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

Author

Alexander, Stephen PH, Kelly, Eamonn, Marrion, Neil, Peters, John A, Benson, Helen E, Faccenda, Elena, Pawson, Adam J, Sharman, Joanna L, Southan, Christopher, Buneman, Peter O, Catterall, William A, Cidlowski, John A, Davenport, Anthony P, Fabbro, Doriano, Fan, Grace, McGrath, John C, Spedding, Michael, Davies, Jamie A, Aldrich, R, Attali, B, Bäck, M l, Barnes, N M, Bathgate, R, Beart, P M, Becirovic, E, Biel, M, Birdsall, N J, Boison, D, Bräuner-Osborne, H, Bröer, S, Bryant, C, Burnstock, G, Burris, T, Cain, D, Calo, G, Chan, S L, Chandy, K G, Chiang, N, Christakos, S, Christopoulos, A, Chun, J J, Chung, J-J, Clapham, D E, Connor, M A, Coons, L, Cox, H M, Dautzenberg, F M, Dent, G, Douglas, S D, Dubocovich, M L, Edwards, D P, Farndale, R, Fong, T M, Forrest, D, Fowler, C J, Fuller, P, Gainetdinov, R R, Gershengorn, M A, Goldin, A, Goldstein, S AN, Grimm, S L, Grissmer, S, Gundlach, A L, Hagenbuch, B, Hammond, J R, Hancox, J C, Hartig, S, Hauger, R L, Hay, D L, Hébert, T, Hollenberg, A N, Holliday, N D, Hoyer, D, Ijzerman, A P, Inui, K I, Ishii, S, Jacobson, K A, Jan, L Y, Jarvis, G E, Jensen, R, Jetten, A, Jockers, R, Kaczmarek, L K, Kanai, Y, Kang, H S, Karnik, S, Kerr, I D, Korach, K S, Lange, C A, Larhammar, D, Leeb-Lundberg, F, Leurs, R, Lolait, S J, Macewan, D, Maguire, J J, May, J M, Mazella, J, Mcardle, C A, Mcdonnell, D P, Michel, M C, Miller, L J, Mitolo, V, Monie, T, Monk, P N, Mouillac, B, Murphy, P M, Nahon, J-L, Nerbonne, J, Nichols, C G, Norel, X, Oakley, R, Offermanns, S, Palmer, L G, Panaro, M A, Perez-Reyes, E, Pertwee, R G, Pike, J W, Pin, J P, Pintor, S, Plant, L D, Poyner, D R, Prossnitz, E R, Pyne, S, Ren, D, Richer, J K, Rondard, P, Ross, R A, Sackin, H, Safi, R, Sanguinetti, M C, Sartorius, C A, Segaloff, D L, Sladek, F M, Stewart, G, Stoddart, L A, Striessnig, J, Summers, R J, Takeda, Y, Tetel, M, Toll, L, Trimmer, J S, Tsai, M-J, Tsai, S Y, Tucker, S, Usdin, T B, Vilargada, J-P, Vore, M, Ward, D T, Waxman, S G, Webb, P, Wei, A D, Weigel, N, Willars, G B, Winrow, C, Wong, S S, Wulff, H, Ye, R D, Young, M, and Zajac, J-M

Published
2015
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10. THE CONCISE GUIDE TO PHARMACOLOGY 2017/18: Overview

