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2. Evolutionary and biomedical implications of sex differences in the primate brain transcriptome

Author

DeCasien, Alex R., Chiou, Kenneth L., Testard, Camille, Mercer, Arianne, Negrón-Del Valle, Josué E., Bauman Surratt, Samuel E., González, Olga, Stock, Michala K., Ruiz-Lambides, Angelina V., Martínez, Melween I., Antón, Susan C., Walker, Christopher S., Sallet, Jérôme, Wilson, Melissa A., Brent, Lauren J.N., Montague, Michael J., Sherwood, Chet C., Platt, Michael L., Higham, James P., and Snyder-Mackler, Noah

Published
2024
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3. Multiregion transcriptomic profiling of the primate brain reveals signatures of aging and the social environment

Author

Chiou, Kenneth L., DeCasien, Alex R., Rees, Katherina P., Testard, Camille, Spurrell, Cailyn H., Gogate, Aishwarya A., Pliner, Hannah A., Tremblay, Sébastien, Mercer, Arianne, Whalen, Connor J., Negrón-Del Valle, Josué E., Janiak, Mareike C., Bauman Surratt, Samuel E., González, Olga, Compo, Nicole R., Stock, Michala K., Ruiz-Lambides, Angelina V., Martínez, Melween I., Wilson, Melissa A., Melin, Amanda D., Antón, Susan C., Walker, Christopher S., Sallet, Jérôme, Newbern, Jason M., Starita, Lea M., Shendure, Jay, Higham, James P., Brent, Lauren J. N., Montague, Michael J., Platt, Michael L., and Snyder-Mackler, Noah

Published
2022
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4. Tirzepatide, GIP(1-42) and GIP(1-30) display unique signaling profiles at two common GIP receptor variants, E354 and Q354.

Author

Rees, Tayla A., Buttle, Benjamin J., Tasma, Zoe, Sung-Hyun Yang, Harris, Paul W. R., and Walker, Christopher S.

Subjects
GASTRIC inhibitory polypeptide, G protein coupled receptors, TYPE 2 diabetes, BODY mass index, METABOLIC disorders
Abstract

Type 2 diabetes (T2D) and obesity are prevalent metabolic disorders affecting millions of individuals worldwide. A new effective therapeutic drug called tirzepatide for the treatment of obesity and T2D is a dual agonist of the GIP receptor and GLP-1 receptor. Tirzepatide is clinically more effective than GLP-1 receptor agonists but the reasons why are not well understood. Tirzepatide reportedly stimulates the GIP receptor more potently than the GLP-1 receptor. However, tirzepatide signaling has not been thoroughly investigated at the E354 (wildtype) or Q354 (E354Q) GIP receptor variants. The E354Q variant is associated increased risk of T2D and lower body mass index. To better understand GIP receptor signaling we characterized the activity of endogenous agonists and tirzepatide at both GIP receptor variants. Using Cos7 cells we examined wildtype and E354Q GIP receptor signaling, analyzing cAMP and IP¹ accumulation as well as AKT, ERK1/2 and CREB phosphorylation. GIP(1-42) and GIP(1-30)NH2 displayed equipotent effects on these pathways excluding CREB phosphorylation where GIP(1-30)NH2 was more potent than GIP(1-42) at the E354Q GIP receptor. Tirzepatide favored cAMP signaling at both variants. These findings indicate that tirzepatide is a biased agonist towards Gas signaling and suggests it equally activates the wildtype and E354Q GIP receptor variants. We also observed differences between the pharmacology of the GIP receptor variants with endogenous peptides, which may help to explain differences in phenotype. These findings contribute to a comprehensive understanding of GIP receptor signaling, and will aid development of therapies combating T2D and obesity. [ABSTRACT FROM AUTHOR]

Published
2024
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5. Extracellular bimolecular fluorescence complementation for investigating membrane protein dimerization: a proof of concept using class B GPCRs.

Author

Garelja, Michael L., Alexander, Tyla I., Walker, Christopher S., and Hay, Debbie L.

Subjects
CELL receptors, FLUORESCENT proteins, FLUORESCENCE yield, CALCITONIN receptors, CALCITONIN gene-related peptide
Abstract

Bimolecular fluorescence complementation (BiFC) methodology uses split fluorescent proteins to detect interactions between proteins in living cells. To date, BiFC has been used to investigate receptor dimerization by splitting the fluorescent protein between the intracellular portions of different receptor components. We reasoned that attaching these split proteins to the extracellular N-terminus instead may improve the flexibility of this methodology and reduce the likelihood of impaired intracellular signal transduction. As a proof-of-concept, we used receptors for calcitonin gene-related peptide, which comprise heterodimers of either the calcitonin or calcitonin receptor-like receptor in complex with an accessory protein (receptor activity-modifying protein 1). We created fusion constructs in which split mVenus fragments were attached to either the C-termini or N-termini of receptor subunits. The resulting constructs were transfected into Cos7 and HEK293S cells, where we measured cAMP production in response to ligand stimulation, cell surface expression of receptor complexes, and BiFC fluorescence. Additionally, we investigated ligand-dependent internalization in HEK293S cells. We found N-terminal fusions were better tolerated with regards to cAMP signaling and receptor internalization. N-terminal fusions also allowed reconstitution of functional fluorescent mVenus proteins; however, fluorescence yields were lower than with C-terminal fusion. Our results suggest that BiFC methodologies can be applied to the receptor N-terminus, thereby increasing the flexibility of this approach, and enabling further insights into receptor dimerization. [ABSTRACT FROM AUTHOR]

