated peptide apelin-13(R10M) retained nanomolar potency (pD2 = 8.70 ± 0.04) but shorter fragments exhibited low micromolar potency. In a β-arrestin recruitment assay the rank order of potency was apelin-17 (pD2 = 10.26 ± 0.09) > [Pyr(1)]apelin-13 (pD2 = 8.43 ± 0.08) > apelin-13(R10M) (pD2 = 8.26 ± 0.17) > apelin-13(F13A) (pD2 = 7.98 ± 0.04) ≥ [Pyr(1)]apelin-13(1-12) (pD2 = 7.84 ± 0.06) > shorter fragments (pD2 < 6). [Pyr(1)]apelin-13(1-12) and apelin-13(F13A) contracted human saphenous vein with similar sub-nanomolar potencies and [Pyr(1)]apelin-13(1-12) was a potent inotrope in paced mouse right ventricle and human atria. [Pyr(1)]apelin-13(1-12) elicited a dose-dependent decrease in blood pressure in anesthetized rat and dose-dependent increase in forearm blood flow in human volunteers. Conclusions: We provide evidence that ACE2 cleaves [Pyr(1)]apelin-13 to [Pyr(1)]apelin-13(1-12) and this cleavage product is expressed in human cardiovascular tissues. We have demonstrated biological activity of [Pyr(1)]apelin-13(1-12) at the human and rodent apelin receptor in vitro and in vivo. Our data show that reported enhanced ACE2 activity in cardiovascular disease should not significantly compromise the beneficial effects of apelin based therapies for example in PAH.
Published: 2017
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9. Elabela/Toddler is an Endogenous Agonist of the Apelin APJ Receptor in the Adult Cardiovascular System, and Exogenous Administration of the Peptide Compensates for the Downregulation of its Expression in Pulmonary Arterial Hypertension

Author: Yang, P, Read, C, Kuc, RE, Buonincontri, G, Southwood, M, Torella, R, Upton, PD, Crosby, A, Sawiak, SJ, Carpenter, TA, Glen, RC, Morrell, NW, Maguire, JJ, Davenport, AP, Upton, Paul [0000-0003-2716-4921], Sawiak, Stephen [0000-0003-4210-9816], Carpenter, Adrian [0000-0002-2939-8222], Glen, Robert [0000-0003-1759-2914], Morrell, Nicholas [0000-0001-5700-9792], Maguire, Janet [0000-0002-9254-7040], Davenport, Anthony [0000-0002-2096-3117], and Apollo - University of Cambridge Repository
Subjects: receptors, G-protein-coupled, Male, Cardiac & Cardiovascular Systems, Toddler, cardiopulmonary, Heart Ventricles, Hypertension, Pulmonary, Peptide Hormones, receptor, Down-Regulation, Molecular Dynamics Simulation, IMMUNOCYTOCHEMICAL LOCALIZATION, DISEASE, Catheterization, 1117 Public Health and Health Services, PATHWAY, Rats, Sprague-Dawley, GPCR, pulmonary hypertension, Animals, Humans, Amino Acid Sequence, 1102 Cardiorespiratory Medicine and Haematology, IN-VIVO, Science & Technology, Binding Sites, Monocrotaline, APELA, 1103 Clinical Sciences, ENDOTHELIAL-CELLS, peptide, Protein Structure, Tertiary, Rats, Disease Models, Animal, Peripheral Vascular Disease, Cardiovascular System & Hematology, apelin, Elabela/Toddler, Cardiovascular System & Cardiology, HEART, Intercellular Signaling Peptides and Proteins, Elabela, Endothelium, Vascular, LIGAND, Life Sciences & Biomedicine, CARDIAC CONTRACTILITY
Abstract: BACKGROUND: -Elabela/Toddler (ELA) is a critical cardiac developmental peptide that acts through the G protein-coupled apelin receptor, despite lack of sequence similarity to the established ligand apelin. Our aim was to investigate the receptor pharmacology, expression pattern and in vivo function of ELA peptides in the adult cardiovascular system, to seek evidence for alteration in pulmonary arterial hypertension (PAH) in which apelin signaling is down-regulated, and to demonstrate attenuation of PAH severity with exogenous administration of ELA in a rat model. METHODS: -In silico docking analysis, competition binding experiments and down-stream assays were used to characterize ELA receptor binding in human heart and signaling in cells expressing the apelin receptor. ELA expression in human cardiovascular tissues and plasma was determined using RT-qPCR, dual-labelling immunofluorescent staining and immunoassays. Acute cardiac effects of ELA-32 and [Pyr(1)]apelin-13 were assessed by magnet resonance imaging and cardiac catheterization in anesthetized rats. Cardiopulmonary human and rat tissues from PAH patients and monocrotaline (MCT) and Sugen/hypoxia exposed rats were used to show changes in ELA expression in PAH. The effect of ELA treatment on cardiopulmonary remodeling in PAH was investigated in the MCT rat model. RESULTS: -ELA competed for binding of apelin in human heart with overlap for the two peptides indicated by in silico modeling. ELA activated G protein- and Β-arrestin-dependent pathways. We detected ELA expression in human vascular endothelium and plasma. Comparable to apelin, ELA increased cardiac contractility, ejection fraction, cardiac output and elicited vasodilatation in rat in vivo ELA expression was reduced in cardiopulmonary tissues from PAH patients and PAH rat models, respectively. ELA treatment significantly attenuated elevation of right ventricular systolic pressure and right ventricular hypertrophy and pulmonary vascular remodeling in MCT exposed rats. CONCLUSIONS: -These results show ELA is an endogenous agonist of the human apelin receptor, exhibits a cardiovascular profile comparable to apelin, is down-regulated in human disease and rodent PAH models and exogenous peptide can reduce the severity of cardiopulmonary remodeling and function in PAH in rats. This study provides additional proof of principle that an apelin receptor agonist may be of therapeutic use in PAH in man.
Published: 2017

10. $^{18}$F-Fluoride and $^{18}$F-Fluorodeoxyglucose Positron Emission Tomography After Transient Ischemic Attack or Minor Ischemic Stroke: Case-Control Study

Author: Vesey, AT, Jenkins, WSA, Irkle, A, Moss, A, Sng, G, Forsythe, RO, Clark, T, Roberts, G, Fletcher, A, Lucatelli, C, Rudd, JHF, Davenport, AP, Mills, NL, Al-Shahi Salman, R, Dennis, M, Whiteley, WN, van Beek, EJR, Dweck, MR, Newby, DE, Rudd, James [0000-0003-2243-3117], Davenport, Anthony [0000-0002-2096-3117], and Apollo - University of Cambridge Repository
Subjects: fluorides, inflammation, phenotype, carotid stenosis, nuclear medicine, stroke
Abstract: BACKGROUND: Combined positron emission tomography (PET) and computed tomography (CT) can assess both anatomy and biology of carotid atherosclerosis. We sought to assess whether $^{18}$F-fluoride or $^{18}$F-fluorodeoxyglucose can identify culprit and high-risk carotid plaque. METHODS AND RESULTS: We performed $^{18}$F-fluoride and $^{18}$F-fluorodeoxyglucose PET/CT in 26 patients after recent transient ischemic attack or minor ischemic stroke: 18 patients with culprit carotid stenosis awaiting carotid endarterectomy and 8 controls without culprit carotid atheroma. We compared standardized uptake values in the clinically adjudicated culprit to the contralateral asymptomatic artery, and assessed the relationship between radiotracer uptake and plaque phenotype or predicted cardiovascular risk (ASSIGN score [Assessing Cardiovascular Risk Using SIGN Guidelines to Assign Preventive Treatment]). We also performed micro PET/CT and histological analysis of excised plaque. On histological and micro PET/CT analysis, $^{18}$F-fluoride selectively highlighted microcalcification. Carotid $^{18}$F-fluoride uptake was increased in clinically adjudicated culprit plaques compared with asymptomatic contralateral plaques (log$_{10}$ standardized uptake value$_{mean}$ 0.29±0.10 versus 0.23±0.11, P=0.001) and compared with control patients (log$_{10}$ standardized uptake value$_{mean}$ 0.29±0.10 versus 0.12±0.11, P=0.001). $^{18}$F-Fluoride uptake correlated with high-risk plaque features (remodeling index [r=0.53, P=0.003], plaque burden [r=0.51, P=0.004]), and predicted cardiovascular risk [r=0.65, P=0.002]). Carotid $^{18}$F-fluorodeoxyglucose uptake appeared to be increased in 7 of 16 culprit plaques, but no overall differences in uptake were observed in culprit versus contralateral plaques or control patients. However, $^{18}$F-fluorodeoxyglucose did correlate with predicted cardiovascular risk (r=0.53, P=0.019), but not with plaque phenotype. CONCLUSIONS: $^{18}$F-Fluoride PET/CT highlights culprit and phenotypically high-risk carotid plaque. This has the potential to improve risk stratification and selection of patients who may benefit from intervention.
Published: 2017
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11. Smooth Muscle Endothelin B Receptors Regulate Blood Pressure but Not Vascular Function or Neointimal Remodeling

Author: Miller, E, Czopek, A, Duthie, KM, Kirkby, NS, van de Putte, EEF, Christen, S, Kimmitt, RA, Moorhouse, R, Castellan, RFP, Kotelevtsev, YV, Kuc, RE, Davenport, AP, Dhaun, N, Webb, DJ, Hadoke, PWF, Davenport, Anthony [0000-0002-2096-3117], and Apollo - University of Cambridge Repository
Subjects: EXPRESSION, Science & Technology, BALLOON ANGIOPLASTY, NITRIC-OXIDE, hypertension, RADIOLIGAND BINDING, 1103 Clinical Sciences, respiratory system, neointima, musculoskeletal system, 1102 Cardiovascular Medicine And Haematology, autoradiography, Peripheral Vascular Disease, ORGAN-CULTURE, Cardiovascular System & Hematology, CELLS, endothelin-1, cardiovascular system, Cardiovascular System & Cardiology, ET(B) RECEPTORS, vasoconstriction, CAROTID-ARTERY, Life Sciences & Biomedicine, KNOCKOUT MICE, circulatory and respiratory physiology
Abstract: The role of smooth muscle endothelin$_{B}$ (ET$_{B}$) receptors in regulating vascular function, blood pressure (BP), and neointimal remodeling has not been established. Selective knockout mice were generated to address the hypothesis that loss of smooth muscle ET$_{B}$ receptors would reduce BP, alter vascular contractility, and inhibit neointimal remodeling. ET$_{B}$ receptors were selectively deleted from smooth muscle by crossing floxed ET$_{B}$ mice with those expressing cre-recombinase controlled by the transgelin promoter. Functional consequences of ET$_{B}$ deletion were assessed using myography. BP was measured by telemetry, and neointimal lesion formation induced by femoral artery injury. Lesion size and composition (day 28) were analyzed using optical projection tomography, histology, and immunohistochemistry. Selective deletion of ET$_{B}$ was confirmed by genotyping, autoradiography, polymerase chain reaction, and immunohistochemistry. ET$_{B}$-mediated contraction was reduced in trachea, but abolished from mesenteric veins, of knockout mice. Induction of ET$_{B}$-mediated contraction in mesenteric arteries was also abolished in these mice. Femoral artery function was unaltered, and baseline BP modestly elevated in smooth muscle ET$_{B}$ knockout compared with controls (+4.2±0.2 mm Hg; $\textit{P}$
Published: 2017
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12. IUPHAR-DB: updated database content and new features

