33 results on '"Behrens, Maik"'
Search Results
2. Pharmacology of TAS1R2/TAS1R3 Receptors and Sweet Taste
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Behrens, Maik, Barrett, James E., Editor-in-Chief, Flockerzi, Veit, Editorial Board Member, Frohman, Michael A., Editorial Board Member, Geppetti, Pierangelo, Editorial Board Member, Hofmann, Franz B., Editorial Board Member, Kuner, Rohini, Editorial Board Member, Michel, Martin C., Editorial Board Member, Page, Clive P., Editorial Board Member, Wang, KeWei, Editorial Board Member, Palmer, R. Kyle, editor, and Servant, Guy, editor
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- 2022
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3. Membrane-bound chemoreception of bitter bile acids and peptides is mediated by the same subset of bitter taste receptors
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Schaefer, Silvia, primary, Ziegler, Florian, additional, Lang, Tatjana, additional, Steuer, Alexandra, additional, Di Pizio, Antonella, additional, and Behrens, Maik, additional
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- 2024
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4. Impact of lactisole on the time-intensity profile of selected sweeteners in dependence of the binding site
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Deck, Corinna M., Behrens, Maik, Wendelin, Martin, Ley, Jakob P., Krammer, Gerhard E., and Lieder, Barbara
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- 2022
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5. BitterMatch: recommendation systems for matching molecules with bitter taste receptors
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Margulis, Eitan, Slavutsky, Yuli, Lang, Tatjana, Behrens, Maik, Benjamini, Yuval, and Niv, Masha Y.
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- 2022
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6. Influence of Sodium Chloride on Human Bitter Taste Receptor Responses.
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Kumar, Praveen and Behrens, Maik
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- 2024
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7. Differential Activation of TAS2R4 May Recover Ability to Taste Propylthiouracil for Some TAS2R38 AVI Homozygotes.
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Nolden, Alissa A., Behrens, Maik, McGeary, John E., Meyerhof, Wolfgang, and Hayes, John E.
- Abstract
Bitterness from phenylthiocarbamide and 6-n-propylthiouracil (PROP) varies with polymorphisms in the TAS2R38 gene. Three SNPs form two common (AVI, PAV) and four rare haplotypes (AAI, AAV, PVI, and PAI). AVI homozygotes exhibit higher detection thresholds and lower suprathreshold bitterness for PROP compared to PAV homozygotes and heterozygotes, and these differences may influence alcohol and vegetable intake. Within a diplotype, substantial variation in suprathreshold bitterness persists, and some AVI homozygotes report moderate bitterness at high concentrations. A second receptor encoded by a gene containing a functional polymorphism may explain this. Early work has suggested that PROP might activate TAS2R4 in vitro, but later work did not replicate this. Here, we identify three TAS2R4 SNPs that result in three diplotypes—SLN/SLN, FVS/SLN, and FVS/FVS—which make up 25.1%, 44.9%, and 23.9% of our sample. These TAS2R4 haplotypes show minimal linkage disequilibrium with TAS2R38, so we examined the suprathreshold bitterness as a function of both. The participants (n = 243) rated five PROP concentrations in duplicate, interleaved with other stimuli. As expected, the TAS2R38 haplotypes explained ~29% (p < 0.0001) of the variation in the bitterness ratings, with substantial variation within the haplotypes (AVI/AVI, PAV/AVI, and PAV/PAV). Notably, the TAS2R4 diplotypes (independent of the TAS2R38 haplotypes) explained ~7–8% of the variation in the bitterness ratings (p = 0.0001). Given this, we revisited if PROP could activate heterologously expressed TAS2R4 in HEK293T cells, and calcium imaging indicated 3 mM PROP is a weak TAS2R4 agonist. In sum, our data are consistent with the second receptor hypothesis and may explain the recovery of the PROP tasting phenotype in some AVI homozygotes; further, this finding may potentially help explain the conflicting results on the TAS2R38 diplotype and food intake. [ABSTRACT FROM AUTHOR]
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- 2024
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8. A singular shark bitter taste receptor provides insights into the evolution of bitter taste perception
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Behrens, Maik, primary, Lang, Tatjana, additional, and Korsching, Sigrun I., additional
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- 2023
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9. Sweet taste of heavy water
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Ben Abu, Natalie, Mason, Philip E., Klein, Hadar, Dubovski, Nitzan, Ben Shoshan-Galeczki, Yaron, Malach, Einav, Pražienková, Veronika, Maletínská, Lenka, Tempra, Carmelo, Chamorro, Victor Cruces, Cvačka, Josef, Behrens, Maik, Niv, Masha Y., and Jungwirth, Pavel
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- 2021
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10. The Growing Complexity of Human Bitter Taste Perception
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Behrens, Maik
- Abstract
Human bitter perception is important for the identification of potentially harmful substances in food. For quite some years, research focused on the identification of activators for ∼25 human bitter taste receptors. The discovery of antagonists as well as increasing knowledge about agonists of different efficacies has substantially added to the intricacy of bitter taste perception. This article seeks to raise awareness for an underestimated new level of complexity when compound mixtures or even whole food items are assessed for their bitter taste.