Author

Alexander, Stephen PH, Kelly, Eamonn, Marrion, Neil V, Peters, John A, Faccenda, Elena, Harding, Simon D, Pawson, Adam J, Sharman, Joanna L, Southan, Christopher, Buneman, O Peter, Cidlowski, John A, Christopoulos, Arthur, Davenport, Anthony P, Fabbro, Doriano, Spedding, Michael, Striessnig, Jörg, Davies, Jamie A, Abbracchio, M. -P., Aldrich, R., Al-Hosaini, K., Arumugam, T. V., Attali, B., Bäck, M., Barnes, N. M., Bathgate, R., Beart, P. M., Becirovic, E., Bettler, B., Biel, M., Birdsall, N. J., Blaho, V., Boison, D., Bräuner-osborne, H., Bröer, S., Bryant, C., Burnstock, G., Calo, G., Catterall, W. A., Ceruti, S., Chan, S. L., Chandy, K. G., Chazot, P., Chiang, N., Chun, J. J., Chung, J. -J., Clapham, D. E., Clapp, L., Connor, M. A., Cox, H. M., Davies, P., Dawson, P. A., Decaen, P., Dent, G., Doherty, P., Douglas, S. D., Dubocovich, M. L., Fong, T. M., Fowler, C. J., Frantz, A., Fuller, P., Fumagalli, M., Futerman, A. H., Gainetdinov, R. R., Gershengorn, M. A., Goldin, A., Goldstein, S. A. N., Goudet, C., Gregory, K., Grissmer, S., Gundlach, A. L., Hagenbuch, B., Hamann, J., Hammond, J. R., Hancox, J. C., Hanson, J., Hanukoglu, I., Hay, D. L., Hobbs, A. J., Hollenberg, A. N., Holliday, N. D., Hoyer, D., Ijzerman, A. P., Inui, K. I., Irving, A. J., Ishii, S., Jacobson, K. A., Jan, L. Y., Jarvis, M. F., Jensen, R., Jockers, R., Kaczmarek, L. K., Kanai, Y., Karnik, S., Kellenberger, S., Kemp, S., Kennedy, C., Kerr, I. D., Kihara, Y., Kukkonen, J., Larhammar, D., Leach, K., Lecca, D., Leeman, S., Leprince, J., Lolait, S. J., Macewan, D., Maguire, J. J., Marshall, F., Mazella, J., Mcardle, C. A., Michel, M. C., Miller, L. J., Mitolo, V., Mizuno, H., Monk, P. N., Mouillac, B., Murphy, P. M., Nahon, J. -L., Nerbonne, J., Nichols, C. G., Norel, X., Offermanns, S., Palmer, L. G., Panaro, M. A., Papapetropoulos, A., Perez-reyes, E., Pertwee, R. G., Pintor, S., Pisegna, J. R., Plant, L. D., Poyner, D. R., Prossnitz, E. R., Pyne, S., Ramachandran, R., Ren, D., Rondard, P., Ruzza, C., Sackin, H., Sanger, G., Sanguinetti, M. C., Schild, L., Schiöth, H., Schulte, G., Schulz, S., Segaloff, D. L., Serhan, C. N., Singh, K. D., Slesinger, P. A., Snutch, T. P., Sobey, C. G., Stewart, G., Stoddart, L. A., Summers, R. J., Szabo, C., Thwaites, D., Toll, L., Trimmer, J. S., Tucker, S., Vaudry, H., Verri, T., Vilargada, J. -P., Waldman, S. A., Ward, D. T., Waxman, S. G., Wei, A. D., Willars, G. B., Wong, S. S., Woodruff, T. M., Wulff, H., Ye, R. D., Yung, Y., Zajac, J. -M., Alexander, Stephen PH, Kelly, Eamonn, Marrion, Neil V, Peters, John A, Faccenda, Elena, Harding, Simon D, Pawson, Adam J, Sharman, Joanna L, Southan, Christopher, Buneman, O Peter, Cidlowski, John A, Christopoulos, Arthur, Davenport, Anthony P, Fabbro, Doriano, Spedding, Michael, Striessnig, Jörg, Davies, Jamie A, Abbracchio, M. -P., Aldrich, R., Al-Hosaini, K., Arumugam, T. V., Attali, B., Bäck, M., Barnes, N. M., Bathgate, R., Beart, P. M., Becirovic, E., Bettler, B., Biel, M., Birdsall, N. J., Blaho, V., Boison, D., Bräuner-osborne, H., Bröer, S., Bryant, C., Burnstock, G., Calo, G., Catterall, W. A., Ceruti, S., Chan, S. L., Chandy, K. G., Chazot, P., Chiang, N., Chun, J. J., Chung, J. -J., Clapham, D. E., Clapp, L., Connor, M. A., Cox, H. M., Davies, P., Dawson, P. A., Decaen, P., Dent, G., Doherty, P., Douglas, S. D., Dubocovich, M. L., Fong, T. M., Fowler, C. J., Frantz, A., Fuller, P., Fumagalli, M., Futerman, A. H., Gainetdinov, R. R., Gershengorn, M. A., Goldin, A., Goldstein, S. A. N., Goudet, C., Gregory, K., Grissmer, S., Gundlach, A. L., Hagenbuch, B., Hamann, J., Hammond, J. R., Hancox, J. C., Hanson, J., Hanukoglu, I., Hay, D. L., Hobbs, A. J., Hollenberg, A. N., Holliday, N. D., Hoyer, D., Ijzerman, A. P., Inui, K. I., Irving, A. J., Ishii, S., Jacobson, K. A., Jan, L. Y., Jarvis, M. F., Jensen, R., Jockers, R., Kaczmarek, L. K., Kanai, Y., Karnik, S., Kellenberger, S., Kemp, S., Kennedy, C., Kerr, I. D., Kihara, Y., Kukkonen, J., Larhammar, D., Leach, K., Lecca, D., Leeman, S., Leprince, J., Lolait, S. J., Macewan, D., Maguire, J. J., Marshall, F., Mazella, J., Mcardle, C. A., Michel, M. C., Miller, L. J., Mitolo, V., Mizuno, H., Monk, P. N., Mouillac, B., Murphy, P. M., Nahon, J. -L., Nerbonne, J., Nichols, C. G., Norel, X., Offermanns, S., Palmer, L. G., Panaro, M. A., Papapetropoulos, A., Perez-reyes, E., Pertwee, R. G., Pintor, S., Pisegna, J. R., Plant, L. D., Poyner, D. R., Prossnitz, E. R., Pyne, S., Ramachandran, R., Ren, D., Rondard, P., Ruzza, C., Sackin, H., Sanger, G., Sanguinetti, M. C., Schild, L., Schiöth, H., Schulte, G., Schulz, S., Segaloff, D. L., Serhan, C. N., Singh, K. D., Slesinger, P. A., Snutch, T. P., Sobey, C. G., Stewart, G., Stoddart, L. A., Summers, R. J., Szabo, C., Thwaites, D., Toll, L., Trimmer, J. S., Tucker, S., Vaudry, H., Verri, T., Vilargada, J. -P., Waldman, S. A., Ward, D. T., Waxman, S. G., Wei, A. D., Willars, G. B., Wong, S. S., Woodruff, T. M., Wulff, H., Ye, R. D., Yung, Y., and Zajac, J. -M.