Author: Sharman JL Benson HE Pawson AJ Lukito V Mpamhanga CP Bombail V Davenport AP Peters JA Speddi
Abstract: The International Union of Basic and Clinical Pharmacology (IUPHAR) database IUPHAR DB (http://www.iuphar db.org) is an open access online database providing detailed expert driven annotation of the primary literature on human and rodent receptors and other drug targets together with the substances that act on them. The present release includes information on the products of 646 genes from four major protein classes (G protein coupled receptors nuclear hormone receptors voltage and ligand gated ion channels) and ~3180 bioactive molecules (endogenous ligands licensed drugs and key pharmacological tools) that interact with them. We have described previously the classification and curation of data for small molecule ligands in the database; in this update we have annotated 366 endogenous peptide ligands with their amino acid sequences post translational modifications links to precursor genes species differences and relationships with other molecules in the database (e.g. those derived from the same precursor). We have also matched targets with their endogenous ligands (peptides and small molecules) with particular attention paid to identifying bioactive peptide ligands generated by post translational modification of precursor proteins. Other improvements to the database include enhanced information on the clinical relevance of targets and ligands in the database more extensive links to other databases and a pilot project for the curation of enzymes as drug targets
Published: 2013

13. THE CONCISE GUIDE TO PHARMACOLOGY 2017/18: Overview.

Author: Alexander, SP, Kelly, E, Marrion, NV, Peters, JA, Faccenda, E, Harding, SD, Pawson, AJ, Sharman, JL, Southan, C, Buneman, OP, Cidlowski, JA, Christopoulos, A, Davenport, AP, Fabbro, D, Spedding, M, Striessnig, J, Davies, JA, CGTP Collaborators, Alexander, SP, Kelly, E, Marrion, NV, Peters, JA, Faccenda, E, Harding, SD, Pawson, AJ, Sharman, JL, Southan, C, Buneman, OP, Cidlowski, JA, Christopoulos, A, Davenport, AP, Fabbro, D, Spedding, M, Striessnig, J, Davies, JA, and CGTP Collaborators
Abstract: The Concise Guide to PHARMACOLOGY 2017/18 is the third in this series of biennial publications. This version provides concise overviews of the key properties of nearly 1800 human drug targets with an emphasis on selective pharmacology (where available), plus links to an open access knowledgebase of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. Although the Concise Guide represents approximately 400 pages, the material presented is substantially reduced compared to information and links presented on the website. It provides a permanent, citable, point-in-time record that will survive database updates. The full contents of this section can be found at http://onlinelibrary.wiley.com/doi/10.1111/bph.13882/full. In addition to this overview, in which are identified 'Other protein targets' which fall outside of the subsequent categorisation, there are eight areas of focus: G protein-coupled receptors, ligand-gated ion channels, voltage-gated ion channels, other ion channels, nuclear hormone receptors, catalytic receptors, enzymes and transporters. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. The landscape format of the Concise Guide is designed to facilitate comparison of related targets from material contemporary to mid-2017, and supersedes data presented in the 2015/16 and 2013/14 Concise Guides and previous Guides to Receptors and Channels. It is produced in close conjunction with the Nomenclature Committee of the Union of Basic and Clinical Pharmacology (NC-IUPHAR), therefore, providing official IUPHAR classification and nomenclature for human drug targets, where appropriate.
Published: 2017

14. Chemerin Elicits Potent Constrictor Actions via Chemokine-Like Receptor 1 (CMKLR1), not G-Protein-Coupled Receptor 1 (GPR1), in Human and Rat Vasculature

Author: Kennedy, AJ, Yang, P, Read, C, Kuc, RE, Yang, L, Taylor, EJA, Taylor, CW, Maguire, JJ, Davenport, AP, Taylor, Colin [0000-0001-7771-1044], Maguire, Janet [0000-0002-9254-7040], Davenport, Anthony [0000-0002-2096-3117], and Apollo - University of Cambridge Repository
Subjects: radioligand binding, G‐protein‐coupled receptors, blood pressure, contraction, antagonist, human, agonist, chemerin, metabolic syndrome
Abstract: BACKGROUND: Circulating levels of chemerin are significantly higher in hypertensive patients and positively correlate with blood pressure. Chemerin activates chemokine-like receptor 1 (CMKLR1 or ChemR23) and is proposed to activate the "orphan" G-protein-coupled receptor 1 (GPR1), which has been linked with hypertension. Our aim was to localize chemerin, CMKLR1, and GPR1 in the human vasculature and determine whether 1 or both of these receptors mediate vasoconstriction. METHODS AND RESULTS: Using immunohistochemistry and molecular biology in conduit arteries and veins and resistance vessels, we localized chemerin to endothelium, smooth muscle, and adventitia and found that CMKLR1 and GPR1 were widely expressed in smooth muscle. C9 (chemerin149-157) contracted human saphenous vein (pD2=7.30±0.31) and resistance arteries (pD2=7.05±0.54) and increased blood pressure in rats by 9.1±1.0 mm Hg at 200 nmol. Crucially, these in vitro and in vivo vascular actions were blocked by CCX832, which we confirmed to be highly selective for CMKLR1 over GPR1. C9 inhibited cAMP accumulation in human aortic smooth muscle cells and preconstricted rat aorta, consistent with the observed vasoconstrictor action. Downstream signaling was explored further and, compared to chemerin, C9 showed a bias factor=≈5000 for the Gi protein pathway, suggesting that CMKLR1 exhibits biased agonism. CONCLUSIONS: Our data suggest that chemerin acts at CMKLR1, but not GPR1, to increase blood pressure. Chemerin has an established detrimental role in metabolic syndrome, and these direct vascular actions may contribute to hypertension, an additional risk factor for cardiovascular disease. This study provides proof of principle for the therapeutic potential of selective CMKLR1 antagonists.
Published: 2016

15. The Concise Guide to PHARMACOLOGY 2015/16: Overview

Author: Alexander, SP, Kelly, E, Marrion, N, Peters, JA, Benson, HE, Faccenda, E, Pawson, AJ, Sharman, JL, Southan, C, Buneman, OP, Catterall, WA, Cidlowski, JA, Davenport, AP, Fabbro, D, Fan, G, McGrath, JC, Spedding, M, Davies, JA, CGTP Collaborators, Davenport, Anthony [0000-0002-2096-3117], and Apollo - University of Cambridge Repository
Subjects: Pharmacology, Databases, Pharmaceutical, Animals, Humans
Abstract: The Concise Guide to PHARMACOLOGY 2015/16 provides concise overviews of the key properties of over 1750 human drug targets with their pharmacology, plus links to an open access knowledgebase of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. The full contents can be found at http://onlinelibrary.wiley.com/doi/10.1111/bph.13347/full. This compilation of the major pharmacological targets is divided into eight areas of focus: G protein-coupled receptors, ligand-gated ion channels, voltage-gated ion channels, other ion channels, nuclear hormone receptors, catalytic receptors, enzymes and transporters. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. The Concise Guide is published in landscape format in order to facilitate comparison of related targets. It is a condensed version of material contemporary to late 2015, which is presented in greater detail and constantly updated on the website www.guidetopharmacology.org, superseding data presented in the previous Guides to Receptors & Channels and the Concise Guide to PHARMACOLOGY 2013/14. It is produced in conjunction with NC-IUPHAR and provides the official IUPHAR classification and nomenclature for human drug targets, where appropriate. It consolidates information previously curated and displayed separately in IUPHAR-DB and GRAC and provides a permanent, citable, point-in-time record that will survive database updates.
Published: 2015

16. Vascular Imaging With 18F-Fluorodeoxyglucose Positron Emission Tomography Is Influenced by Hypoxia

Author: Joshi, FR, Manavaki, R, Fryer, TD, Figg, NL, Sluimer, JC, Aigbirhio, FI, Davenport, AP, Kirkpatrick, PJ, Warburton, EA, Rudd, JHF, Pathologie, RS: CARIM - R3.06 - The vulnerable plaque: makers and markers, Manavaki, Roido [0000-0002-4384-6626], Aigbirhio, Franklin [0000-0001-9453-5257], Davenport, Anthony [0000-0002-2096-3117], Rudd, James [0000-0003-2243-3117], and Apollo - University of Cambridge Repository
Subjects: Carotid Artery Diseases, Male, Plaque, Atherosclerotic, Stroke, Carotid Arteries, INFLAMMATION, Fluorodeoxyglucose F18, Positron-Emission Tomography, Humans, Female, Letters, MACROPHAGES, Radiopharmaceuticals, Hypoxia, ATHEROSCLEROTIC PLAQUES, Aged
Published: 2017