Published
2024
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8. Homo naledi, a new species of the genus Homo

Author

Krause, Johannes, Conard, Nicholas J, Berger, Lee R, Hawks, John, de Ruiter, Darryl J, Churchill, Steven E, Schmid, Peter, Delezene, Lucas K, Kivell, Tracy L, Garvin, Heather M, Williams, Scott A, DeSilva, Jeremy M, Skinner, Matthew M, Musiba, Charles M, Cameron, Noel, Holliday, Trenton W, Harcourt-Smith, William, Ackermann, Rebecca R, Bastir, Markus, Bogin, Barry, Bolter, Debra, Brophy, Juliet, Cofran, Zachary D, Congdon, Kimberly A, Deane, Andrew S, Dembo, Mana, Drapeau, Michelle, Elliott, Marina C, Feuerriegel, Elen M, Green, David J, Gurtov, Alia, Irish, Joel D, Kruger, Ashley, Laird, Myra F, Marchi, Damiano, Meyer, Marc R, Nalla, Shahed, Negash, Enquye W, Orr, Caley M, Radovcic, Davorka, Schroeder, Lauren, Scott, Jill E, Throckmorton, Zachary, Tocheri, Matthew W, VanSickle, Caroline, Walker, Christopher S, Wei, Pianpian, Zipfel, Bernhard, García Martínez, Daniel, Krause, Johannes, Conard, Nicholas J, Berger, Lee R, Hawks, John, de Ruiter, Darryl J, Churchill, Steven E, Schmid, Peter, Delezene, Lucas K, Kivell, Tracy L, Garvin, Heather M, Williams, Scott A, DeSilva, Jeremy M, Skinner, Matthew M, Musiba, Charles M, Cameron, Noel, Holliday, Trenton W, Harcourt-Smith, William, Ackermann, Rebecca R, Bastir, Markus, Bogin, Barry, Bolter, Debra, Brophy, Juliet, Cofran, Zachary D, Congdon, Kimberly A, Deane, Andrew S, Dembo, Mana, Drapeau, Michelle, Elliott, Marina C, Feuerriegel, Elen M, Green, David J, Gurtov, Alia, Irish, Joel D, Kruger, Ashley, Laird, Myra F, Marchi, Damiano, Meyer, Marc R, Nalla, Shahed, Negash, Enquye W, Orr, Caley M, Radovcic, Davorka, Schroeder, Lauren, Scott, Jill E, Throckmorton, Zachary, Tocheri, Matthew W, VanSickle, Caroline, Walker, Christopher S, Wei, Pianpian, Zipfel, Bernhard, and García Martínez, Daniel

Abstract

Homo naledi es una especie previamente desconocida de homínido extinto descubierta dentro de la Cámara Dinaledi del sistema de cuevas Rising Star, en el Cradle of Humankind, Sudáfrica. Esta especie se caracteriza por tener una masa corporal y estatura similar a las poblaciones humanas de cuerpo pequeño, pero un volumen endocraneal pequeño similar al de los australopitecos. La morfología craneal de H. naledi es única, pero se asemeja más a las especies tempranas de Homo, incluyendo Homo erectus, Homo habilis o Homo rudolfensis. Aunque primitiva, la dentición es generalmente pequeña y simple en su morfología oclusal. H. naledi presenta adaptaciones manipulativas de la mano y la muñeca similares a las humanas. También exhibe un pie y miembro inferior similares a los humanos. Estos aspectos humanos se contrastan en el postcráneo con un tronco, hombro, pelvis y fémur proximal más primitivos o similares a los australopitecos. Representando al menos 15 individuos con la mayoría de los elementos esqueléticos repetidos múltiples veces, esta es la mayor colección de una sola especie de homínidos descubierta en África., National Geographic Society, The National Research Foundation of South Africa (WARF), The Palaeontological Scientific Trust, Lyda Hill Foundation, Wisconsin Alumni Research Foundation (WARF), Texas A and M University, Depto. de Biodiversidad, Ecología y Evolución, Fac. de Ciencias Biológicas, TRUE, pub

Published
2024
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10. Pharmacology of PACAP and VIP receptors in the spinal cord highlights the importance of the PAC1 receptor.

Author

Tasma, Zoe, Rees, Tayla A., Guo, Song, Tan, Sheryl, O'Carroll, Simon J., Faull, Richard L. M., Curtis, Maurice A., Christensen, Sarah L., Hay, Debbie L., and Walker, Christopher S.

Subjects
SPINAL cord, PITUITARY adenylate cyclase activating polypeptide, NOCICEPTIN, G protein coupled receptors, VASOACTIVE intestinal peptide, PEPTIDES, CELLULAR signal transduction
Abstract