Subjects
Pharmacology
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

12. Modulation of Glucagon Receptor Pharmacology by Receptor Activity-modifying Protein-2 (RAMP2)

Author

Weston, C., Lu, J., Li, N., Barkan, K., Richards, G.O., Roberts, D.J., Skerry, T.M., Poyner, D., Pardamwar, M., Reynolds, C.A., Dowell, S.J., Willars, G.B., and Ladds, G.

Subjects
endocrine system, digestive, oral, and skin physiology, hormones, hormone substitutes, and hormone antagonists
Abstract

The glucagon and glucagon-like peptide-1 (GLP-1) receptors\ud play important, opposing roles in regulating blood glucose levels.\ud Consequently, these receptors have been identified as targets\ud for novel diabetes treatments. However, drugs acting at the\ud GLP-1 receptor, although having clinical efficacy, have been\ud associated with severe adverse side-effects, and targeting of the\ud glucagon receptor has yet to be successful. Here we use a combination\ud of yeast reporter assays and mammalian systems to\ud provide a more complete understanding of glucagon receptor\ud signaling, considering the effect of multiple ligands, association\ud with the receptor-interacting protein receptor activity-modifying\ud protein-2 (RAMP2), and the role of individual G protein\ud -subunits. We demonstrate that RAMP2 alters both ligand\ud selectivity and G protein preference of the glucagon receptor.\ud Importantly, we also uncover novel cross-reactivity of therapeutically\ud used GLP-1 receptor ligands at the glucagon receptor that\ud is abolished by RAMP2 interaction. This study reveals the glucagon\ud receptor as a previously unidentified target for GLP-1\ud receptor agonists and highlights a role for RAMP2 in regulating\ud its pharmacology. Such previously unrecognized functions of\ud RAMPs highlight the need to consider all receptor-interacting\ud proteins in future drug development.\ud

Published
2015

13. Receptor activity modifying proteins (RAMPs) interact with the VPAC 2 receptor and CRF 1 receptors and modulate their function: RAMP interactions with VPAC2and CRF1receptors

Author

Barwell, J., Caron, K. M., Lindmark, H., Poyner, D. R., Wootten, D., Drmota, T., Kadmiel, M., and Willcockson, H.

Subjects
endocrine system, hormones, hormone substitutes, and hormone antagonists
Abstract

Although it is established that the receptor activity modifying proteins (RAMPs) can interact with a number of GPCRs, little is known about the consequences of these interactions. Here the interaction of RAMPs with the glucagon-like peptide 1 receptor (GLP-1 receptor), the human vasoactive intestinal polypeptide/pituitary AC-activating peptide 2 receptor (VPAC2) and the type 1 corticotrophin releasing factor receptor (CRF1) has been examined.

Published
2013
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14. Investigating G protein signalling bias at the glucagon-like peptide-1 receptor in yeast

Author

Weston, C., Poyner, D., Patel, V., Dowell, S., Ladds, G., Weston, C., Poyner, D., Patel, V., Dowell, S., and Ladds, G.