17. The Concise Guide to PHARMACOLOGY 2013/14: overview

Author: Alexander, SP, Benson, HE, Faccenda, E, Pawson, AJ, Sharman, JL, McGrath, JC, Catterall, WA, Spedding, M, Peters, JA, Harmar, AJ, CGTP Collaborators, Abul-Hasn, N, Anderson, CM, Araiksinen, MS, Arita, M, Arthofer, E, Barker, EL, Barratt, C, Barnes, NM, Bathgate, R, Beart, PM, Belelli, D, Bennett, AJ, Birdsall, NJ, Boison, D, Bonner, TI, Brailsford, L, Bröer, S, Brown, P, Calo, G, Carter, WG, Chan, SL, Chao, MV, Chiang, N, Christopoulos, A, Chun, JJ, Cidlowski, J, Clapham, DE, Cockcroft, S, Connor, MA, Cox, HM, Cuthbert, A, Dautzenberg, FM, Davenport, AP, Dawson, PA, Dent, G, Dijksterhuis, JP, Dollery, CT, Dolphin, AC, Donowitz, M, Dubocovich, ML, Eiden, L, Eidne, K, Evans, BA, Fabbro, D, Fahlke, C, Farndale, R, Fitzgerald, GA, Fong, TM, Fowler, CJ, Fry, JR, Funk, CD, Futerman, AH, Ganapathy, V, Gaisnier, B, Gershengorn, MA, Goldin, A, Goldman, ID, Gundlach, AL, Hagenbuch, B, Hales, TG, Hammond, JR, Hamon, M, Hancox, JC, Hauger, RL, Hay, DL, Hobbs, AJ, Hollenberg, MD, Holliday, ND, Hoyer, D, Hynes, NA, Inui, KI, Ishii, S, Jacobson, KA, Jarvis, GE, Jarvis, MF, Jensen, R, Jones, CE, Jones, RL, Kaibuchi, K, Kanai, Y, Kennedy, C, Kerr, ID, Khan, AA, Klienz, MJ, Kukkonen, JP, Lapoint, JY, Leurs, R, Lingueglia, E, Lippiat, J, Lolait, SJ, Lummis, SC, Lynch, JW, MacEwan, D, Maguire, JJ, Marshall, IL, May, JM, McArdle, CA, Michel, MC, Millar, NS, Miller, LJ, Mitolo, V, Monk, PN, Moore, PK, Moorhouse, AJ, Mouillac, B, Murphy, PM, Neubig, RR, Neumaier, J, Niesler, B, Obaidat, A, Offermanns, S, Ohlstein, E, Panaro, MA, Parsons, S, Pwrtwee, RG, Petersen, J, Pin, JP, Poyner, DR, Prigent, S, Prossnitz, ER, Pyne, NJ, Pyne, S, Quigley, JG, Ramachandran, R, Richelson, EL, Roberts, RE, Roskoski, R, Ross, RA, Roth, M, Rudnick, G, Ryan, RM, Said, SI, Schild, L, Sanger, GJ, Scholich, K, Schousboe, A, Schulte, G, Schulz, S, Serhan, CN, Sexton, PM, Sibley, DR, Siegel, JM, Singh, G, Sitsapesan, R, Smart, TG, Smith, DM, Soga, T, Stahl, A, Stewart, G, Stoddart, LA, Summers, RJ, Thorens, B, Thwaites, DT, Toll, L, Traynor, JR, Usdin, TB, Vandenberg, RJ, Villalon, C, Vore, M, Waldman, SA, Ward, DT, Willars, GB, Wonnacott, SJ, Wright, E, Ye, RD, Yonezawa, A, and Zimmermann, M
Abstract: The Concise Guide to PHARMACOLOGY 2013/14 provides concise overviews of the key properties of over 2000 human drug targets with their pharmacology, plus links to an open access knowledgebase of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties from the IUPHAR database. The full contents can be found at http://onlinelibrary.wiley.com/doi/10.1111/bph.12444/full. This compilation of the major pharmacological targets is divided into seven areas of focus: G protein-coupled receptors, ligand-gated ion channels, ion channels, catalytic receptors, nuclear hormone receptors, transporters and enzymes. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. A new landscape format has easy to use tables comparing related targets. It is a condensed version of material contemporary to late 2013, which is presented in greater detail and constantly updated on the website www.guidetopharmacology.org, superseding data presented in previous Guides to Receptors & Channels. It is produced in conjunction with NC-IUPHAR and provides the official IUPHAR classification and nomenclature for human drug targets, where appropriate. It consolidates information previously curated and displayed separately in IUPHAR-DB and GRAC and provides a permanent, citable, point-in-time record that will survive database updates.
Published: 2013

18. THE CONCISE GUIDE TO PHARMACOLOGY 2015/16: Overview

Author: Alexander, SPH, Kelly, E, Marrion, N, Peters, JA, Benson, HE, Faccenda, E, Pawson, AJ, Sharman, JL, Southan, C, Buneman, OP, Catterall, WA, Cidlowski, JA, Davenport, AP, Fabbro, D, Fan, G, McGrath, JC, Spedding, M, Davies, JA, Aldrich, R, Attali, B, Back, M, Barnes, NM, Bathgate, R, Beart, PM, Becirovic, E, Biel, M, Birdsall, NJ, Boison, D, Brauner-Osborne, H, Broeer, S, Bryant, C, Burnstock, G, Burris, T, Cain, D, Calo, G, Chan, SL, Chandy, KG, Chiang, N, Christakos, S, Christopoulos, A, Chun, JJ, Chung, J-J, Clapham, DE, Connor, MA, Coons, L, Cox, HM, Dautzenberg, FM, Dent, G, Douglas, SD, Dubocovich, ML, Edwards, DP, Farndale, R, Fong, TM, Forrest, D, Fowler, CJ, Fuller, P, Gainetdinov, RR, Gershengorn, MA, Goldin, A, Goldstein, SAN, Grimm, SL, Grissmer, S, Gundlach, AL, Hagenbuch, B, Hammond, JR, Hancox, JC, Hartig, S, Hauger, RL, Hay, DL, Hebert, T, Hollenberg, AN, Holliday, ND, Hoyer, D, Ijzerman, AP, Inui, KI, Ishii, S, Jacobson, KA, Jan, LY, Jarvis, GE, Jensen, R, Jetten, A, Jockers, R, Kaczmarek, LK, Kanai, Y, Kang, HS, Karnik, S, Kerr, ID, Korach, KS, Lange, CA, Larhammar, D, Leeb-Lundberg, F, Leurs, R, Lolait, SJ, Macewan, D, Maguire, JJ, May, JM, Mazella, J, McArdle, CA, McDonnell, DP, Michel, MC, Miller, LJ, Mitolo, V, Monie, T, Monk, PN, Mouillac, B, Murphy, PM, Nahon, J-L, Nerbonne, J, Nichols, CG, Norel, X, Oakley, R, Offermanns, S, Palmer, LG, Panaro, MA, Perez-Reyes, E, Pertwee, RG, Pike, JW, Pin, JP, Pintor, S, Plant, LD, Poyner, DR, Prossnitz, ER, Pyne, S, Ren, D, Richer, JK, Rondard, P, Ross, RA, Sackin, H, Safi, R, Sanguinetti, MC, Sartorius, CA, Segaloff, DL, Sladek, FM, Stewart, G, Stoddart, LA, Striessnig, J, Summers, RJ, Takeda, Y, Tetel, M, Toll, L, Trimmer, JS, Tsai, M-J, Tsai, SY, Tucker, S, Usdin, TB, Vilargada, J-P, Vore, M, Ward, DT, Waxman, SG, Webb, P, Wei, AD, Weigel, N, Willars, GB, Winrow, C, Wong, SS, Wulff, H, Ye, RD, Young, M, Zajac, J-M, Alexander, SPH, Kelly, E, Marrion, N, Peters, JA, Benson, HE, Faccenda, E, Pawson, AJ, Sharman, JL, Southan, C, Buneman, OP, Catterall, WA, Cidlowski, JA, Davenport, AP, Fabbro, D, Fan, G, McGrath, JC, Spedding, M, Davies, JA, Aldrich, R, Attali, B, Back, M, Barnes, NM, Bathgate, R, Beart, PM, Becirovic, E, Biel, M, Birdsall, NJ, Boison, D, Brauner-Osborne, H, Broeer, S, Bryant, C, Burnstock, G, Burris, T, Cain, D, Calo, G, Chan, SL, Chandy, KG, Chiang, N, Christakos, S, Christopoulos, A, Chun, JJ, Chung, J-J, Clapham, DE, Connor, MA, Coons, L, Cox, HM, Dautzenberg, FM, Dent, G, Douglas, SD, Dubocovich, ML, Edwards, DP, Farndale, R, Fong, TM, Forrest, D, Fowler, CJ, Fuller, P, Gainetdinov, RR, Gershengorn, MA, Goldin, A, Goldstein, SAN, Grimm, SL, Grissmer, S, Gundlach, AL, Hagenbuch, B, Hammond, JR, Hancox, JC, Hartig, S, Hauger, RL, Hay, DL, Hebert, T, Hollenberg, AN, Holliday, ND, Hoyer, D, Ijzerman, AP, Inui, KI, Ishii, S, Jacobson, KA, Jan, LY, Jarvis, GE, Jensen, R, Jetten, A, Jockers, R, Kaczmarek, LK, Kanai, Y, Kang, HS, Karnik, S, Kerr, ID, Korach, KS, Lange, CA, Larhammar, D, Leeb-Lundberg, F, Leurs, R, Lolait, SJ, Macewan, D, Maguire, JJ, May, JM, Mazella, J, McArdle, CA, McDonnell, DP, Michel, MC, Miller, LJ, Mitolo, V, Monie, T, Monk, PN, Mouillac, B, Murphy, PM, Nahon, J-L, Nerbonne, J, Nichols, CG, Norel, X, Oakley, R, Offermanns, S, Palmer, LG, Panaro, MA, Perez-Reyes, E, Pertwee, RG, Pike, JW, Pin, JP, Pintor, S, Plant, LD, Poyner, DR, Prossnitz, ER, Pyne, S, Ren, D, Richer, JK, Rondard, P, Ross, RA, Sackin, H, Safi, R, Sanguinetti, MC, Sartorius, CA, Segaloff, DL, Sladek, FM, Stewart, G, Stoddart, LA, Striessnig, J, Summers, RJ, Takeda, Y, Tetel, M, Toll, L, Trimmer, JS, Tsai, M-J, Tsai, SY, Tucker, S, Usdin, TB, Vilargada, J-P, Vore, M, Ward, DT, Waxman, SG, Webb, P, Wei, AD, Weigel, N, Willars, GB, Winrow, C, Wong, SS, Wulff, H, Ye, RD, Young, M, and Zajac, J-M
Abstract: The Concise Guide to PHARMACOLOGY 2015/16 provides concise overviews of the key properties of over 1750 human drug targets with their pharmacology, plus links to an open access knowledgebase of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. The full contents can be found at http://onlinelibrary.wiley.com/doi/10.1111/bph.13347/full. This compilation of the major pharmacological targets is divided into eight areas of focus: G protein-coupled receptors, ligand-gated ion channels, voltage-gated ion channels, other ion channels, nuclear hormone receptors, catalytic receptors, enzymes and transporters. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. The Concise Guide is published in landscape format in order to facilitate comparison of related targets. It is a condensed version of material contemporary to late 2015, which is presented in greater detail and constantly updated on the website www.guidetopharmacology.org, superseding data presented in the previous Guides to Receptors & Channels and the Concise Guide to PHARMACOLOGY 2013/14. It is produced in conjunction with NC-IUPHAR and provides the official IUPHAR classification and nomenclature for human drug targets, where appropriate. It consolidates information previously curated and displayed separately in IUPHAR-DB and GRAC and provides a permanent, citable, point-in-time record that will survive database updates.
Published: 2015