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- 2024
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11. Bitter taste receptors of the zebra finch (Taeniopygia guttata)
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Kumar, Praveen, primary, Redel, Ulrike, additional, Lang, Tatjana, additional, Korsching, Sigrun I., additional, and Behrens, Maik, additional
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- 2023
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12. Taste 2 receptors in GtoPdb v.2023.1
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Behrens, Maik, primary
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- 2023
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13. Human Gingival Fibroblasts as a Novel Cell Model Describing the Association between Bitter Taste Thresholds and Interleukin-6 Release
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Tiroch, Johanna, primary, Dunkel, Andreas, additional, Sterneder, Sonja, additional, Zehentner, Sofie, additional, Behrens, Maik, additional, Di Pizio, Antonella, additional, Ley, Jakob P., additional, Lieder, Barbara, additional, and Somoza, Veronika, additional
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- 2023
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14. Activation Profile of Tas2r2, The 26th Human Bitter Taste Receptor
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Lang, Tatjana, primary, Pizio, Antonella Di, additional, Risso, Davide, additional, Drayna, Dennis, additional, and Behrens, Maik, additional
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- 2023
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15. The Concise Guide to PHARMACOLOGY 2023/24 : G protein-coupled receptors
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Alexander, Stephen P. H., Christopoulos, Arthur, Davenport, Anthony P., Kelly, Eamonn, Mathie, Alistair A., Peters, John A., Veale, Emma L., Armstrong, Jane F., Faccenda, Elena, Harding, Simon D., Davies, Jamie A., Abbracchio, Maria Pia, Abraham, George, Agoulnik, Alexander, Alexander, Wayne, Al-hosaini, Khaled, Baeck, Magnus, Baker, Jillian G., Barnes, Nicholas M., Bathgate, Ross, Beaulieu, Jean-Martin, Beck-Sickinger, Annette G., Behrens, Maik, Bernstein, Kenneth E., Bettler, Bernhard, Birdsall, Nigel J. M., Blaho, Victoria, Boulay, Francois, Bousquet, Corinne, Braeuner-Osborne, Hans, Burnstock, Geoffrey, Calo, Girolamo, Castano, Justo P., Catt, Kevin J., Ceruti, Stefania, Chazot, Paul, Chiang, Nan, Chini, Bice, Chun, Jerold, Cianciulli, Antonia, Civelli, Olivier, Clapp, Lucie H., Couture, Rejean, Cox, Helen M., Csaba, Zsolt, Dahlgren, Claes, Dent, Gordon, Douglas, Steven D., Dournaud, Pascal, Eguchi, Satoru, Escher, Emanuel, Filardo, Edward J., Fong, Tung, Fumagalli, Marta, Gainetdinov, Raul R., Garelja, Michael L., de Gasparo, Marc, Gerard, Craig, Gershengorn, Marvin, Gobeil, Fernand, Goodfriend, Theodore L., Goudet, Cyril, Graetz, Lukas, Gregory, Karen J., Gundlach, Andrew L., Hamann, Joerg, Hanson, Julien, Hauger, Richard L., Hay, Debbie L., Heinemann, Akos, Herr, Deron, Hollenberg, Morley D., Holliday, Nicholas D., Horiuchi, Mastgugu, Hoyer, Daniel, Hunyady, Laszlo, Husain, Ahsan, Ijzerman, Adriaan P., Inagami, Tadashi, Jacobson, Kenneth A., Jensen, Robert T., Jockers, Ralf, Jonnalagadda, Deepa, Karnik, Sadashiva, Kaupmann, Klemens, Kemp, Jacqueline, Kennedy, Charles, Kihara, Yasuyuki, Kitazawa, Takio, Kozielewicz, Pawel, Kreienkamp, Hans-Juergen, Kukkonen, Jyrki