Abstract

Background and Purpose The glucagon-like peptide 1 (GLP-1) receptor performs an important role in glycaemic control, stimulating the release of insulin. It is an attractive target for treating type 2 diabetes. Recently, several reports of adverse side effects following prolonged use of GLP-1 receptor therapies have emerged: most likely due to an incomplete understanding of signalling complexities. Experimental Approach We describe the expression of the GLP-1 receptor in a panel of modified yeast strains that couple receptor activation to cell growth via single Gα/yeast chimeras. This assay enables the study of individual ligand-receptor G protein coupling preferences and the quantification of the effect of GLP-1 receptor ligands on G protein selectivity. Key Results The GLP-1 receptor functionally coupled to the chimeras representing the human Gαs, Gαi and Gαq subunits. Calculation of the dissociation constant for a receptor antagonist, exendin-3 revealed no significant difference between the two systems. We obtained previously unobserved differences in G protein signalling bias for clinically relevant therapeutic agents, liraglutide and exenatide; the latter displaying significant bias for the Gαi pathway. We extended the use of the system to investigate small-molecule allosteric compounds and the closely related glucagon receptor. Conclusions and Implications These results provide a better understanding of the molecular events involved in GLP-1 receptor pleiotropic signalling and establish the yeast platform as a robust tool to screen for more selective, efficacious compounds acting at this important class of receptors in the future.

Published
2014

23. The interaction of CGRP with its receptors

Author

Poyner, D. R., primary, Conner, A. C., additional, Howitt, S. G., additional, Hay, D. L., additional, Langel, U., additional, Kilk, K., additional, Smith, D. M., additional, and Wheatley, M., additional

Published
2002
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29. ChemInform Abstract: Synthesis and Iron Binding Studies of myo‐Inositol 1,2,3‐Trisphosphate and (.+‐.)‐myo‐Inositol 1,2‐Bisphosphate, and Iron Binding Studies of All myo‐Inositol Tetrakisphosphates.

Author

SPIERS, I. D., primary, BARKER, C. J., additional, CHUNG, S.‐K., additional, CHANG, Y.‐T., additional, FREEMAN, S., additional, GARDINER, J. M., additional, HIRST, P. H., additional, LAMBERT, P. A., additional, MICHELL, R. H., additional, POYNER, D. R., additional, SCHWALBE, C. H., additional, SMITH, A. W., additional, and SOLOMONS, K. R. H., additional

Published
1996
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42. A nonantisense sequence-selective effect of a phosphorothioate oligodeoxynucleotide directed against the epidermal growth factor receptor in A431 cells.

Author

Coulson, J M, Poyner, D R, Chantry, A, Irwin, W J, and Akhtar, S

Abstract

The overexpression of epidermal growth factor receptor (EGFr) has been implicated as a causative factor and a poor prognostic marker in a number of carcinomas. Therefore, strategies that down-regulate EGFr expression may be therapeutically useful. We designed antisense ODNs complementary to the initiation codon region of the EGFr mRNA and evaluated their efficacy in several tumor-derived cells, including the A431 cell line, that express amplified levels of EGFr. A 15-mer phosphorothioate (PS) antisense ODN (erbB1AS15) induced a concentration-dependent reduction in proliferation that was accompanied by a change in the morphology of A431 cells into more tightly clustered and discrete colonies. A 15-mer sense (PS) control oligodeoxynucleotide (ODN) and a phosphodiester (PO) version of erbB1AS15 had little or no effect on cell number of morphology, and erbB1AS15 (PS) did not induce these effects in control cell lines expressing lower levels of EGFr. The effects of erbB1AS15 (PS) on A431 cells were not mediated by a true antisense mechanism in that there was no reduction in the level of EGFr mRNA or protein over a 24-hr period, as determined by Northern and Western blotting, respectively. However, autophosphorylation of the receptor was significantly reduced by erbB1AS15 (PS) and not by control ODNs. The results of further studies suggested that this effect was mediated by a direct, dose-dependent inhibition of the EGFr tyrosine kinase enzyme and was not due to impairment of either ligand-binding or receptor dimerization. These data suggest that erbB1AS15 (PS) can inhibit proliferation and alter the morphology of A431 cells by a sequence-selective, but nonantisense, mechanism affecting receptor tyrosine kinase activity.