Background and Purpose: The spinal cord is a key structure involved in the transmission and modulation of pain. Pituitary adenylate cyclase‐activating peptide (PACAP) and vasoactive intestinal peptide (VIP), are expressed in the spinal cord. These peptides activate G protein‐coupled receptors (PAC1, VPAC1 and VPAC2) that could provide targets for the development of novel pain treatments. However, it is not clear which of these receptors are expressed within the spinal cord and how these receptors signal. Experimental Approach: Dissociated rat spinal cord cultures were used to examine agonist and antagonist receptor pharmacology. Signalling profiles were determined for five signalling pathways. The expression of different PACAP and VIP receptors was then investigated in mouse, rat and human spinal cords using immunoblotting and immunofluorescence. Key Results: PACAP, but not VIP, potently stimulated cAMP, IP1 accumulation and ERK and cAMP response element‐binding protein (CREB) but not Akt phosphorylation in spinal cord cultures. Signalling was antagonised by M65 and PACAP6–38. PACAP‐27 was more effectively antagonised than either PACAP‐38 or VIP. The patterns of PAC1 and VPAC2 receptor‐like immunoreactivity appeared to be distinct in the spinal cord. Conclusions and Implications: The pharmacological profile in the spinal cord suggested that a PAC1 receptor is the major functional receptor subtype present and thus likely mediates the nociceptive effects of the PACAP family of peptides in the spinal cord. However, the potential expression of both PAC1 and VPAC2 receptors in the spinal cord highlights that these receptors may play differential roles and are both possible therapeutic targets. [ABSTRACT FROM AUTHOR]

Published
2024
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11. RAMP and MRAP accessory proteins have selective effects on expression and signalling of the CB1, CB2, GPR18 and GPR55 cannabinoid receptors.

Author

Glenn, Nathaniel A. K., Finlay, David B., Carruthers, Emma R., Mountjoy, Kathleen G., Walker, Christopher S., and Grimsey, Natasha L.

Subjects
CANNABINOID receptors, G protein coupled receptors, MELANOCORTIN receptors, PEPTIDES, PROTEIN receptors, G proteins
Abstract

Background and Purpose: Receptor activity‐modifying proteins (RAMPs) and melanocortin receptor accessory proteins (MRAPs) modulate expression and signalling of calcitonin and melanocortin GPCRs. Interactions with other GPCRs have also been reported. The cannabinoid receptors, CB1 and CB2, and two putative cannabinoid receptors, GPR18 and GPR55, exhibit substantial intracellular expression and there are discrepancies in ligand responsiveness between studies. We investigated whether interactions with RAMPs or MRAPs could explain these phenomena. Experimental Approach: Receptors and accessory proteins were co‐expressed in HEK‐293 cells. Selected receptors were studied at basal expression levels and also with enhanced expression produced by incorporation of a preprolactin signal sequence/peptide (pplss). Cell surface and total expression of receptors and accessory proteins were quantified using immunocytochemistry. Signalling was measured using cAMP (CAMYEL) and G protein dissociation (TRUPATH Gα13) biosensors. Key Results: MRAP2 enhanced surface and total expression of GPR18. Pplss‐GPR18 increased detection of cell surface MRAP2. MRAP1α and MRAP2 reduced GPR55 surface and total expression, correlating with reduced constitutive, but not agonist‐induced, signalling. GPR55, pplss‐CB1 and CB2 reduced detection of MRAP1α at the cell surface. Pplss‐CB1 agonist potency was reduced by MRAP2 in Gα13 but not cAMP assays, consistent with MRAP2 reducing pplss‐CB1 expression. Some cannabinoid receptors increased RAMP2 or RAMP3 total expression without influencing surface expression. Conclusions and Implications: Mutual influences on expression and/or function for specific accessory protein‐receptor pairings raises the strong potential for physiological and disease‐relevant consequences. Sequestration and/or hetero‐oligomerisation of cannabinoid receptors with accessory proteins is a possible novel mechanism for receptor crosstalk. LINKED ARTICLES: This article is part of a themed issue Therapeutic Targeting of G Protein‐Coupled Receptors: hot topics from the Australasian Society of Clinical and Experimental Pharmacologists and Toxicologists 2021 Virtual Annual Scientific Meeting. To view the other articles in this section visit http://onlinelibrary.wiley.com/doi/10.1111/bph.v181.14/issuetoc [ABSTRACT FROM AUTHOR]

Published
2024
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12. Class B GPCR: Receptors and RAMPs

Author

Gingell, Joseph J., Walker, Christopher S., Hay, Debbie L., Di Giovanni, Giuseppe, Editor-in-chief, Herrick-Davis, Katharine, editor, and Milligan, Graeme, editor

Published
2017
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14. Pharmacological characterisation of erenumab, Aimovig, at two calcitonin gene‐related peptide responsive receptors.

Author

Garelja, Michael L., Alexander, Tyla I., Bennie, Amy, Nimick, Mhairi, Petersen, Jakeb, Walker, Christopher S., and Hay, Debbie L.

Subjects
CALCITONIN gene-related peptide, ERENUMAB, PEPTIDE receptors, CALCITONIN receptors, MONOCLONAL antibodies
Abstract

Background and Purpose: Calcitonin gene‐related peptide (CGRP) is involved in migraine pathophysiology. CGRP can signal through two receptors. The canonical CGRP receptor comprises the calcitonin receptor‐like receptor and receptor activity‐modifying protein 1 (RAMP1); the AMY1 receptor comprises the calcitonin receptor with RAMP1. Drugs that reduce CGRP activity, such as receptor antagonists, are approved for the treatment and prevention of migraine. Despite being designed to target the canonical CGRP receptor, emerging evidence suggests that these antagonists, including erenumab (a monoclonal antibody antagonist) can also antagonise the AMY1 receptor. However, it is difficult to estimate its selectivity because direct comparisons between receptors under matched conditions have not been made. We therefore characterised erenumab at both CGRP‐responsive receptors with multiple ligands, including αCGRP and βCGRP. Experimental Approach: Erenumab antagonism was quantified through IC50 and pKB experiments, measuring cAMP production. We used SK‐N‐MC cells which endogenously express the human CGRP receptor, and HEK293S and Cos7 cells transiently transfected to express either human CGRP or AMY1 receptors. Key Results: Erenumab antagonised both the CGRP and AMY1 receptors with an ~20–120‐fold preference for the CGRP receptor, depending on the cells, agonist, analytical approach and/or assay format. Erenumab antagonised both forms of CGRP equally, and appeared to act as a competitive reversible antagonist at both receptors. Conclusion and Implications: Despite being designed to target the CGRP receptor, erenumab can antagonise the AMY1 receptor. Its ability to antagonise CGRP activity at both receptors may be useful in better understanding the clinical profile of erenumab. [ABSTRACT FROM AUTHOR]