P., Langenhan, Tobias, Larhammar, Dan, Leach, Katie, Lecca, Davide, Lee, John D., Leeman, Susan E., Leprince, Jerome, Li, Xaria X., Lolait, Stephen J., Lupp, Amelie, Macrae, Robyn, Maguire, Janet, Malfacini, Davide, Mazella, Jean, Mcardle, Craig A., Melmed, Shlomo, Michel, Martin C., Miller, Laurence J., Mitolo, Vincenzo, Mouillac, Bernard, Mueller, Christa E., Murphy, Philip M., Nahon, Jean-Louis, Ngo, Tony, Norel, Xavier, Nyimanu, Duuamene, O'Carroll, Anne-Marie, Offermanns, Stefan, Panaro, Maria Antonietta, Parmentier, Marc, Pertwee, Roger G., Pin, Jean-Philippe, Prossnitz, Eric R., Quinn, Mark, Ramachandran, Rithwik, Ray, Manisha, Reinscheid, Rainer K., Rondard, Philippe, Rovati, G. Enrico, Ruzza, Chiara, Sanger, Gareth J., Schoeneberg, Torsten, Schulte, Gunnar, Schulz, Stefan, Segaloff, Deborah L., Serhan, Charles N., Singh, Khuraijam Dhanachandra, Smith, Craig M., Stoddart, Leigh A., Sugimoto, Yukihiko, Summers, Roger, Tan, Valerie P., Thal, David, Thomas, Walter ( Wally), Timmermans, Pieter B. M. W. M., Tirupula, Kalyan, Toll, Lawrence, Tulipano, Giovanni, Unal, Hamiyet, Unger, Thomas, Valant, Celine, Vanderheyden, Patrick, Vaudry, David, Vaudry, Hubert, Vilardaga, Jean-Pierre, Walker, Christopher S., Wang, Ji Ming, Ward, Donald T., Wester, Hans-Juergen, Willars, Gary B., Williams, Tom Lloyd, Woodruff, Trent M., Yao, Chengcan, Ye, Richard D., Alexander, Stephen P. H., Christopoulos, Arthur, Davenport, Anthony P., Kelly, Eamonn, Mathie, Alistair A., Peters, John A., Veale, Emma L., Armstrong, Jane F., Faccenda, Elena, Harding, Simon D., Davies, Jamie A., Abbracchio, Maria Pia, Abraham, George, Agoulnik, Alexander, Alexander, Wayne, Al-hosaini, Khaled, Baeck, Magnus, Baker, Jillian G., Barnes, Nicholas M., Bathgate, Ross, Beaulieu, Jean-Martin, Beck-Sickinger, Annette G., Behrens, Maik, Bernstein, Kenneth E., Bettler, Bernhard, Birdsall, Nigel J. M., Blaho, Victoria, Boulay, Francois, Bousquet, Corinne, Braeuner-Osborne, Hans, Burnstock, Geoffrey, Calo, Girolamo, Castano, Justo P., Catt, Kevin J., Ceruti, Stefania, Chazot, Paul, Chiang, Nan, Chini, Bice, Chun, Jerold, Cianciulli, Antonia, Civelli, Olivier, Clapp, Lucie H., Couture, Rejean, Cox, Helen M., Csaba, Zsolt, Dahlgren, Claes, Dent, Gordon, Douglas, Steven D., Dournaud, Pascal, Eguchi, Satoru, Escher, Emanuel, Filardo, Edward J., Fong, Tung, Fumagalli, Marta, Gainetdinov, Raul R., Garelja, Michael L., de Gasparo, Marc, Gerard, Craig, Gershengorn, Marvin, Gobeil, Fernand, Goodfriend, Theodore L., Goudet, Cyril, Graetz, Lukas, Gregory, Karen J., Gundlach, Andrew L., Hamann, Joerg, Hanson, Julien, Hauger, Richard L., Hay, Debbie L., Heinemann, Akos, Herr, Deron, Hollenberg, Morley D., Holliday, Nicholas D., Horiuchi, Mastgugu, Hoyer, Daniel, Hunyady, Laszlo, Husain, Ahsan, Ijzerman, Adriaan P., Inagami, Tadashi, Jacobson, Kenneth A., Jensen, Robert T., Jockers, Ralf, Jonnalagadda, Deepa, Karnik, Sadashiva, Kaupmann, Klemens, Kemp, Jacqueline, Kennedy, Charles, Kihara, Yasuyuki, Kitazawa, Takio, Kozielewicz, Pawel, Kreienkamp, Hans-Juergen, Kukkonen, Jyrki P., Langenhan, Tobias, Larhammar, Dan, Leach, Katie, Lecca, Davide, Lee, John D., Leeman, Susan E., Leprince, Jerome, Li, Xaria X., Lolait, Stephen J., Lupp, Amelie, Macrae, Robyn, Maguire, Janet, Malfacini, Davide, Mazella, Jean, Mcardle, Craig