Published
1996

43. Propylbenzilylcholine Mustard Labels an Acidic Residue in Transmembrane Helix 3 of the Muscarinic Receptor

Author

Curtis, C A M, Wheatley, M, Bansal, S, Birdsall, N J M, Eveleigh, P, Pedder, E K, Poyner, D, and Hulme, E C

Abstract

Muscarinic acetylcholine receptors were purified from rat forebrain and labeled with [3H]N-(2-chloroethyl)N- (2′,3′ - [3H2]propyl) - 2 - aminoethylbenzilate. Cleavage of the labeled muscarinic acetylcholine receptors with a lysine-specific protease yielded labeled, glycosylated peptides about 130 and 200 residues in length, which came from different receptor sequences. The probable cleavage sites are in the second intracellular loop and in the second extracellular or third intracellular loop. The N-terminal 130 residues are disulfide-bonded to another part of the receptor structure, supporting the presence of a link between the second and third extracellular loops. The [3H]propylbenzilylcholine mustard-receptor link is cleaved by nucleophiles, acids, and bases under denaturing conditions, suggesting modification of an acidic residue. Cyanogen bromide cleavage points to transmembrane helix 3 as the site of label attachment.

Published
1989
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44. Stimulation of adenylate cyclase by amylin in CHO-K1 cells.

Author

D'Santos, C S, Gatti, A, Poyner, D R, and Hanley, M R

Abstract

The CHO-K1 cell line responds to the peptide amylin by a rapid elevation of cAMP. The related peptide calcitonin gene-related peptide (CGRP) is 100 times less potent at stimulating adenylate cyclase than is amylin. The actions of amylin at this receptor are concentration dependent and not antagonized by the CGRP antagonist CGRP-(8-37). Although these cells have receptors for calcitonin, amylin is unable to take part in any high affinity interaction with these receptors, as assessed by radioligand binding. The CHO-K1 cell line has receptors for amylin that are distinct from those for calcitonin and CGRP.

Published
1992

45. Binding and hydrodynamic properties of muscarinic receptor subtypes solubilized in 3-(3-cholamidopropyl)dimethylammonio-2-hydroxy-1-propanesulfonate.

Author

Poyner, D R, Birdsall, N J, Curtis, C, Eveleigh, P, Hulme, E C, Pedder, E K, and Wheatley, M

Abstract

The muscarinic receptor from the cerebral cortex, heart, and lacrimal gland can be solubilized in the zwitterionic detergent 3-(3-cholamidopropyl)dimethylammonio-2-hydroxy-1-propane sulfonate (CHAPSO) with retention of high affinity [3H]N-methyls-copolamine binding. However, in this detergent there are significant differences in the binding properties of the receptors, compared with those observed in membranes and digitonin solution. Some agents retain a degree of selectivity. In the heart and cortex, agonists can bind with high affinity to a receptor-GTP-binding protein complex. A second, lower affinity, agonist binding state is also present, which resembles a class of sites seen in membranes but not in digitonin solution. The high affinity agonist binding state has been resolved from the lower affinity state on sucrose density gradient centrifugation. Hydrodynamic analysis suggests that the high affinity state is approximately 110,000 Da larger than the lower affinity state. The binding properties of the receptor in CHAPSO can be altered to those seen in digitonin by exchanging detergents after CHAPSO solubilization.

Published
1989

48. Propylbenzilylcholine mustard labels an acidic residue in transmembrane helix 3 of the muscarinic receptor

Author

Ca, Curtis, Mark Wheatley, Bansal S, Nj, Birdsall, Eveleigh P, Ek, Pedder, Poyner D, and Ec, Hulme

Subjects
Kinetics, Protein Conformation, Cell Membrane, Chromatography, Gel, Animals, Brain, Cyanogen Bromide, Receptors, Muscarinic, Peptide Fragments, Propylbenzilylcholine Mustard, Choline, Rats
Abstract

Muscarinic acetylcholine receptors were purified from rat forebrain and labeled with [3H]N-(2-chloroethyl)N-(2',3'-[3H2]propyl)-2-aminoethylbenzilate. Cleavage of the labeled muscarinic acetylcholine receptors with a lysine-specific protease yielded labeled, glycosylated peptides about 130 and 200 residues in length, which came from different receptor sequences. The probable cleavage sites are in the second intracellular loop and in the second extracellular or third intracellular loop. The N-terminal 130 residues are disulfide-bonded to another part of the receptor structure, supporting the presence of a link between the second and third extracellular loops. The [3H]propylbenzilylcholine mustard-receptor link is cleaved by nucleophiles, acids, and bases under denaturing conditions, suggesting modification of an acidic residue. Cyanogen bromide cleavage points to transmembrane helix 3 as the site of label attachment.

Published
1989

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