Published
2024
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17. The Concise Guide to PHARMACOLOGY 2023/24 : G protein-coupled receptors

Author

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

Author

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

21. Characterization of Antibodies against Receptor Activity-Modifying Protein 1 (RAMP1): A Cautionary Tale

Author

Hendrikse, Erica R., primary, Rees, Tayla A., additional, Tasma, Zoe, additional, Garelja, Michael L., additional, Siow, Andrew, additional, Harris, Paul W. R., additional, Pawlak, John B., additional, Caron, Kathleen M., additional, Blakeney, Elizabeth S., additional, Russo, Andrew F., additional, Sowers, Levi P., additional, Lutz, Thomas A., additional, Le Foll, Christelle, additional, Walker, Christopher S., additional, and Hay, Debbie L., additional

Published
2022
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27. Calcitonin receptor antibody validation and expression in the rodent brain

Author

Hendrikse, Erica R, Rees, Tayla A, Tasma, Zoe, Le Foll, Christelle, Lutz, Thomas A, Siow, Andrew, Wookey, Peter J, Walker, Christopher S, Hay, Debbie L, University of Zurich, and Hay, Debbie L

Subjects
Calcitonin Gene-Related Peptide, Migraine Disorders, Brain, General Medicine, Receptors, Calcitonin, 10081 Institute of Veterinary Physiology, Receptors, Islet Amyloid Polypeptide, Islet Amyloid Polypeptide, Rats, Mice, 2728 Neurology (clinical), Animals, 570 Life sciences, biology, Neurology (clinical), hormones, hormone substitutes, and hormone antagonists, Receptors, Calcitonin Gene-Related Peptide
Abstract

Background and aim Therapeutics that reduce calcitonin gene-related peptide activity are effective migraine treatments. However, gaps remain in our understanding of the molecular mechanisms that link calcitonin gene-related peptide to migraine. The amylin 1 receptor responds potently to calcitonin gene-related peptide, and to the related peptide amylin, but its role in relation to either peptide or to migraine is unclear. We sought to better understand the expression of the amylin 1 receptor protein subunit, the calcitonin receptor, in the rodent brain. Methods We profiled three antibodies for immunodetection of calcitonin receptor, using immunocytochemistry, western blotting, and calcitonin receptor conditional knockout mouse tissue. Selected migraine-relevant rat brain regions were then examined for calcitonin receptor-like immunoreactivity. Results All three antibodies detected calcitonin receptor protein but only one (188/10) produced robust immunostaining in rodent brain, under the conditions used. Calcitonin receptor-like immunoreactivity was apparent in the rat brainstem and midbrain including the locus coeruleus, periaqueductal grey and spinal trigeminal nucleus. Conclusions Anti-calcitonin receptor antibodies require comprehensive profiling to ensure confidence in the detection of calcitonin receptor. Using a validated antibody, calcitonin receptor-like immunoreactivity was detected in several brain regions relevant to migraine. Further research is needed to understand the functional consequences of calcitonin receptor expression for calcitonin gene-related peptide or amylin physiology and pathophysiology.

Published
2022

28. Characterization of Antibodies against Receptor Activity-Modifying Protein 1 (RAMP1): A Cautionary Tale

Author

Hendrikse, Erica R; https://orcid.org/0000-0003-0763-5044, Rees, Tayla A, Tasma, Zoe; https://orcid.org/0000-0002-7652-6004, Garelja, Michael L; https://orcid.org/0000-0001-5332-1236, Siow, Andrew; https://orcid.org/0000-0002-0341-065X, Harris, Paul W R, Pawlak, John B; https://orcid.org/0000-0002-2407-2944, Caron, Kathleen M, Blakeney, Elizabeth S, Russo, Andrew F; https://orcid.org/0000-0002-8156-5649, Sowers, Levi P, Lutz, Thomas A; https://orcid.org/0000-0002-5056-8548, Le Foll, Christelle; https://orcid.org/0000-0002-6677-5488, Walker, Christopher S; https://orcid.org/0000-0001-8151-4123, Hay, Debbie L; https://orcid.org/0000-0002-9558-5122, Hendrikse, Erica R; https://orcid.org/0000-0003-0763-5044, Rees, Tayla A, Tasma, Zoe; https://orcid.org/0000-0002-7652-6004, Garelja, Michael L; https://orcid.org/0000-0001-5332-1236, Siow, Andrew; https://orcid.org/0000-0002-0341-065X, Harris, Paul W R, Pawlak, John B; https://orcid.org/0000-0002-2407-2944, Caron, Kathleen M, Blakeney, Elizabeth S, Russo, Andrew F; https://orcid.org/0000-0002-8156-5649, Sowers, Levi P, Lutz, Thomas A; https://orcid.org/0000-0002-5056-8548, Le Foll, Christelle; https://orcid.org/0000-0002-6677-5488, Walker, Christopher S; https://orcid.org/0000-0001-8151-4123, and Hay, Debbie L; https://orcid.org/0000-0002-9558-5122