19. THE CONCISE GUIDE TO PHARMACOLOGY 2015/16: G protein-coupled receptors

Author: Alexander, SPH, Davenport, AP, Kelly, E, Marrion, N, Peters, JA, Benson, HE, Faccenda, E, Pawson, AJ, Sharman, JL, Southan, C, Davies, JA, Aldrich, R, Attali, B, Back, M, Barnes, NM, Bathgate, R, Beart, PM, Becirovic, E, Biel, M, Birdsall, NJ, Boison, D, Brauner-Osborne, H, Broeer, S, Bryant, C, Burnstock, G, Burris, T, Cain, D, Calo, G, Chan, SL, Chandy, KG, Chiang, N, Christakos, S, Christopoulos, A, Chun, JJ, Chung, J-J, Clapham, DE, Connor, MA, Coons, L, Cox, HM, Dautzenberg, FM, Dent, G, Douglas, SD, Dubocovich, ML, Edwards, DP, Farndale, R, Fong, TM, Forrest, D, Fowler, CJ, Fuller, P, Gainetdinov, RR, Gershengorn, MA, Goldin, A, Goldstein, SAN, Grimm, SL, Grissmer, S, Gundlach, AL, Hagenbuch, B, Hammond, JR, Hancox, JC, Hartig, S, Hauger, RL, Hay, DL, Hebert, T, Hollenberg, AN, Holliday, ND, Hoyer, D, Ijzerman, AP, Inui, KI, Ishii, S, Jacobson, KA, Jan, LY, Jarvis, GE, Jensen, R, Jetten, A, Jockers, R, Kaczmarek, LK, Kanai, Y, Kang, HS, Karnik, S, Kerr, ID, Korach, KS, Lange, CA, Larhammar, D, Leeb-Lundberg, F, Leurs, R, Lolait, SJ, Macewan, D, Maguire, JJ, May, JM, Mazella, J, McArdle, CA, McDonnell, DP, Michel, MC, Miller, LJ, Mitolo, V, Monie, T, Monk, PN, Mouillac, B, Murphy, PM, Nahon, J-L, Nerbonne, J, Nichols, CG, Norel, X, Oakley, R, Offermanns, S, Palmer, LG, Panaro, MA, Perez-Reyes, E, Pertwee, RG, Pike, JW, Pin, JP, Pintor, S, Plant, LD, Poyner, DR, Prossnitz, ER, Pyne, S, Ren, D, Richer, JK, Rondard, P, Ross, RA, Sackin, H, Safi, R, Sanguinetti, MC, Sartorius, CA, Segaloff, DL, Sladek, FM, Stewart, G, Stoddart, LA, Striessnig, J, Summers, RJ, Takeda, Y, Tetel, M, Toll, L, Trimmer, JS, Tsai, M-J, Tsai, SY, Tucker, S, Usdin, TB, Vilargada, J-P, Vore, M, Ward, DT, Waxman, SG, Webb, P, Wei, AD, Weigel, N, Willars, GB, Winrow, C, Wong, SS, Wulff, H, Ye, RD, Young, M, Zajac, J-M, Alexander, SPH, Davenport, AP, Kelly, E, Marrion, N, Peters, JA, Benson, HE, Faccenda, E, Pawson, AJ, Sharman, JL, Southan, C, Davies, JA, Aldrich, R, Attali, B, Back, M, Barnes, NM, Bathgate, R, Beart, PM, Becirovic, E, Biel, M, Birdsall, NJ, Boison, D, Brauner-Osborne, H, Broeer, S, Bryant, C, Burnstock, G, Burris, T, Cain, D, Calo, G, Chan, SL, Chandy, KG, Chiang, N, Christakos, S, Christopoulos, A, Chun, JJ, Chung, J-J, Clapham, DE, Connor, MA, Coons, L, Cox, HM, Dautzenberg, FM, Dent, G, Douglas, SD, Dubocovich, ML, Edwards, DP, Farndale, R, Fong, TM, Forrest, D, Fowler, CJ, Fuller, P, Gainetdinov, RR, Gershengorn, MA, Goldin, A, Goldstein, SAN, Grimm, SL, Grissmer, S, Gundlach, AL, Hagenbuch, B, Hammond, JR, Hancox, JC, Hartig, S, Hauger, RL, Hay, DL, Hebert, T, Hollenberg, AN, Holliday, ND, Hoyer, D, Ijzerman, AP, Inui, KI, Ishii, S, Jacobson, KA, Jan, LY, Jarvis, GE, Jensen, R, Jetten, A, Jockers, R, Kaczmarek, LK, Kanai, Y, Kang, HS, Karnik, S, Kerr, ID, Korach, KS, Lange, CA, Larhammar, D, Leeb-Lundberg, F, Leurs, R, Lolait, SJ, Macewan, D, Maguire, JJ, May, JM, Mazella, J, McArdle, CA, McDonnell, DP, Michel, MC, Miller, LJ, Mitolo, V, Monie, T, Monk, PN, Mouillac, B, Murphy, PM, Nahon, J-L, Nerbonne, J, Nichols, CG, Norel, X, Oakley, R, Offermanns, S, Palmer, LG, Panaro, MA, Perez-Reyes, E, Pertwee, RG, Pike, JW, Pin, JP, Pintor, S, Plant, LD, Poyner, DR, Prossnitz, ER, Pyne, S, Ren, D, Richer, JK, Rondard, P, Ross, RA, Sackin, H, Safi, R, Sanguinetti, MC, Sartorius, CA, Segaloff, DL, Sladek, FM, Stewart, G, Stoddart, LA, Striessnig, J, Summers, RJ, Takeda, Y, Tetel, M, Toll, L, Trimmer, JS, Tsai, M-J, Tsai, SY, Tucker, S, Usdin, TB, Vilargada, J-P, Vore, M, Ward, DT, Waxman, SG, Webb, P, Wei, AD, Weigel, N, Willars, GB, Winrow, C, Wong, SS, Wulff, H, Ye, RD, Young, M, and Zajac, J-M
Abstract: The Concise Guide to PHARMACOLOGY 2015/16 provides concise overviews of the key properties of over 1750 human drug targets with their pharmacology, plus links to an open access knowledgebase of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. The full contents can be found at http://onlinelibrary.wiley.com/doi/10.1111/bph.13348/full. G protein-coupled receptors are one of the eight major pharmacological targets into which the Guide is divided, with the others being: ligand-gated ion channels, voltage-gated ion channels, other ion channels, nuclear hormone receptors, catalytic receptors, enzymes and transporters. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. The Concise Guide is published in landscape format in order to facilitate comparison of related targets. It is a condensed version of material contemporary to late 2015, which is presented in greater detail and constantly updated on the website www.guidetopharmacology.org, superseding data presented in the previous Guides to Receptors & Channels and the Concise Guide to PHARMACOLOGY 2013/14. It is produced in conjunction with NC-IUPHAR and provides the official IUPHAR classification and nomenclature for human drug targets, where appropriate. It consolidates information previously curated and displayed separately in IUPHAR-DB and GRAC and provides a permanent, citable, point-in-time record that will survive database updates.
Published: 2015

20. Chemokine receptor CCR5: from AIDS to atherosclerosis

Author: Jones, KL, Maguire, JJ, and Davenport, AP
Subjects: Acquired Immunodeficiency Syndrome, Receptors, CCR5, CCR5 Receptor Antagonists, virus diseases, Reviews, Animals, Humans, Chemokines, Atherosclerosis
Abstract: There is increasing recognition of an important contribution of chemokines and their receptors in the pathology of atherosclerosis and related cardiovascular disease. The chemokine receptor CCR5 was initially known for its role as a co-receptor for HIV infection of macrophages and is the target of the recently approved CCR5 antagonist maraviroc. However, evidence is now emerging supporting a role for CCR5 and its ligands CCL3 (MIP-1α), CCL4 (MIP-1β) and CCL5 (RANTES) in the initiation and progression of atherosclerosis. Specifically, the CCR5 deletion polymorphism CCR5delta32, which confers resistance to HIV infection, has been associated with a reduced risk of cardiovascular disease and both CCR5 antagonism and gene deletion reduce atherosclerosis in mouse models of the disease. Antagonism of CCL5 has also been shown to reduce atherosclerotic burden in these animal models. Crucially, CCR5 and its ligands CCL3, CCL4 and CCL5 have been identified in human and mouse vasculature and have been detected in human atherosclerotic plaque. Not unexpectedly, CC chemokines have also been linked to saphenous vein graft disease, which shares similarity to native vessel atherosclerosis. Distinct roles for chemokine-receptor systems in atherogenesis have been proposed, with CCR5 likely to be critical in recruitment of monocytes to developing plaques. With an increased burden of cardiovascular disease observed in HIV-infected individuals, the potential cardiovascular-protective effects of drugs that target the CCR5 receptor warrant greater attention. The availability of clinically validated antagonists such as maraviroc currently provides an advantage for targeting of CCR5 over other chemokine receptors.
Published: 2011

21. 12 Pharmacology of Human ETA and ETB Receptor Signalling VIA G-Protein and Beta-Arrestin Pathways

Author: Maguire, JJ, primary, Kuc, RE, additional, Pell, VR, additional, and Davenport, AP, additional
Published: 2012
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22. 09 Biomarkers for Detection of Activated Macrophages in Atherosclerosis

Author: Bird, JLE, primary, Burzynski, L, additional, Manavaki, R, additional, Rudd, JHF, additional, Warburton, EA, additional, and Davenport, AP, additional
Published: 2012
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23. 07 Simultaneous Positron Emission Tomography and Magnetic Resonance Imaging of Receptors Using a Novel Combined Pre-Clinical Micropet/Mr System

Author: Bird, JLE, primary, Hawkes, RC, additional, Manavaki, R, additional, Sawiak, SJ, additional, Williamson, DJ, additional, Aigbirhio, FI, additional, Rudd, JHF, additional, Bennett, M, additional, Gillard, JH, additional, Carpenter, TA, additional, Warburton, EA, additional, and Davenport, AP, additional
Published: 2012
Full Text: View/download PDF

24. Chemokine receptor CCR5: from AIDS to atherosclerosis

Author: Jones, KL, primary, Maguire, JJ, additional, and Davenport, AP, additional
Published: 2011
Full Text: View/download PDF

25. Emerging pharmacology and physiology of neuromedin U and the structurally related peptide neuromedin S

Author: Mitchell, JD, primary, Maguire, JJ, additional, and Davenport, AP, additional
Published: 2009
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26. The haemodynamic effects of iodinated water soluble radiographic contrast media: a review.