A., Melmed, Shlomo, Michel, Martin C., Miller, Laurence J., Mitolo, Vincenzo, Mouillac, Bernard, Mueller, Christa E., Murphy, Philip M., Nahon, Jean-Louis, Ngo, Tony, Norel, Xavier, Nyimanu, Duuamene, O'Carroll, Anne-Marie, Offermanns, Stefan, Panaro, Maria Antonietta, Parmentier, Marc, Pertwee, Roger G., Pin, Jean-Philippe, Prossnitz, Eric R., Quinn, Mark, Ramachandran, Rithwik, Ray, Manisha, Reinscheid, Rainer K., Rondard, Philippe, Rovati, G. Enrico, Ruzza, Chiara, Sanger, Gareth J., Schoeneberg, Torsten, Schulte, Gunnar, Schulz, Stefan, Segaloff, Deborah L., Serhan, Charles N., Singh, Khuraijam Dhanachandra, Smith, Craig M., Stoddart, Leigh A., Sugimoto, Yukihiko, Summers, Roger, Tan, Valerie P., Thal, David, Thomas, Walter ( Wally), Timmermans, Pieter B. M. W. M., Tirupula, Kalyan, Toll, Lawrence, Tulipano, Giovanni, Unal, Hamiyet, Unger, Thomas, Valant, Celine, Vanderheyden, Patrick, Vaudry, David, Vaudry, Hubert, Vilardaga, Jean-Pierre, Walker, Christopher S., Wang, Ji Ming, Ward, Donald T., Wester, Hans-Juergen, Willars, Gary B., Williams, Tom Lloyd, Woodruff, Trent M., Yao, Chengcan, and Ye, Richard D.
- 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 (), 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 . 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
- Full Text
- View/download PDF
16. Rebaudioside A from Stevia rebaudiana stimulates GLP-1 release by enteroendocrine cells via bitter taste signalling pathways
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Noya-Leal, Francisca, van der Wielen, Nikkie, Behrens, Maik, Rouschop, Sven, van Arkel, Jeroen, Jongsma, Maarten, Witkamp, Renger, Mes, Jurriaan J., Bastiaan-Net, Shanna, Meijerink, Jocelijn, Noya-Leal, Francisca, van der Wielen, Nikkie, Behrens, Maik, Rouschop, Sven, van Arkel, Jeroen, Jongsma, Maarten, Witkamp, Renger, Mes, Jurriaan J., Bastiaan-Net, Shanna, and Meijerink, Jocelijn
- Abstract
Glucagon-like peptide 1 (GLP-1) is a multifaceted intestinal hormone with diverse physiological functions throughout the body. Previously, we demonstrated that the steviol glycoside rebaudioside A (rebA) from Stevia rebaudiana stimulates the release of GLP-1 from mouse intestinal organoids and pig intestinal segments. To further unravel the underlying mechanisms, we examined the involvement of sweet- and bitter taste receptors and their associated signal transduction pathways. Experiments with mouse and human intestinal enteroendocrine cell lines (STC-1 and HuTu-80, respectively) confirmed that rebA stimulates GLP-1 release in a concentration-dependent manner. Experiments with selective inhibitors of sweet signalling in both the murine as well as the human enteroendocrine cells showed that the GLP-1-induced release by rebA occurs independently of the sweet taste receptor. Functional screening of 34 murine bitter taste receptors (Tas2rs) revealed an activation response with Tas2r108, Tas2r123 and Tas2r134. Moreover, we found evidence in human HuTu-80 cells, that TAS2R4 and TRPM5 are involved in rebA-induced GLP-1 secretion, suggesting a role for bitter taste signaling in gut hormone release. Interestingly, the rebA-dependent GLP-1 release may be modulated by GABA and 6-methoxyflavanone present in the diet. Together, our findings warrant further characterization of the specific metabolic effects of rebA among the non-caloric sweeteners.