Abstract

Calcitonin gene-related peptide (CGRP) is a key component of migraine pathophysiology, yielding effective migraine therapeutics. CGRP receptors contain a core accessory protein subunit: receptor activity-modifying protein 1 (RAMP1). Understanding of RAMP1 expression is incomplete, partly due to the challenges in identifying specific and validated antibody tools. We profiled antibodies for immunodetection of RAMP1 using Western blotting, immunocytochemistry and immunohistochemistry, including using RAMP1 knockout mouse tissue. Most antibodies could detect RAMP1 in Western blotting and immunocytochemistry using transfected cells. Two antibodies (844, ab256575) could detect a RAMP1-like band in Western blots of rodent brain but not RAMP1 knockout mice. However, cross-reactivity with other proteins was evident for all antibodies. This cross-reactivity prevented clear conclusions about RAMP1 anatomical localization, as each antibody detected a distinct pattern of immunoreactivity in rodent brain. We cannot confidently attribute immunoreactivity produced by RAMP1 antibodies (including 844) to the presence of RAMP1 protein in immunohistochemical applications in brain tissue. RAMP1 expression in brain and other tissues therefore needs to be revisited using RAMP1 antibodies that have been comprehensively validated using multiple strategies to establish multiple lines of convincing evidence. As RAMP1 is important for other GPCR/ligand pairings, our results have broader significance beyond the CGRP field.

Published
2022

33. Social connections predict brain structure in a multidimensional free-ranging primate society

Author

Testard, Camille, primary, Brent, Lauren J. N., additional, Andersson, Jesper, additional, Chiou, Kenneth L., additional, Negron-Del Valle, Josue E., additional, DeCasien, Alex R., additional, Acevedo-Ithier, Arianna, additional, Stock, Michala K., additional, Antón, Susan C., additional, Gonzalez, Olga, additional, Walker, Christopher S., additional, Foxley, Sean, additional, Compo, Nicole R., additional, Bauman, Samuel, additional, Ruiz-Lambides, Angelina V., additional, Martinez, Melween I., additional, Skene, J. H. Pate, additional, Horvath, Julie E., additional, Unit, Cayo Biobank Research, additional, Higham, James P., additional, Miller, Karla L., additional, Snyder-Mackler, Noah, additional, Montague, Michael J., additional, Platt, Michael L., additional, and Sallet, Jérôme, additional

Published
2022
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35. sj-pdf-1-cep-10.1177_03331024221084029 - Supplemental material for Calcitonin receptor antibody validation and expression in the rodent brain

Author

Hendrikse, Erica R, Rees, Tayla A, Tasma, Zoe, Le Foll, Christelle, Lutz, Thomas A, Siow, Andrew, Wookey, Peter J, Walker, Christopher S, and Hay, Debbie L

Subjects
FOS: Psychology, FOS: Clinical medicine, 170199 Psychology not elsewhere classified, 110319 Psychiatry (incl. Psychotherapy), 110306 Endocrinology, 111599 Pharmacology and Pharmaceutical Sciences not elsewhere classified, 110904 Neurology and Neuromuscular Diseases, Neuroscience
Abstract

Supplemental material, sj-pdf-1-cep-10.1177_03331024221084029 for Calcitonin receptor antibody validation and expression in the rodent brain by Erica R Hendrikse, Tayla A Rees, Zoe Tasma, Christelle Le Foll, Thomas A Lutz, Andrew Siow, Peter J Wookey, Christopher S Walker and Debbie L Hay: on behalf of the Hand Wrist Study Group in Cephalalgia

Published
2022
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36. Lipidated Calcitonin Gene-Related Peptide (CGRP) Peptide Antagonists Retain CGRP Receptor Activity and Attenuate CGRP Action In Vivo

Author

Jamaluddin, Aqfan, primary, Chuang, Chia-Lin, additional, Williams, Elyse T., additional, Siow, Andrew, additional, Yang, Sung Hyun, additional, Harris, Paul W. R., additional, Petersen, Jakeb S. S. M., additional, Bower, Rebekah L., additional, Chand, Shanan, additional, Brimble, Margaret A., additional, Walker, Christopher S., additional, Hay, Debbie L., additional, and Loomes, Kerry M., additional

Published
2022
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39. Sociality predicts individual variation in the immunity of free-ranging rhesus macaques

Author

Pavez-Fox, Melissa A., primary, Negron-Del Valle, Josue E., additional, Thompson, Indya J., additional, Walker, Christopher S., additional, Bauman, Samuel E., additional, Gonzalez, Olga, additional, Compo, Nicole, additional, Ruiz-Lambides, Angelina, additional, Martinez, Melween I., additional, Platt, Michael L., additional, Montague, Michael J., additional, Higham, James P., additional, Snyder-Mackler, Noah, additional, and Brent, Lauren J.N., additional

Published
2021
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42. Pharmacological characterisation of mouse calcitonin and calcitonin receptor‐like receptors reveals differences compared with human receptors

Author

Garelja, Michael L., primary, Bower, Rebekah L., additional, Brimble, Margaret A., additional, Chand, Shanan, additional, Harris, Paul W. R., additional, Jamaluddin, Muhammad Aqfan, additional, Petersen, Jakeb, additional, Siow, Andrew, additional, Walker, Christopher S., additional, and Hay, Debbie L., additional

Published
2021
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44. PAC 1 , VPAC 1 , and VPAC 2 Receptor Expression in Rat and Human Trigeminal Ganglia: Characterization of PACAP-Responsive Receptor Antibodies.