Author: Morcos, SK, Dawson, P, Pearson, JD, Jeremy, JY, Davenport, AP, Yates, MS, Tirone, P, Cipolla, P, de Haen, C, Muschick, P, Krause, W, Refsum, H, Emery, CJ, Liss, P, Nygren, A, Haylor, J, Pugh, ND, Karlsson, JO, Morcos, SK, Dawson, P, Pearson, JD, Jeremy, JY, Davenport, AP, Yates, MS, Tirone, P, Cipolla, P, de Haen, C, Muschick, P, Krause, W, Refsum, H, Emery, CJ, Liss, P, Nygren, A, Haylor, J, Pugh, ND, and Karlsson, JO
Published: 1999

27. Validation of mRNA Quantification in Human Kidney by a Novel Fluorescent Nested RT-PCR Method

Author: Karet, FE, primary, Charnock-Jones, DS, primary, Harrison-Woolrych, ML, primary, O'Reilly, GE, primary, Davenport, AP, primary, and Smith, SK, primary
Published: 1994
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28. Characterisation of Immunoreactive Endothelin in Human kidney by RP-HPLC and RIA

Author: Karet, FE, primary, Plumpton, C, additional, and Davenport, AP, additional
Published: 1993
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29. Endothelins in reproduction

Author: Cameron, IT, primary and Davenport, AP, additional
Published: 1992
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30. FDG-PET can distinguish inflamed from non-inflamed plaque in an animal model of atherosclerosis.

Author: Davies JR, Izquierdo-Garcia D, Rudd JH, Figg N, Richards HK, Bird JL, Aigbirhio FI, Davenport AP, Weissberg PL, Fryer TD, Warburton EA, Davies, John R, Izquierdo-Garcia, David, Rudd, James H F, Figg, Nichola, Richards, Hugh K, Bird, Joseph L E, Aigbirhio, Franklin I, Davenport, Anthony P, and Weissberg, Peter L
Abstract: The presence of activated macrophages is an important predictor of atherosclerotic plaque rupture. In this study, our aim was to determine the accuracy of (18)F- fluorodeoxyglucose (FDG) microPET imaging for quantifying aortic wall macrophage content in a rabbit model of atherosclerosis. Rabbits were divided into a control group and two groups post aortic balloon injury: 6 months high-cholesterol diet (HC); and 3 months HC followed by 3 months low-cholesterol diet plus statin (LCS). In vivo and ex vivo microPET, ex vivo well counting and histological quantification of the atherosclerotic aortas were performed for all groups. Macrophage density was greater in the HC group than the LCS group (5.1 +/- 1.4% vs. 0.6 +/- 0.7%, P < 0.001) with a trend towards greater macrophage density in LCS compared to controls (P = 0.08). There was a strong correlation across all groups between macrophage density and standardized uptake value (SUV) derived from ex vivo microPET (r = 0.95, P < 0.001) and well counting (r = 0.96, P < 0.001). Ex vivo FDG SUV was significantly different between the three groups (P < 0.001). However, the correlation between in vivo microPET FDG SUV and macrophage density was insignificant (r = 0.16, P = 0.57) with no statistical differences in FDG SUV seen between the three groups. This study confirms that in an animal model of inflamed and non-inflamed atherosclerosis, significant differences in FDG SUV allow differentiation of highly inflamed atherosclerotic aortas from those stabilized by statin therapy and low cholesterol diet and controls. [ABSTRACT FROM AUTHOR]
Published: 2010
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31. Mitogenic Effects of Vasoactive Peptides on Rat Vascular Smooth Muscle Cells

Author: Weissberg, PL, primary, Witchell, C, additional, Davenport, AP, additional, Hesketh, TR, additional, and Metcalfe, JC, additional
Published: 1991
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32. Pharmacological targeting of apelin impairs glioblastoma growth

Author: Harford-Wright, E, Andre-Gregoire, G, Jacobs, KA, Treps, L, Le Gonidec, S, Leclair, HM, Gonzalez-Diest, S, Roux, Q, Guillonneau, F, Loussouarn, D, Oliver, L, Vallette, FM, Foufelle, F, Valet, P, Davenport, AP, Glen, RC, Bidere, N, and Gavard, J
Subjects: Proteomics, Apelin Receptors, vascular niche, Brain Neoplasms, Cell Survival, Endothelial Cells, antagonist, In Vitro Techniques, Xenograft Model Antitumor Assays, Mass Spectrometry, 3. Good health, Receptors, G-Protein-Coupled, Mice, HEK293 Cells, apelin, APJ, glioblastoma initiating cells, Animals, Humans, Intercellular Signaling Peptides and Proteins, Molecular Targeted Therapy, RNA, Small Interfering, Glioblastoma, Cell Proliferation
Abstract: Glioblastoma are highly aggressive brain tumours that are associated with an extremely poor prognosis. Within these tumours, a subpopulation of highly plastic self-renewing cancer cells exist that retain the ability to expand ex vivo as tumourspheres, induce tumour growth in mice, and have been implicated in radio- and chemo-resistance. Although their identity and fate are regulated by external cues emanating from endothelial cells, the nature of such angiocrine signals remains unknown. Here, we deployed a mass spectrometry proteomic approach to characterise the factors released by brain endothelial cells. We report the identification of the vasoactive peptide apelin as a central regulator for endothelial-mediated maintenance of glioblastoma patient-derived cells with stem-like properties (GSCs). Genetic and pharmacological targeting of apelin cognate receptor APLNR abrogates apelin- and endothelial-mediated expansion of GSCs and suppresses tumour initiation and growth. Functionally, selective competitive antagonists of APLNR were shown to be safe and effective in lengthening the survival of intracranially xenografted mice. Therefore, the APLN/APLNR signalling nexus may operate as a paracrine signal that sustains tumour cell expansion and progression, suggesting that apelin is a druggable factor in glioblastoma.

33. Detection of Atherosclerotic Inflammation by $^{68}$Ga-DOTATATE PET Compared to [$^{18}$F]FDG PET Imaging

Author: Tarkin, JM, Joshi, FR, Evans, NR, Chowdhury, MM, Figg, NL, Shah, AV, Starks, LT, Martin-Garrido, A, Manavaki, R, Yu, E, Kuc, RE, Grassi, L, Kreuzhuber, R, Kostadima, MA, Frontini, M, Kirkpatrick, PJ, Coughlin, PA, Gopalan, D, Fryer, TD, Buscombe, Groves, AM, Ouwehand, WH, Bennett, MR, Warburton, EA, Davenport, AP, and Rudd, JHF
Subjects: somatostatin receptor, positron emission tomography, inflammation, atherosclerosis, molecular imaging, 3. Good health, macrophages
Abstract: $\textbf{Background}$ Inflammation drives atherosclerotic plaque rupture. Although inflammation can be measured using fluorine-18-labeled fluorodeoxyglucose positron emission tomography ([$^{18}$F]FDG PET), [$^{18}$F]FDG lacks cell specificity, and coronary imaging is unreliable because of myocardial spillover. $\textbf{Objectives}$ Objectives This study tested the efficacy of gallium-68-labeled DOTATATE ($^{68}$Ga-DOTATATE), a somatostatin receptor subtype-2 (SST2)-binding PET tracer, for imaging atherosclerotic inflammation. $\textbf{Methods}$ We confirmed $^{68}$Ga-DOTATATE binding in macrophages and excised carotid plaques. $^{68}$Ga-DOTATATE PET imaging was compared to [$^{18}$F]FDG PET imaging in 42 patients with atherosclerosis. $\textbf{Results}$ Target $\textit{SSTR2}$ gene expression occurred exclusively in “proinflammatory” M1 macrophages, specific $^{68}$Ga-DOTATATE ligand binding to SST$_{2}$ receptors occurred in CD68-positive macrophage-rich carotid plaque regions, and carotid $\textit{SSTR2}$ mRNA was highly correlated with in vivo $^{68}$Ga-DOTATATE PET signals (r = 0.89; 95% confidence interval [CI]: 0.28 to 0.99; p = 0.02). $^{68}$Ga-DOTATATE mean of maximum tissue-to-blood ratios (mTBR$_{max}$) correctly identified culprit versus nonculprit arteries in patients with acute coronary syndrome (median difference: 0.69; interquartile range [IQR]: 0.22 to 1.15; p = 0.008) and transient ischemic attack/stroke (median difference: 0.13; IQR: 0.07 to 0.32; p = 0.003). $^{68}$Ga-DOTATATE mTBR$_{max}$ predicted high-risk coronary computed tomography features (receiver operating characteristics area under the curve [ROC AUC]: 0.86; 95% CI: 0.80 to 0.92; p < 0.0001), and correlated with Framingham risk score (r = 0.53; 95% CI: 0.32 to 0.69; p

34. The Concise Guide to PHARMACOLOGY 2015/16: Overview

Author: Alexander, SP, Kelly, E, Marrion, N, Peters, JA, Benson, HE, Faccenda, E, Pawson, AJ, Sharman, JL, Southan, C, Buneman, OP, Catterall, WA, Cidlowski, JA, Davenport, AP, Fabbro, D, Fan, G, McGrath, JC, Spedding, M, Davies, JA, and CGTP Collaborators
Subjects: Pharmacology, Databases, Pharmaceutical, Animals, Humans, 3. Good health
Abstract: The Concise Guide to PHARMACOLOGY 2015/16 provides concise overviews of the key properties of over 1750 human drug targets with their pharmacology, plus links to an open access knowledgebase of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. The full contents can be found at http://onlinelibrary.wiley.com/doi/10.1111/bph.13347/full. This compilation of the major pharmacological targets is divided into eight areas of focus: G protein-coupled receptors, ligand-gated ion channels, voltage-gated ion channels, other ion channels, nuclear hormone receptors, catalytic receptors, enzymes and transporters. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. The Concise Guide is published in landscape format in order to facilitate comparison of related targets. It is a condensed version of material contemporary to late 2015, which is presented in greater detail and constantly updated on the website www.guidetopharmacology.org, superseding data presented in the previous Guides to Receptors & Channels and the Concise Guide to PHARMACOLOGY 2013/14. It is produced in conjunction with NC-IUPHAR and provides the official IUPHAR classification and nomenclature for human drug targets, where appropriate. It consolidates information previously curated and displayed separately in IUPHAR-DB and GRAC and provides a permanent, citable, point-in-time record that will survive database updates.

35. Cardiovascular and renal effects of apelin in chronic kidney disease: a randomised, double-blind, placebo-controlled, crossover study.