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- 2023
17. The Concise Guide to PHARMACOLOGY 2023/24:G protein-coupled receptors
- Author
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Alexander, Stephen P H, Christopoulos, Arthur, Davenport, Anthony P, Kelly, Eamonn, Mathie, Alistair A, Peters, John A, Veale, Emma L, Armstrong, Jane F, Faccenda, Elena, Harding, Simon D, Davies, Jamie A, Abbracchio, Maria Pia, Abraham, George, Agoulnik, Alexander, Alexander, Wayne, Al-Hosaini, Khaled, Bäck, Magnus, Baker, Jillian G, Barnes, Nicholas M, Bathgate, Ross, Beaulieu, Jean-Martin, Beck-Sickinger, Annette G, Behrens, Maik, Bernstein, Kenneth E, Bettler, Bernhard, Birdsall, Nigel J M, Blaho, Victoria, Boulay, Francois, Bousquet, Corinne, Bräuner-Osborne, Hans, Burnstock, Geoffrey, Caló, Girolamo, Castaño, Justo P, Catt, Kevin J, Ceruti, Stefania, Chazot, Paul, Chiang, Nan, Chini, Bice, Chun, Jerold, Cianciulli, Antonia, Civelli, Olivier, Clapp, Lucie H, Couture, Réjean, Cox, Helen M, Csaba, Zsolt, Dahlgren, Claes, Dent, Gordon, Douglas, Steven D, Dournaud, Pascal, Eguchi, Satoru, Escher, Emanuel, Filardo, Edward J, Fong, Tung, Fumagalli, Marta, Gainetdinov, Raul R, Garelja, Michael L, de Gasparo, Marc, Gerard, Craig, Gershengorn, Marvin, Gobeil, Fernand, Goodfriend, Theodore L, Goudet, Cyril, Grätz, Lukas, Gregory, Karen J, Gundlach, Andrew L, Hamann, Jörg, Hanson, Julien, Hauger, Richard L, Hay, Debbie L, Heinemann, Akos, Herr, Deron, Hollenberg, Morley D, Holliday, Nicholas D, Horiuchi, Mastgugu, Hoyer, Daniel, Hunyady, László, Husain, Ahsan, IJzerman, Adriaan P, Inagami, Tadashi, Jacobson, Kenneth A, Jensen, Robert T, Jockers, Ralf, Jonnalagadda, Deepa, Karnik, Sadashiva, Kaupmann, Klemens, Kemp, Jacqueline, Kennedy, Charles, Kihara, Yasuyuki, Kitazawa, Takio, Kozielewicz, Pawel, Kreienkamp, Hans-Jürgen, Kukkonen, Jyrki P, Langenhan, Tobias, Larhammar, Dan, Leach, Katie, Lecca, Davide, Lee, John D, Leeman, Susan E, Leprince, Jérôme, Li, Xaria X, Lolait, Stephen J, Lupp, Amelie, Macrae, Robyn, Maguire, Janet, Malfacini, Davide, Mazella, Jean, McArdle, Craig A, Melmed, Shlomo, Michel, Martin C, Miller, Laurence J, Mitolo, Vincenzo, Mouillac, Bernard, Müller, Christa E, Murphy, Philip M, Nahon, Jean-Louis, Ngo, Tony, Norel, Xavier, Nyimanu, Duuamene, O'Carroll, Anne-Marie, Offermanns, Stefan, Panaro, Maria Antonietta, Parmentier, Marc, Pertwee, Roger G, Pin, Jean-Philippe, Prossnitz, Eric R, Quinn, Mark, Ramachandran, Rithwik, Ray, Manisha, Reinscheid, Rainer K, Rondard, Philippe, Rovati, G Enrico, Ruzza, Chiara, Sanger, Gareth J, Schöneberg, Torsten, Schulte, Gunnar, Schulz, Stefan, Segaloff, Deborah L, Serhan, Charles N, Singh, Khuraijam Dhanachandra, Smith, Craig M, Stoddart, Leigh A, Sugimoto, Yukihiko, Summers, Roger, Tan, Valerie P, Thal, David, Thomas, Walter Wally, Timmermans, Pieter B M W M, Tirupula, Kalyan, Toll, Lawrence, Tulipano, Giovanni, Unal, Hamiyet, Unger, Thomas, Valant, Celine, Vanderheyden, Patrick, Vaudry, David, Vaudry, Hubert, Vilardaga, Jean-Pierre, Walker, Christopher S, Wang, Ji Ming, Ward, Donald T, Wester, Hans-Jürgen, Willars, Gary B, Williams, Tom Lloyd, Woodruff, Trent M, Yao, Chengcan, Ye, Richard D, Alexander, Stephen P H, Christopoulos, Arthur, Davenport, Anthony P, Kelly, Eamonn, Mathie, Alistair A, Peters, John A, Veale, Emma L, Armstrong, Jane F, Faccenda, Elena, Harding, Simon D, Davies, Jamie A, Abbracchio, Maria Pia, Abraham, George, Agoulnik, Alexander, Alexander, Wayne, Al-Hosaini, Khaled, Bäck, Magnus, Baker, Jillian G, Barnes, Nicholas M, Bathgate, Ross, Beaulieu, Jean-Martin, Beck-Sickinger, Annette G, Behrens, Maik, Bernstein, Kenneth E, Bettler, Bernhard, Birdsall, Nigel J M, Blaho, Victoria, Boulay, Francois, Bousquet, Corinne, Bräuner-Osborne, Hans, Burnstock, Geoffrey, Caló, Girolamo, Castaño, Justo P, Catt, Kevin J, Ceruti, Stefania, Chazot, Paul, Chiang, Nan, Chini, Bice, Chun, Jerold, Cianciulli, Antonia, Civelli, Olivier, Clapp, Lucie H, Couture, Réjean, Cox, Helen M, Csaba, Zsolt, Dahlgren, Claes, Dent, Gordon, Douglas, Steven