Author

Tasma, Zoe, Siow, Andrew, Harris, Paul W. R., Brimble, Margaret A., O'Carroll, Simon J., Hay, Debbie L., and Walker, Christopher S.

Subjects
RECEPTOR antibodies, CELL receptors, PEPTIDES, GANGLIA, PITUITARY adenylate cyclase activating polypeptide, SUMATRIPTAN
Abstract

Pituitary adenylate cyclase-activating peptide (PACAP) is a neuropeptide expressed in the trigeminal ganglia (TG). The TG conducts nociceptive signals in the head and may play roles in migraine. PACAP infusion provokes headaches in healthy individuals and migraine-like attacks in patients; however, it is not clear whether targeting this system could be therapeutically efficacious. To effectively target the PACAP system, an understanding of PACAP receptor distribution is required. Therefore, this study aimed to characterize commercially available antibodies and use these to detect PACAP-responsive receptors in the TG. Antibodies were initially validated in receptor transfected cell models and then used to explore receptor expression in rat and human TG. Antibodies were identified that could detect PACAP-responsive receptors, including the first antibody to differentiate between the PAC1n and PAC1s receptor splice variants. PAC1, VPAC1, and VPAC2 receptor-like immunoreactivity were observed in subpopulations of both neuronal and glial-like cells in the TG. In this study, PAC1, VPAC1, and VPAC2 receptors were detected in the TG, suggesting they are all potential targets to treat migraine. These antibodies may be useful tools to help elucidate PACAP-responsive receptor expression in tissues. However, most antibodies exhibited limitations, requiring the use of multiple methodologies and the careful inclusion of controls. [ABSTRACT FROM AUTHOR]

Published
2022
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45. THE CONCISE GUIDE TO PHARMACOLOGY 2021/22: G protein‐coupled receptors

Author

Alexander, Stephen P H, primary, Christopoulos, Arthur, additional, Davenport, Anthony P, additional, Kelly, Eamonn, additional, Mathie, Alistair, additional, Peters, John A, additional, Veale, Emma L, additional, Armstrong, Jane F, additional, Faccenda, Elena, additional, Harding, Simon D, additional, Pawson, Adam J, additional, Southan, Christopher, additional, Davies, Jamie A, additional, Abbracchio, Maria Pia, additional, Alexander, Wayne, additional, Al‐hosaini, Khaled, additional, Bäck, Magnus, additional, Barnes, Nicholas M., additional, Bathgate, Ross, additional, Beaulieu, Jean‐Martin, additional, Bernstein, Kenneth E., additional, Bettler, Bernhard, additional, Birdsall, Nigel J.M., additional, Blaho, Victoria, additional, Boulay, Francois, additional, Bousquet, Corinne, additional, Bräuner‐Osborne, Hans, additional, Burnstock, Geoffrey, additional, Caló, Girolamo, additional, Castaño, Justo P., additional, Catt, Kevin J., additional, Ceruti, Stefania, additional, Chazot, Paul, additional, Chiang, Nan, additional, Chini, Bice, additional, Chun, Jerold, additional, Cianciulli, Antonia, additional, Civelli, Olivier, additional, Clapp, Lucie H., additional, Couture, Réjean, additional, Csaba, Zsolt, additional, Dahlgren, Claes, additional, Dent, Gordon, additional, Singh, Khuraijam Dhanachandra, additional, Douglas, Steven D., additional, Dournaud, Pascal, additional, Eguchi, Satoru, additional, Escher, Emanuel, additional, Filardo, Edward J., additional, Fong, Tung, additional, Fumagalli, Marta, additional, Gainetdinov, Raul R, additional, Gasparo, Marc de, additional, Gerard, Craig, additional, Gershengorn, Marvin, additional, Gobeil, Fernand, additional, Goodfriend, Theodore L., additional, Goudet, Cyril, additional, Gregory, Karen J., additional, Gundlach, Andrew L., additional, Hamann, Jörg, additional, Hanson, Julien, additional, Hauger, Richard L., additional, Hay, Debbie L., additional, Heinemann, Akos, additional, Hollenberg, Morley D., additional, Holliday, Nicholas D., additional, Horiuchi, Mastgugu, additional, Hoyer, Daniel, additional, Hunyady, László, additional, Husain, Ahsan, additional, IJzerman, Adriaan P., additional, Inagami, Tadashi, additional, Jacobson, Kenneth A., additional, Jensen, Robert T., additional, Jockers, Ralf, additional, Jonnalagadda, Deepa, additional, Karnik, Sadashiva, additional, Kaupmann, Klemens, additional, Kemp, Jacqueline, additional, Kennedy, Charles, additional, Kihara, Yasuyuki, additional, Kitazawa, Takio, additional, Kozielewicz, Pawel, additional, Kreienkamp, Hans‐Jürgen, additional, Kukkonen, Jyrki P., additional, Langenhan, Tobias, additional, Leach, Katie, additional, Lecca, Davide, additional, Lee, John D., additional, Leeman, Susan E., additional, Leprince, Jérôme, additional, Li, Xaria X., additional, Williams, Tom Lloyd, additional, Lolait, Stephen J., additional, Lupp, Amelie, additional, Macrae, Robyn, additional, Maguire, Janet, additional, Mazella, Jean, additional, McArdle, Craig A., additional, Melmed, Shlomo, additional, Michel, Martin C., additional, Miller, Laurence J., additional, Mitolo, Vincenzo, additional, Mouillac, Bernard, additional, Müller, Christa E., additional, Murphy, Philip, additional, Nahon, Jean‐Louis, additional, Ngo, Tony, additional, Norel, Xavier, additional, Nyimanu, Duuamene, additional, O’Carroll, Anne‐Marie, additional, Offermanns, Stefan, additional, Panaro, Maria Antonietta, additional, Parmentier, Marc, additional, Pertwee, Roger G., additional, Pin, Jean‐Philippe, additional, Prossnitz, Eric R., additional, Quinn, Mark, additional, Ramachandran, Rithwik, additional, Ray, Manisha, additional, Reinscheid, Rainer K., additional, Rondard, Philippe, additional, Rovati, G. Enrico, additional, Ruzza, Chiara, additional, Sanger, Gareth J., additional, Schöneberg, Torsten, additional, Schulte, Gunnar, additional, Schulz, Stefan, additional, Segaloff, Deborah L., additional, Serhan, Charles N., additional, Stoddart, Leigh A., additional, Sugimoto, Yukihiko, additional, Summers, Roger, additional, Tan, Valerie P., additional, Thal, David, additional, Thomas, Walter (Wally), additional, Timmermans, Pieter B. M. W. M., additional, Tirupula, Kalyan, additional, Tulipano, Giovanni, additional, Unal, Hamiyet, additional, Unger, Thomas, additional, Valant, Celine, additional, Vanderheyden, Patrick, additional, Vaudry, David, additional, Vaudry, Hubert, additional, Vilardaga, Jean‐Pierre, additional, Walker, Christopher S., additional, Wang, Ji Ming, additional, Ward, Donald T., additional, Wester, Hans‐Jürgen, additional, Willars, Gary B, additional, Woodruff, Trent M., additional, Yao, Chengcan, additional, and Ye, Richard D., additional