Author: Chapman FA, Melville V, Godden E, Morrison B, Bruce L, Maguire JJ, Davenport AP, Newby DE, and Dhaun N
Subjects: Humans, Male, Female, Double-Blind Method, Middle Aged, Adult, Blood Pressure drug effects, Kidney drug effects, Kidney physiopathology, Kidney metabolism, Aged, Vascular Resistance drug effects, Renal Circulation drug effects, Natriuresis drug effects, Hemodynamics drug effects, Cardiac Output drug effects, Renal Insufficiency, Chronic drug therapy, Renal Insufficiency, Chronic physiopathology, Cross-Over Studies, Glomerular Filtration Rate drug effects, Intercellular Signaling Peptides and Proteins, Apelin
Abstract: Chronic kidney disease (CKD) affects ~10% of the population and cardiovascular disease is its commonest complication. Despite treatment, patient outcomes remain poor and newer therapies are urgently needed. Here, we investigated the systemic and renal effects of apelin in CKD. In a randomized, double-blind, placebo-controlled, crossover study, 24 subjects (12 patients with CKD and 12 matched healthy subjects) received pyroglutamated apelin-13 ([Pyr 1 ]apelin-13, 1 nmol/min and 30 nmol/min) or matched placebo on two separate visits. Systemic and renal hemodynamics were monitored throughout. The co-primary endpoints were change in systemic vascular resistance index and renal blood flow. Secondary endpoints were change in blood pressure, cardiac output, pulse wave velocity, glomerular filtration rate, natriuresis, free water clearance and urinary protein excretion. In both health and CKD, 30 nmol/min [Pyr 1 ]apelin-13 reduced mean arterial pressure by ~4%, systemic vascular resistance by ~12%, and increased cardiac index by ~10%, compared to placebo (p < 0.05 for all). Both doses of [Pyr 1 ]apelin-13 increased renal blood flow by ~15%, natriuresis by ~20% and free water clearance by ~10%, compared to placebo (p < 0.05 for all). In patients with chronic kidney disease only, glomerular filtration rate fell by ~10%, effective filtration fraction by ~5% and proteinuria by ~25% (p < 0.01 for all). Apelin has short-term cardiovascular and renal benefits in CKD. If maintained longer-term, these should improve patient outcomes. Clinical trials of long-acting oral apelin agonists are justified in CKD and other conditions with impaired salt and water balance. Registration number at www.clinicalTrials.gov : NCT03956576. Funded by Kidney Research UK., (© 2024. The Author(s).)
Published: 2024
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36. Short communications: Endothelin-1 in cardiac allograft vasculopathy.

Author: Abraham GR, Davenport AP, and Hoole SP
Abstract: Introduction: Cardiac allograft vasculopathy (CAV) is a leading cause of death following heart transplant. Endothelin-1 (ET-1) is a highly potent vasoconstrictor peptide derived from the vascular endothelium with multiple biological actions known to be relevant for CAV. We assessed the trans-myocardial gradient (TMG: coronary sinus minus coronary artery concentration: negative = extraction, positive = secretion) of ET-1 in heart transplant patients to determine correlations with angiographic, Intravascular Ultrasound (IVUS) and Optical Coherence Tomography (OCT) features of CAV., Results: Vessels with more severe CAV demonstrated significantly higher (more positive) ET-1 TMG (IVUS Stanford Grade IV: -0.05 [-0.21, 0.13] pg/ml versus Stanford Grade I-III: -0.31 [-0.64, -0.11] pg/ml, p = 0.01). ET-1 TMG was positively correlated with mean intimal thickness on both IVUS and OCT (IVUS: Kendall's tau-b = 0.254, p = 0.02 and OCT: Kendall's tau-b = 0.344, p < 0.0001). Patients who died had net ET-1 release compared with surviving patients (died: 0.21 [0.19-0.24] versus surviving: -0.28 [-0.52, -0.17], p = 0.01)., Conclusion: In heart transplant patients, coronary arteries with more intimal thickening are associated with a higher (more positive) trans-myocardial gradient of ET-1, suggesting that up-regulated ET-1 release in the coronary circulation may be permissive for the development of CAV., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.)
Published: 2024
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37. Microarray analysis demonstrates up-regulation of the endothelin-1 gene with compensatory down-regulation of the ETA receptor gene in human portal vein.

Author: Owen NE, Williams TL, Maguire JJ, Kuc RE, Davenport EE, and Davenport AP
Subjects: Adult, Female, Humans, Male, Middle Aged, Down-Regulation, Liver Transplantation, Up-Regulation, Endothelin-1 genetics, Endothelin-1 metabolism, Hypertension, Portal genetics, Hypertension, Portal metabolism, Liver Cirrhosis genetics, Liver Cirrhosis metabolism, Liver Cirrhosis pathology, Portal Vein metabolism, Portal Vein pathology, Receptor, Endothelin A genetics, Receptor, Endothelin A metabolism
Abstract: High blood pressure in the portal vein, portal hypertension (PH), is the final common pathway in liver cirrhosis regardless of aetiology. Complications from PH are the major cause of morbidity and mortality in these patients. Current drug therapy to reduce portal pressure is mainly limited to β-adrenergic receptor blockade but approximately 40% of patients do not respond. Our aim was to use microarray to measure the expression of ∼20,800 genes in portal vein from patients with PH undergoing transplantation for liver cirrhosis (PH, n=12) versus healthy vessels (control, n=9) to identify potential drug targets to improve therapy. Expression of 9,964 genes above background was detected in portal vein samples. Comparing PH veins versus control (adjusted P-value < 0.05, fold change > 1.5) identified 548 up-regulated genes and 1,996 down-regulated genes. The 2,544 differentially expressed genes were subjected to pathway analysis. We identified 49 significantly enriched pathways. The endothelin pathway was ranked the tenth most significant, the only vasoconstrictive pathway to be identified. ET-1 gene (EDN1) was significantly up-regulated, consistent with elevated levels of ET-1 peptide previously measured in PH and cirrhosis. ETA receptor gene (EDNRA) was significantly down-regulated, consistent with an adaptive response to increased peptide levels in the portal vein but there was no change in the ETB gene (EDNRB). The results provide further support for evaluating the efficacy of ETA receptor antagonists as a potential therapy in addition to β-blockers in patients with PH and cirrhosis., (© 2024 The Author(s).)
Published: 2024
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38. Co-localization of the sodium-glucose co-transporter-2 channel (SGLT-2) with endothelin ETA and ETB receptors in human cardiorenal tissue.

Author: Williams TL, Kuc RE, Paterson AL, Abraham GR, Pullinger AL, Maguire JJ, Sinha S, Greasley PJ, Ambery P, and Davenport AP
Subjects: Humans, Kidney metabolism, Kidney Tubules, Proximal metabolism, Kidney Tubules, Proximal drug effects, Myocardium metabolism, Sodium-Glucose Transporter 2 Inhibitors pharmacology, Receptor, Endothelin A metabolism, Receptor, Endothelin B metabolism, Sodium-Glucose Transporter 2 metabolism, Sodium-Glucose Transporter 2 genetics
Abstract: Endothelin (ET) receptor antagonists are being investigated in combination with sodium-glucose co-transporter-2 inhibitors (SGLT-2i). These drugs primarily inhibit the SGLT-2 transporter that, in humans, is thought to be mainly restricted to the renal proximal convoluted tubule, resulting in increased glucose excretion favouring improved glycaemic control and diuresis. This action reduces fluid retention with ET receptor antagonists. Studies have suggested SGLT-2 may also be expressed in cardiomyocytes of human heart. To understand the potential of combining the two classes of drugs, our aim was to compare the distribution of ET receptor sub-types in human kidney, with SGLT-2. Secondly, using the same experimental conditions, we determined if SGLT-2 expression could be detected in human heart and whether the transporter co-localised with ET receptors., Methods: Immunocytochemistry localised SGLT-2, ETA and ETB receptors in sections of histologically normal kidney, left ventricle from patients undergoing heart transplantation or controls. Primary antisera were visualised using fluorescent microscopy. Image analysis was used to measure intensity compared with background in adjacent control sections., Results: As expected, SGLT-2 localised to epithelial cells of the proximal convoluted tubules, and co-localised with both ET receptor sub-types. Similarly, ETA receptors predominated in cardiomyocytes; low (compared with kidney but above background) positive staining was also detected for SGLT-2., Discussion: Whether low levels of SGLT-2 have a (patho)physiological role in cardiomyocytes is not known but results suggest the effect of direct blockade of sodium (and glucose) influx via SGLT-2 inhibition in cardiomyocytes should be explored, with potential for additive effects with ETA antagonists., (© 2024 The Author(s).)
Published: 2024
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39. Targeting the endothelium by combining endothelin-1 antagonism and SGLT-2 inhibition: better together?

Author: Ambery P, Greasley PJ, Menzies RI, Brynne L, Kulkarni S, Oscarsson J, and Davenport AP
Subjects: Humans, Animals, Drug Therapy, Combination, Endothelin Receptor Antagonists therapeutic use, Heart Failure drug therapy, Heart Failure physiopathology, Sodium-Glucose Transporter 2 Inhibitors therapeutic use, Sodium-Glucose Transporter 2 Inhibitors pharmacology, Endothelin-1 metabolism, Endothelium, Vascular drug effects, Endothelium, Vascular metabolism
Abstract: Endothelin A and B receptors, together with sodium-glucose cotransporter-2 (SGLT-2) channels are important targets in improving endothelial function and intervention with inhibitors has been the subject of multiple mechanistic and clinical outcome trials over recent years. Notable successes include the treatment of pulmonary hypertension with endothelin receptor antagonists, and the treatment of heart failure and chronic kidney disease with SGLT-2 inhibitors. With distinct and complementary mechanisms, in this review, we explore the logic of combination therapy for a number of diseases which have endothelial dysfunction at their heart., (© 2024 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society.)
Published: 2024
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40. Survivorship in Advanced Lung Cancer: Understanding a New Landscape and Opportunities.

Author: Presley CJ, Dalal N, Davenport AP, Gounden A, Ramchandran K, and Tonorezos E
Subjects: Humans, Cancer Survivors, Neoplasm Staging, Quality of Life, Lung Neoplasms therapy, Survivorship, Palliative Care
Abstract: People with advanced lung cancer represent a distinct group whose needs remain understudied, especially compared with people diagnosed with limited-stage disease. Fortunately, novel treatments such as tyrosine kinase inhibitors and immune checkpoint inhibitors are leading to significant advances in prognosis and survival, even among those with advanced disease at the time of diagnosis. However, there are known gaps in symptom management, psychosocial and nutritional support, complex care coordination, health behavior coaching, and health care delivery efforts among patients living with advanced lung cancer. Many of these patients would benefit from survivorship and palliative care approaches. In particular, survivorship care may include health care maintenance, treatment of immune-related adverse events and late- or long-term effects, frailty assessment and rehabilitation, and care coordination. Palliative care may be best suited to discuss ongoing symptom management, advanced care planning, and end-of-life considerations, as well as psychosocial well-being. To this end, we share a review of the current status of the palliative and survivorship care infrastructure for patients with advanced lung cancer and provide suggestions across the care continuum for this diverse group of patients and families.
Published: 2024
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41. A Retrospective Cohort Study of At-Home Catheter Removal After Urogynecologic Surgery.