D, Dournaud, Pascal, Eguchi, Satoru, Escher, Emanuel, Filardo, Edward J, Fong, Tung, Fumagalli, Marta, Gainetdinov, Raul R, Garelja, Michael L, de Gasparo, Marc, Gerard, Craig, Gershengorn, Marvin, Gobeil, Fernand, Goodfriend, Theodore L, Goudet, Cyril, Grätz, Lukas, Gregory, Karen J, Gundlach, Andrew L, Hamann, Jörg, Hanson, Julien, Hauger, Richard L, Hay, Debbie L, Heinemann, Akos, Herr, Deron, Hollenberg, Morley D, Holliday, Nicholas D, Horiuchi, Mastgugu, Hoyer, Daniel, Hunyady, László, Husain, Ahsan, IJzerman, Adriaan P, Inagami, Tadashi, Jacobson, Kenneth A, Jensen, Robert T, Jockers, Ralf, Jonnalagadda, Deepa, Karnik, Sadashiva, Kaupmann, Klemens, Kemp, Jacqueline, Kennedy, Charles, Kihara, Yasuyuki, Kitazawa, Takio, Kozielewicz, Pawel, Kreienkamp, Hans-Jürgen, Kukkonen, Jyrki P, Langenhan, Tobias, Larhammar, Dan, Leach, Katie, Lecca, Davide, Lee, John D, Leeman, Susan E, Leprince, Jérôme, Li, Xaria X, Lolait, Stephen J, Lupp, Amelie, Macrae, Robyn, Maguire, Janet, Malfacini, Davide, Mazella, Jean, McArdle, Craig A, Melmed, Shlomo, Michel, Martin C, Miller, Laurence J, Mitolo, Vincenzo, Mouillac, Bernard, Müller, Christa E, Murphy, Philip M, Nahon, Jean-Louis, Ngo, Tony, Norel, Xavier, Nyimanu, Duuamene, O'Carroll, Anne-Marie, Offermanns, Stefan, Panaro, Maria Antonietta, Parmentier, Marc, Pertwee, Roger G, Pin, Jean-Philippe, Prossnitz, Eric R, Quinn, Mark, Ramachandran, Rithwik, Ray, Manisha, Reinscheid, Rainer K, Rondard, Philippe, Rovati, G Enrico, Ruzza, Chiara, Sanger, Gareth J, Schöneberg, Torsten, Schulte, Gunnar, Schulz, Stefan, Segaloff, Deborah L, Serhan, Charles N, Singh, Khuraijam Dhanachandra, Smith, Craig M, Stoddart, Leigh A, Sugimoto, Yukihiko, Summers, Roger, Tan, Valerie P, Thal, David, Thomas, Walter Wally, Timmermans, Pieter B M W M, Tirupula, Kalyan, Toll, Lawrence, Tulipano, Giovanni, Unal, Hamiyet, Unger, Thomas, Valant, Celine, Vanderheyden, Patrick, Vaudry, David, Vaudry, Hubert, Vilardaga, Jean-Pierre, Walker, Christopher S, Wang, Ji Ming, Ward, Donald T, Wester, Hans-Jürgen, Willars, Gary B, Williams, Tom Lloyd, Woodruff, Trent M, Yao, Chengcan, and Ye, Richard D
- 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
18. Rebaudioside A from Stevia rebaudiana stimulates GLP-1 release by enteroendocrine cells via bitter taste signalling pathways
- Author
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Noya-Leal, Francisca, primary, van der Wielen, Nikkie, additional, Behrens, Maik, additional, Rouschop, Sven, additional, van Arkel, Jeroen, additional, Jongsma, Maarten, additional, Witkamp, Renger, additional, Mes, Jurriaan J., additional, Bastiaan-Net, Shanna, additional, and Meijerink, Jocelijn, additional
- Published
- 2023
- Full Text
- View/download PDF
19. Overlapping activation pattern of bitter taste receptors affect sensory adaptation and food perception
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Lang, Roman, primary, Lang, Tatjana, additional, Dunkel, Andreas, additional, Ziegler, Florian, additional, and Behrens, Maik, additional
- Published
- 2022
- Full Text
- View/download PDF
20. Bitter Peptides YFYPEL, VAPFPEVF, and YQEPVLGPVRGPFPIIV, Released during Gastric Digestion of Casein, Stimulate Mechanisms of Gastric Acid Secretion via Bitter Taste Receptors TAS2R16 and TAS2R38
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Richter, Phil, primary, Sebald, Karin, additional, Fischer, Konrad, additional, Behrens, Maik, additional, Schnieke, Angelika, additional, and Somoza, Veronika, additional
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- 2022
- Full Text
- View/download PDF
21. Nahrungsinhaltsstoffe: Chemorezeptor-vermitteltes pharmakonutritives Potenzial
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Olias, Gisela, additional, Behrens, Maik, additional, Andersen, Gaby, additional, and Somoza, Veronika, additional
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- 2022
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22. Bitter Odorants and Odorous Bitters: Toxicity and Human TAS2R Targets.