Published
2021
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46. Evaluating bony predictors of bite force across the order Carnivora

Author

Dickinson, Edwin, primary, Davis, Jillian S., additional, Deutsch, Ashley R., additional, Patel, Dhuru, additional, Nijhawan, Akash, additional, Patel, Meet, additional, Blume, Abby, additional, Gannon, Jordan L., additional, Turcotte, Cassandra M., additional, Walker, Christopher S., additional, and Hartstone‐Rose, Adam, additional

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

Author

Alexander, Stephen Ph, Christopoulos, Arthur, Davenport, Anthony P, Kelly, Eamonn, Mathie, Alistair, Peters, John A, Veale, Emma L, Armstrong, Jane F, Faccenda, Elena, Harding, Simon D, Pawson, Adam J, Southan, Christopher, Davies, Jamie A, Abbracchio, Maria Pia, Alexander, Wayne, Al-Hosaini, Khaled, Bäck, Magnus, Barnes, Nicholas M, Bathgate, Ross, Beaulieu, Jean-Martin, 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, Csaba, Zsolt, Dahlgren, Claes, Dent, Gordon, Singh, Khuraijam Dhanachandra, Douglas, Steven D, Dournaud, Pascal, Eguchi, Satoru, Escher, Emanuel, Filardo, Edward J, Fong, Tung, Fumagalli, Marta, Gainetdinov, Raul R, Gasparo, Marc de, Gerard, Craig, Gershengorn, Marvin, Gobeil, Fernand, Goodfriend, Theodore L, Goudet, Cyril, Gregory, Karen J, Gundlach, Andrew L, Hamann, Jörg, Hanson, Julien, Hauger, Richard L, Hay, Debbie L, Heinemann, Akos, 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, Leach, Katie, Lecca, Davide, Lee, John D, Leeman, Susan E, Leprince, Jérôme, Li, Xaria X, Williams, Tom Lloyd, Lolait, Stephen J, Lupp, Amelie, Macrae, Robyn, Maguire, Janet, Mazella, Jean, McArdle, Craig A, Melmed, Shlomo, Michel, Martin C, Miller, Laurence J, Mitolo, Vincenzo, Mouillac, Bernard, Müller, Christa E, Murphy, Philip, 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, Stoddart, Leigh A, Sugimoto, Yukihiko, Summers, Roger, Tan, Valerie P, Thal, David, Thomas, Walter Wally, Timmermans, Pieter B M W M, Tirupula, Kalyan, 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, Woodruff, Trent M, Yao, Chengcan, Ye, Richard D, Alexander, Stephen Ph, Christopoulos, Arthur, Davenport, Anthony P, Kelly, Eamonn, Mathie, Alistair, Peters, John A, Veale, Emma L, Armstrong, Jane F, Faccenda, Elena, Harding, Simon D, Pawson, Adam J, Southan, Christopher, Davies, Jamie A, Abbracchio, Maria Pia, Alexander, Wayne, Al-Hosaini, Khaled, Bäck, Magnus, Barnes, Nicholas M, Bathgate, Ross, Beaulieu, Jean-Martin, 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, Csaba, Zsolt, Dahlgren, Claes, Dent, Gordon, Singh, Khuraijam Dhanachandra, Douglas, Steven D, Dournaud, Pascal, Eguchi, Satoru, Escher, Emanuel, Filardo, Edward J, Fong, Tung, Fumagalli, Marta, Gainetdinov, Raul R, Gasparo, Marc de, Gerard, Craig, Gershengorn, Marvin, Gobeil, Fernand, Goodfriend, Theodore L, Goudet, Cyril, Gregory, Karen J, Gundlach, Andrew L, Hamann, Jörg, Hanson, Julien, Hauger, Richard L, Hay, Debbie L, Heinemann, Akos, 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, Leach, Katie, Lecca, Davide, Lee, John D, Leeman, Susan E, Leprince, Jérôme, Li, Xaria X, Williams, Tom Lloyd, Lolait, Stephen J, Lupp, Amelie, Macrae, Robyn, Maguire, Janet, Mazella, Jean, McArdle, Craig A, Melmed, Shlomo, Michel, Martin C, Miller, Laurence J, Mitolo, Vincenzo, Mouillac, Bernard, Müller, Christa E, Murphy, Philip, 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, Stoddart, Leigh A, Sugimoto, Yukihiko, Summers, Roger, Tan, Valerie P, Thal, David, Thomas, Walter Wally, Timmermans, Pieter B M W M, Tirupula, Kalyan, 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, Woodruff, Trent M, Yao, Chengcan, and Ye, Richard D