Author: Davenport AP, Li YW, Lefbom LT, Iglesia CB, and Dieter AA
Subjects: Humans, Female, Retrospective Studies, Middle Aged, Aged, Gynecologic Surgical Procedures adverse effects, Urinary Catheters adverse effects, Self Care, Device Removal statistics & numerical data, Postoperative Complications epidemiology, Postoperative Complications etiology, Urinary Retention etiology, Urinary Retention epidemiology, Urinary Catheterization adverse effects, Urinary Catheterization statistics & numerical data
Abstract: Importance: In-office postoperative voiding trials (VTs) increase health care burden for patients and physicians. Adoption of an at-home VT option may decrease burden without increasing adverse events postoperatively., Objective: The purpose of this study was to compare 30-day postoperative outcomes between participants who performed an at-home autofill VT after catheter self-discontinuation during the Assessing Healthcare Utilization and Feasibility of Transurethral Catheter Self-discontinuation (FLOTUS) study and a "historic" control cohort of patients who presented to the office for backfill-assisted VT on postoperative day (POD) 1., Study Design: This was a retrospective cohort study of women with postoperative urinary retention after urogynecologic surgery between June 2020 and March 2022. Outcomes from the FLOTUS study were compared with a "historic" control cohort of patients that were identified on chart review from the year before FLOTUS initiation. Demographic, medical history, and procedure-related data were collected. Thirty-day outcome data included office calls/messages, office visits, emergency department visits, complications, and catheterization outcomes., Results: Forty-six participants were included in the FLOTUS cohort and 65 participants in the historic cohort. There was no difference in the POD1 VT pass rate, number of office calls/messages, emergency department visits, or postoperative complications between the 2 cohorts. The FLOTUS patients attended 1 less office visit (1 vs 2 office visits, P <0.001), and this difference persisted on regression analysis (-0.87 office visits; 95% CI, -1.18 to -0.56, P <0.001)., Conclusion: Patients who had backfill-assisted VTs on POD1 attended 1 additional office visit compared with those who removed their catheters at home., Competing Interests: Disclosures: Cheryl B. Iglesia reported the following: Executive Board SGS; Editorial Board Urogynecology and OBG Management; Special Government Employee, US FDA; Chair, NICHD PFDN Advisory Board; Medical Advisory Board for the Patty Brisben Foundation, Healthy Women Foundation, Foundation for Female Health Awareness. The other authors did not report any potential conflicts of interest., (Copyright © 2024 American Urogynecologic Society. All rights reserved.)
Published: 2024
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42. Expression of the apelin receptor, a novel potential therapeutic target, and its endogenous ligands in diverse stem cell populations in human glioblastoma.

Author: Williams TL, Nwokoye P, Kuc RE, Smith K, Paterson AL, Allinson K, Maguire JJ, and Davenport AP
Abstract: Glioblastoma multiforme (GBM) is one of the most common and lethal forms of brain cancer, carrying a very poor prognosis (median survival of ~15 months post-diagnosis). Treatment typically involves invasive surgical resection of the tumour mass, followed by radiotherapy and adjuvant chemotherapy using the alkylating agent temozolomide, but over half of patients do not respond to this drug and considerable resistance is observed. Tumour heterogeneity is the main cause of therapeutic failure, where diverse progenitor glioblastoma stem cell (GSC) lineages in the microenvironment drive tumour recurrence and therapeutic resistance. The apelin receptor is a class A GPCR that binds two endogenous peptide ligands, apelin and ELA, and plays a role in the proliferation and survival of cancer cells. Here, we used quantitative whole slide immunofluorescent imaging of human GBM samples to characterise expression of the apelin receptor and both its ligands in the distinct GSC lineages, namely neural-progenitor-like cells (NPCs), oligodendrocyte-progenitor-like cells (OPCs), and mesenchymal-like cells (MES), as well as reactive astrocytic cells. The data confirm the presence of the apelin receptor as a tractable drug target that is common across the key cell populations driving tumour growth and maintenance, offering a potential novel therapeutic approach for patients with GBM., Competing Interests: The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest., (Copyright © 2024 Williams, Nwokoye, Kuc, Smith, Paterson, Allinson, Maguire and Davenport.)
Published: 2024
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43. The biased apelin receptor agonist, MM07, reverses Sugen/hypoxia-induced pulmonary arterial hypertension as effectively as the endothelin antagonist macitentan.

Author: Williams TL, Nyimanu D, Kuc RE, Foster R, Glen RC, Maguire JJ, and Davenport AP
Abstract: Introduction: Pulmonary arterial hypertension (PAH) is characterised by endothelial dysfunction and pathological vascular remodelling, resulting in the occlusion of pulmonary arteries and arterioles, right ventricular hypertrophy, and eventually fatal heart failure. Targeting the apelin receptor with the novel, G protein-biased peptide agonist, MM07, is hypothesised to reverse the developed symptoms of elevated right ventricular systolic pressure and right ventricular hypertrophy. Here, the effects of MM07 were compared with the clinical standard-of-care endothelin receptor antagonist macitentan. Methods: Male Sprague-Dawley rats were randomised and treated with either normoxia/saline, or Sugen/hypoxia (SuHx) to induce an established model of PAH, before subsequent treatment with either saline, macitentan (30 mg/kg), or MM07 (10 mg/kg). Rats were then anaesthetised and catheterised for haemodynamic measurements, and tissues collected for histopathological assessment. Results: The SuHx/saline group presented with significant increases in right ventricular hypertrophy, right ventricular systolic pressure, and muscularization of pulmonary arteries compared to normoxic/saline controls. Critically, MM07 was as at least as effective as macitentan in significantly reversing detrimental structural and haemodynamic changes after 4 weeks of treatment. Discussion: These results support the development of G protein-biased apelin receptor agonists with improved pharmacokinetic profiles for use in human disease., Competing Interests: The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest., (Copyright © 2024 Williams, Nyimanu, Kuc, Foster, Glen, Maguire and Davenport.)
Published: 2024
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44. The IUPHAR/BPS Guide to PHARMACOLOGY in 2024.

Author: Harding SD, Armstrong JF, Faccenda E, Southan C, Alexander SPH, Davenport AP, Spedding M, and Davies JA
Subjects: Ligands, Databases, Pharmaceutical, Proteins, Drug Discovery
Abstract: The IUPHAR/BPS Guide to PHARMACOLOGY (GtoPdb; https://www.guidetopharmacology.org) is an open-access, expert-curated, online database that provides succinct overviews and key references for pharmacological targets and their recommended experimental ligands. It includes over 3039 protein targets and 12 163 ligand molecules, including approved drugs, small molecules, peptides and antibodies. Here, we report recent developments to the resource and describe expansion in content over the six database releases made during the last two years. The database update section of this paper focuses on two areas relating to important global health challenges. The first, SARS-CoV-2 COVID-19, remains a major concern and we describe our efforts to expand the database to include a new family of coronavirus proteins. The second area is antimicrobial resistance, for which we have extended our coverage of antibacterials in partnership with AntibioticDB, a collaboration that has continued through support from GARDP. We discuss other areas of curation and also focus on our external links to resources such as PubChem that bring important synergies to the resources., (© The Author(s) 2023. Published by Oxford University Press on behalf of Nucleic Acids Research.)
Published: 2024
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45. Targeting the apelin system for the treatment of cardiovascular diseases.

Author: Chapman FA, Maguire JJ, Newby DE, Davenport AP, and Dhaun N
Subjects: Humans, Apelin Receptors metabolism, Heart, Apelin metabolism, Cardiovascular Diseases drug therapy, Cardiovascular Diseases metabolism, Cardiovascular System metabolism
Abstract: Cardiovascular disease is the leading cause of death worldwide. Its prevalence is rising due to ageing populations and the increasing incidence of diseases such as chronic kidney disease, obesity, and diabetes that are associated with elevated cardiovascular risk. Despite currently available treatments, there remains a huge burden of cardiovascular disease-associated morbidity for patients and healthcare systems, and newer treatments are needed. The apelin system, comprising the apelin receptor and its two endogenous ligands apelin and elabela, is a broad regulator of physiology that opposes the actions of the renin-angiotensin and vasopressin systems. Activation of the apelin receptor promotes endothelium-dependent vasodilatation and inotropy, lowers blood pressure, and promotes angiogenesis. The apelin system appears to protect against arrhythmias, inhibits thrombosis, and has broad anti-inflammatory and anti-fibrotic actions. It also promotes aqueous diuresis through direct and indirect (central) effects in the kidney. Thus, the apelin system offers therapeutic promise for a range of cardiovascular, kidney, and metabolic diseases. This review will discuss current cardiovascular disease targets of the apelin system and future clinical utility of apelin receptor agonism., Competing Interests: Conflict of interest: None declared., (© The Author(s) 2023. Published by Oxford University Press on behalf of the European Society of Cardiology.)
Published: 2023
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46. Current and future strategies for targeting the endothelin pathway in cardiovascular disease.

Author: Abraham GR, Williams TL, Maguire JJ, Greasley PJ, Ambery P, and Davenport AP
Subjects: Humans, COVID-19, Animals, Signal Transduction drug effects, Endothelin-1 metabolism, Endothelin-1 antagonists & inhibitors, SARS-CoV-2 drug effects, Endothelins metabolism, Cardiovascular Diseases drug therapy, Cardiovascular Diseases metabolism, Endothelin Receptor Antagonists therapeutic use, Endothelin Receptor Antagonists pharmacology
Abstract: The first endothelin (ET)-1 receptor antagonist was approved for clinical use over 20 years ago, but to date this class of compounds has been limited to treating pulmonary arterial hypertension, a rare disease. Translational research over the last 5 years has reignited interest in the ET system as a therapeutic target across the spectrum of cardiovascular diseases including resistant hypertension, microvascular angina and post-coronavirus disease 2019 conditions. Notable developments include approval of a new ET A receptor antagonist and, intriguingly, combining the actions of ET A and an angiotensin II type 1 receptor antagonist within the same novel small molecule. Combinations of ET receptor blockers with other drugs, including phosphodiesterase-5 inhibitors and sodium-glucose co-transporter-2 antagonists, may drive synergistic benefits with the prospect of alleviating side effects. These new therapeutic strategies have the potential to dramatically widen the scope of indications targeting the ET-1 pathway., (© 2023. Springer Nature Limited.)
Published: 2023
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47. The Concise Guide to PHARMACOLOGY 2023/24: G protein-coupled receptors.