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Margulis, Eitan, Lang, Tatjana, Tromelin, Anne, Ziaikin, Evgenii, Behrens, Maik, and Niv, Masha Y.
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- 2023
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23. Physiological activation of human and mouse bitter taste receptors by bile acids.
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Ziegler, Florian, Steuer, Alexandra, Di Pizio, Antonella, and Behrens, Maik
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Beside the oral cavity, bitter taste receptors are expressed in several non-gustatory tissues. Whether extra-oral bitter taste receptors function as sensors for endogenous agonists is unknown. To address this question, we devised functional experiments combined with molecular modeling approaches to investigate human and mouse receptors using a variety of bile acids as candidate agonists. We show that five human and six mouse receptors are responsive to an array of bile acids. Moreover, their activation threshold concentrations match published data of bile acid concentrations in human body fluids, suggesting a putative physiological activation of non-gustatory bitter receptors. We conclude that these receptors could serve as sensors for endogenous bile acid levels. These results also indicate that bitter receptor evolution may not be driven solely by foodstuff or xenobiotic stimuli, but also depend on endogenous ligands. The determined bitter receptor activation profiles of bile acids now enable detailed physiological model studies. Using a combined experimental-computational approach, the activation profiles of human and mouse bitter taste receptors, TAS2Rs and Tas2rs, by bile acids is described, suggesting a physiological role of bile acids for taste receptors in non-gustatory tissues. [ABSTRACT FROM AUTHOR]
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- 2023
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24. Extra-Oral Taste Receptors—Function, Disease, and Perspectives
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Behrens, Maik, primary and Lang, Tatjana, additional
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- 2022
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25. Activation Spectra of Human Bitter Taste Receptors Stimulated with Cyclolinopeptides Corresponding to Fresh and Aged Linseed Oil
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Lang, Tatjana, primary, Frank, Oliver, additional, Lang, Roman, additional, Hofmann, Thomas, additional, and Behrens, Maik, additional
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- 2022
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26. Additional file 7 of BitterMatch: recommendation systems for matching molecules with bitter taste receptors
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Margulis, Eitan, Slavutsky, Yuli, Lang, Tatjana, Behrens, Maik, Benjamini, Yuval, and Niv, Masha Y.
- Abstract
Additional file 7: Table S1. Substances used for experimental testing of prospective predictions and their maximal employed concentrations. Table S2. XGBoost hyper-parameters. To avoid overfitting 1000 trees were used accordingly the following hyper-parameters were adjusted. The rest of the parameters were set to their default values. Table S3. Prospective prediction results per ligand. 1–represents an activation of the receptor that was confirmed experimentally and blank space means no activation was detected. *-positive activation that was detected in another publication but not in our in-vitro experiment. green–TP, red-FN, blue-FP and white-TN
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- 2022
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27. BitterMatch: Recommendation systems for matching molecules with bitter taste receptors
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Margulis, Eitan, primary, Slavutsky, Yuli, additional, Lang, Tatjana, additional, Behrens, Maik, additional, Benjamini, Yuval, additional, and Niv, Masha Y., additional
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- 2022
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28. Bitter Sensing TAS2R50 Mediates the trans-Resveratrol-Induced Anti-inflammatory Effect on Interleukin 6 Release in HGF-1 Cells in Culture.