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

49. Effect of Adrenomedullin on Migraine-Like Attacks in Patients With Migraine:A Randomized Crossover Study

Author

Ghanizada, Hashmat, Al-Karagholi, Mohammad Al Mahdi, Arngrim, Nanna, Mørch-Rasmussen, Mette, Walker, Christopher S., Hay, Debbie L., Ashina, Messoud, Ghanizada, Hashmat, Al-Karagholi, Mohammad Al Mahdi, Arngrim, Nanna, Mørch-Rasmussen, Mette, Walker, Christopher S., Hay, Debbie L., and Ashina, Messoud

Abstract

OBJECTIVE: To determine whether the IV infusion of adrenomedullin, a potent vasodilator belonging to calcitonin family of peptides, provokes attacks of migraine in patients. METHODS: Twenty patients with migraine without aura participated in a placebo-controlled and double-blind clinical study. In a randomized crossover design, the patients received an IV infusion of human adrenomedullin (19.9 pmol/kg/min) or placebo (saline) administrated via an automated IV pump (20 minutes). The patients participated in 2 study days with a washout period of minimum of 7 days. The primary outcome of the study was predefined as a difference in migraine incidence (0-12 hours), and the secondary outcomes were the area under curve (AUC0-12 hours) for the headache intensity score and AUC0-90 minutes for mean arterial blood pressure (MAP), flushing, and heart rate (HR). RESULTS: Eleven patients with migraine without aura (55%) fulfilled migraine attacks criteria after adrenomedullin infusion compared to only 3 patients who reported attack (15%) after placebo (p = 0.039). We found that patients reported in a period of 0 to 12 hours stronger headache intensity after adrenomedullin compared to placebo infusion (p = 0.035). AUC0-90 minutes value for HR and flushing (p < 0.05) was significant and for MAP (p = 0.502) remained unchanged. Common reported adverse events were facial flushing, heat sensation, and palpitation (p < 0.001). CONCLUSION: Our data implicate adrenomedullin in migraine pathogenesis. This suggests that adrenomedullin or its receptors are novel therapeutic targets for the treatment of migraine. However, we cannot discount the possibility that adrenomedullin may be acting through the canonical calcitonin gene-related peptide receptor. TRIAL REGISTRATION INFORMATION: ClinicalTrials.gov Identifier: NCT04111484.

Published
2021

50. Regulation of signal transduction by calcitonin gene-related peptide receptors

Author

Walker, Christopher S., Conner, Alex C., Poyner, David R., and Hay, Debbie L.

Subjects
Peptides -- Physiological aspects, Membrane proteins -- Physiological aspects, Calcitonin -- Physiological aspects, G proteins -- Physiological aspects, Migraine -- Physiological aspects, Biological sciences, Chemistry, Pharmaceuticals and cosmetics industries
Abstract

To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/j.tips.2010.06.006 Byline: Christopher S Walker (1), Alex C Conner (2), David R Poyner (3), Debbie L Hay (1) Abstract: Calcitonin gene-related peptide (CGRP) plays a pivotal role in migraine, activating its cognate receptor to initiate intracellular signalling. This atypical receptor comprises a distinct assembly, made up of a G protein-coupled receptor (GPCR), a single transmembrane protein, and an additional protein that is required for G[alpha].sub.s coupling. By altering the expression of individual receptor components, it might be possible to adjust cellular sensitivity to CGRP. In recognition of the increasing clinical significance of CGRP receptors, it is timely to review the signalling pathways that might be controlled by this receptor, how the activity of the receptor itself is regulated, and our current understanding of the molecular mechanisms involved in these processes. Like many GPCRs, the CGRP receptor appears to be promiscuous, potentially coupling to several G proteins and intracellular pathways. Their precise composition is likely to be cell type-dependent, and much work is needed to ascertain their physiological significance. Author Affiliation: (1) School of Biological Sciences, and Centre for Brain Research, University of Auckland, Auckland, New Zealand (2) Warwick Medical School, University of Warwick, Coventry, United Kingdom (3) School of Life and Health Sciences, Aston University, Birmingham, United Kingdom

Published
2010

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