Author: Alexander SPH, Christopoulos A, Davenport AP, Kelly E, Mathie AA, Peters JA, Veale EL, Armstrong JF, Faccenda E, Harding SD, Davies JA, Abbracchio MP, Abraham G, Agoulnik A, Alexander W, Al-Hosaini K, Bäck M, Baker JG, Barnes NM, Bathgate R, Beaulieu JM, Beck-Sickinger AG, Behrens M, Bernstein KE, Bettler B, Birdsall NJM, Blaho V, Boulay F, Bousquet C, Bräuner-Osborne H, Burnstock G, Caló G, Castaño JP, Catt KJ, Ceruti S, Chazot P, Chiang N, Chini B, Chun J, Cianciulli A, Civelli O, Clapp LH, Couture R, Cox HM, Csaba Z, Dahlgren C, Dent G, Douglas SD, Dournaud P, Eguchi S, Escher E, Filardo EJ, Fong T, Fumagalli M, Gainetdinov RR, Garelja ML, de Gasparo M, Gerard C, Gershengorn M, Gobeil F, Goodfriend TL, Goudet C, Grätz L, Gregory KJ, Gundlach AL, Hamann J, Hanson J, Hauger RL, Hay DL, Heinemann A, Herr D, Hollenberg MD, Holliday ND, Horiuchi M, Hoyer D, Hunyady L, Husain A, IJzerman AP, Inagami T, Jacobson KA, Jensen RT, Jockers R, Jonnalagadda D, Karnik S, Kaupmann K, Kemp J, Kennedy C, Kihara Y, Kitazawa T, Kozielewicz P, Kreienkamp HJ, Kukkonen JP, Langenhan T, Larhammar D, Leach K, Lecca D, Lee JD, Leeman SE, Leprince J, Li XX, Lolait SJ, Lupp A, Macrae R, Maguire J, Malfacini D, Mazella J, McArdle CA, Melmed S, Michel MC, Miller LJ, Mitolo V, Mouillac B, Müller CE, Murphy PM, Nahon JL, Ngo T, Norel X, Nyimanu D, O'Carroll AM, Offermanns S, Panaro MA, Parmentier M, Pertwee RG, Pin JP, Prossnitz ER, Quinn M, Ramachandran R, Ray M, Reinscheid RK, Rondard P, Rovati GE, Ruzza C, Sanger GJ, Schöneberg T, Schulte G, Schulz S, Segaloff DL, Serhan CN, Singh KD, Smith CM, Stoddart LA, Sugimoto Y, Summers R, Tan VP, Thal D, Thomas WW, Timmermans PBMWM, Tirupula K, Toll L, Tulipano G, Unal H, Unger T, Valant C, Vanderheyden P, Vaudry D, Vaudry H, Vilardaga JP, Walker CS, Wang JM, Ward DT, Wester HJ, Willars GB, Williams TL, Woodruff TM, Yao C, and Ye RD
Subjects: Humans, Ligands, Ion Channels chemistry, Receptors, Cytoplasmic and Nuclear, Databases, Pharmaceutical, Receptors, G-Protein-Coupled
Abstract: The Concise Guide to PHARMACOLOGY 2023/24 is the sixth in this series of biennial publications. The Concise Guide provides concise overviews, mostly in tabular format, of the key properties of approximately 1800 drug targets, and about 6000 interactions with about 3900 ligands. There is an emphasis on selective pharmacology (where available), plus links to the open access knowledgebase source of drug targets and their ligands (https://www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. Although the Concise Guide constitutes almost 500 pages, the material presented is substantially reduced compared to information and links presented on the website. It provides a permanent, citable, point-in-time record that will survive database updates. The full contents of this section can be found at http://onlinelibrary.wiley.com/doi/bph.16177. G protein-coupled receptors are one of the six major pharmacological targets into which the Guide is divided, with the others being: ion channels, nuclear hormone receptors, catalytic receptors, enzymes and transporters. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. The landscape format of the Concise Guide is designed to facilitate comparison of related targets from material contemporary to mid-2023, and supersedes data presented in the 2021/22, 2019/20, 2017/18, 2015/16 and 2013/14 Concise Guides and previous Guides to Receptors and Channels. It is produced in close conjunction with the Nomenclature and Standards Committee of the International Union of Basic and Clinical Pharmacology (NC-IUPHAR), therefore, providing official IUPHAR classification and nomenclature for human drug targets, where appropriate., (© 2023 The Authors. British Journal of Pharmacology published by John Wiley & Sons Ltd on behalf of The British Pharmacological Society.)
Published: 2023
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48. The Concise Guide to PHARMACOLOGY 2023/24: Introduction and Other Protein Targets.

Author: Alexander SPH, Kelly E, Mathie AA, Peters JA, Veale EL, Armstrong JF, Buneman OP, Faccenda E, Harding SD, Spedding M, Cidlowski JA, Fabbro D, Davenport AP, Striessnig J, Davies JA, Ahlers-Dannen KE, Alqinyah M, Arumugam TV, Bodle C, Dagner JB, Chakravarti B, Choudhuri SP, Druey KM, Fisher RA, Gerber KJ, Hepler JR, Hooks SB, Kantheti HS, Karaj B, Layeghi-Ghalehsoukhteh S, Lee JK, Luo Z, Martemyanov K, Mascarenhas LD, McNabb H, Montañez-Miranda C, Ogujiofor O, Phan H, Roman DL, Shaw V, Sjogren B, Sobey C, Spicer MM, Squires KE, Sutton L, Wendimu M, Wilkie T, Xie K, Zhang Q, and Zolghadri Y
Subjects: Humans, Databases, Factual, Ion Channels, Ligands, Receptors, Cytoplasmic and Nuclear, Databases, Pharmaceutical, Pharmacology
Abstract: The Concise Guide to PHARMACOLOGY 2023/24 is the sixth in this series of biennial publications. The Concise Guide provides concise overviews, mostly in tabular format, of the key properties of approximately 1800 drug targets, and about 6000 interactions with about 3900 ligands. There is an emphasis on selective pharmacology (where available), plus links to the open access knowledgebase source of drug targets and their ligands (www.guidetopharmacology.org), which provides more detailed views of target and ligand properties. Although the Concise Guide constitutes almost 500 pages, the material presented is substantially reduced compared to information and links presented on the website. It provides a permanent, citable, point-in-time record that will survive database updates. The full contents of this section can be found at http://onlinelibrary.wiley.com/doi/10.1111/bph.16176. In addition to this overview, in which are identified 'Other protein targets' which fall outside of the subsequent categorisation, there are six areas of focus: G protein-coupled receptors, ion channels, nuclear hormone receptors, catalytic receptors, enzymes and transporters. These are presented with nomenclature guidance and summary information on the best available pharmacological tools, alongside key references and suggestions for further reading. The landscape format of the Concise Guide is designed to facilitate comparison of related targets from material contemporary to mid-2023, and supersedes data presented in the 2021/22, 2019/20, 2017/18, 2015/16 and 2013/14 Concise Guides and previous Guides to Receptors and Channels. It is produced in close conjunction with the Nomenclature and Standards Committee of the International Union of Basic and Clinical Pharmacology (NC-IUPHAR), therefore, providing official IUPHAR classification and nomenclature for human drug targets, where appropriate., (© 2023 The Authors. British Journal of Pharmacology published by John Wiley & Sons Ltd on behalf of The British Pharmacological Society.)
Published: 2023
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49. Advances in malaria pharmacology and the online guide to MALARIA PHARMACOLOGY: IUPHAR review 38.

Author: Armstrong JF, Campo B, Alexander SPH, Arendse LB, Cheng X, Davenport AP, Faccenda E, Fidock DA, Godinez-Macias KP, Harding SD, Kato N, Lee MCS, Luth MR, Mazitschek R, Mittal N, Niles JC, Okombo J, Ottilie S, Pasaje CFA, Probst AS, Rawat M, Rocamora F, Sakata-Kato T, Southan C, Spedding M, Tye MA, Yang T, Zhao N, and Davies JA
Subjects: Humans, Drug Discovery, High-Throughput Screening Assays, Malaria drug therapy, Antimalarials pharmacology, Antimalarials therapeutic use
Abstract: Antimalarial drug discovery has until recently been driven by high-throughput phenotypic cellular screening, allowing millions of compounds to be assayed and delivering clinical drug candidates. In this review, we will focus on target-based approaches, describing recent advances in our understanding of druggable targets in the malaria parasite. Targeting multiple stages of the Plasmodium lifecycle, rather than just the clinically symptomatic asexual blood stage, has become a requirement for new antimalarial medicines, and we link pharmacological data clearly to the parasite stages to which it applies. Finally, we highlight the IUPHAR/MMV Guide to MALARIA PHARMACOLOGY, a web resource developed for the malaria research community that provides open and optimized access to published data on malaria pharmacology., (© 2023 The Authors. British Journal of Pharmacology published by John Wiley & Sons Ltd on behalf of British Pharmacological Society.)
Published: 2023
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50. Inducible apelin receptor knockdown reduces differentiation efficiency and contractility of hESC-derived cardiomyocytes.

Author: Macrae RGC, Colzani MT, Williams TL, Bayraktar S, Kuc RE, Pullinger AL, Bernard WG, Robinson EL, Davenport EE, Maguire JJ, Sinha S, and Davenport AP
Subjects: Adult, Humans, Apelin genetics, Apelin metabolism, Apelin Receptors genetics, Apelin Receptors metabolism, Embryonic Stem Cells metabolism, Cell Differentiation, Myocytes, Cardiac metabolism, Human Embryonic Stem Cells
Abstract: Aims: The apelin receptor, a G protein-coupled receptor, has emerged as a key regulator of cardiovascular development, physiology, and disease. However, there is a lack of suitable human in vitro models to investigate the apelinergic system in cardiovascular cell types. For the first time we have used human embryonic stem cell-derived cardiomyocytes (hESC-CMs) and a novel inducible knockdown system to examine the role of the apelin receptor in both cardiomyocyte development and to determine the consequences of loss of apelin receptor function as a model of disease., Methods and Results: Expression of the apelin receptor and its ligands in hESCs and hESC-CMs was determined. hESCs carrying a tetracycline-inducible short hairpin RNA targeting the apelin receptor were generated using the sOPTiKD system. Phenotypic assays characterized the consequences of either apelin receptor knockdown before hESC-CM differentiation (early knockdown) or in 3D engineered heart tissues as a disease model (late knockdown). hESC-CMs expressed the apelin signalling system at a similar level to the adult heart. Early apelin receptor knockdown decreased cardiomyocyte differentiation efficiency and prolonged voltage sensing, associated with asynchronous contraction. Late apelin receptor knockdown had detrimental consequences on 3D engineered heart tissue contractile properties, decreasing contractility and increasing stiffness., Conclusions: We have successfully knocked down the apelin receptor, using an inducible system, to demonstrate a key role in hESC-CM differentiation. Knockdown in 3D engineered heart tissues recapitulated the phenotype of apelin receptor down-regulation in a failing heart, providing a potential platform for modelling heart failure and testing novel therapeutic strategies., Competing Interests: Conflict of interest: None declared., (© The Author(s) 2022. Published by Oxford University Press on behalf of the European Society of Cardiology.)
Published: 2023
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