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Tiroch, Johanna, Sterneder, Sonja, Pizio, Antonella Di, Lieder, Barbara, Hoelz, Kathrin, Holik, Ann-Katrin, Pignitter, Marc, Behrens, Maik, Somoza, Mark, Ley, Jakob P., and Somoza, Veronika
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- 2021
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29. Correction to “The Growing Complexity of Human Bitter Taste Perception”
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Behrens, Maik
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- 2024
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30. Bitter Peptides YFYPEL, VAPFPEVF, and YQEPVLGPVRGPFPIIV, Released during Gastric Digestion of Casein, Stimulate Mechanisms of Gastric Acid Secretion viaBitter Taste Receptors TAS2R16 and TAS2R38
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Richter, Phil, Sebald, Karin, Fischer, Konrad, Behrens, Maik, Schnieke, Angelika, and Somoza, Veronika
- Abstract
Eating satiating, protein-rich foods is one of the key aspects of modern diet, although a bitter off-taste often limits the application of some proteins and protein hydrolysates, especially in processed foods. Previous studies of our group demonstrated that bitter-tasting food constituents, such as caffeine, stimulate mechanisms of gastric acid secretion as a signal of gastric satiation and a key process of gastric protein digestion viaactivation of bitter taste receptors (TAS2Rs). Here, we tried to elucidate whether dietary non-bitter-tasting casein is intra-gastrically degraded into bitter peptides that stimulate mechanisms of gastric acid secretion in physiologically achievable concentrations. An in vitromodel of gastric digestion was verified by casein-fed pigs, and the peptides resulting from gastric digestion were identified by liquid chromatography–time-of-flight-mass spectrometry. The bitterness of five selected casein-derived peptides was validated by sensory analyses and by an in vitroscreening approach based on human gastric parietal cells (HGT-1). For three of these peptides (YFYPEL, VAPFPEVF, and YQEPVLGPVRGPFPIIV), an upregulation of gene expression of TAS2R16and TAS2R38was observed. The functional involvement of these TAS2Rs was verified by siRNA knock-down (kd) experiments in HGT-1 cells. This resulted in a reduction of the mean proton secretion promoted by the peptides by up to 86.3 ± 9.9% for TAS2R16kd (p< 0.0001) cells and by up to 62.8 ± 7.0% for TAS2R38kd (p< 0.0001) cells compared with mock-transfected cells.
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- 2022
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31. International Union of Basic and Clinical Pharmacology. CXVII: Taste 2 receptors: Structures, functions, activators and blockers.
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Behrens M
- Abstract
Bitter perception plays a critical role for the detection of potentially harmful substances in food items for most vertebrates. The detection of bitter compounds is facilitated by specialized receptors located in taste buds of the oral cavity. This work focuses on the receptors, including their sensitivities, structure-function relationships, agonists and antagonists. Moreover, the existence of numerous bitter taste receptor variants in the human population and the fact that several of them affect individual bitter tasting profoundly, is discussed as well. The identification of bitter taste receptors in numerous tissues outside the oral cavity and their multiple proposed roles in these tissues is also described briefly. Although this work is mainly focused on human bitter taste receptors, it is imperative to compare human bitter taste with that of other animals to understand which evolutionary forces might have shaped bitter taste receptors and their functions and to distinguish apparent typical human from rather general features. For the readers who are not too familiar with the gustatory system short descriptions of taste anatomy, signal transduction and oral bitter taste receptor expression are included in the beginning of this article. Significance Statement Apart from their role as sensors for potentially harmful substances in the oral cavity, the numerous additional roles of bitter taste receptors in tissues outside the gustatory system have received much attention recently. For the careful assessment of functions inside and outside the taste system a solid knowledge about the specific and general pharmacological features of these receptors and the growing toolbox available for studying them is imperative and provided in this work., (Copyright © 2024 American Society for Pharmacology and Experimental Therapeutics.)
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- 2024
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32. The Concise Guide to PHARMACOLOGY 2023/24: G protein-coupled receptors.
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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.)
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- 2023
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33. Bitter taste receptors: Genes, evolution and health.
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Wooding SP, Ramirez VA, and Behrens M
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Bitter taste perception plays vital roles in animal behavior and fitness. By signaling the presence of toxins in foods, particularly noxious defense compounds found in plants, it enables animals to avoid exposure. In vertebrates, bitter perception is initiated by TAS2Rs, a family of G protein-coupled receptors expressed on the surface of taste buds. There, oriented toward the interior of the mouth, they monitor the contents of foods, drinks and other substances as they are ingested. When bitter compounds are encountered, TAS2Rs respond by triggering neural pathways leading to sensation. The importance of this role placed TAS2Rs under selective pressures in the course of their evolution, leaving signatures in patterns of gene gain and loss, sequence polymorphism, and population structure consistent with vertebrates' diverse feeding ecologies. The protective value of bitter taste is reduced in modern humans because contemporary food supplies are safe and abundant. However, this is not always the case. Some crops, particularly in the developing world, retain surprisingly high toxicity and bitterness remains an important measure of safety. Bitter perception also shapes health through its influence on preference driven behaviors such as diet choice, alcohol intake and tobacco use. Further, allelic variation in TAS2R s is extensive, leading to individual differences in taste sensitivity that drive these behaviors, shaping susceptibility to disease. Thus, bitter taste perception occupies a critical intersection between ancient evolutionary processes and modern human health., (© The Author(s) 2021. Published by Oxford University Press on behalf of the Foundation for Evolution, Medicine, and Public Health.)
- Published
- 2021
- Full Text
- View/download PDF
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