Pituitary Adenylate Cyclase-Activating Polypeptide and Its Receptors: 20 Years after the Discovery
Pituitary adenylate cyclase-activating polypeptide (PACAP) is a 38-amino acid C-terminally α-amidated peptide that was first isolated 20 years ago from an ovine hypothalamic extract on the basis of its ability to stimulate cAMP formation in anterior pituitary cells ( Miyata et al., 1989 . PACAP bel...
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| Published in | Pharmacological reviews Vol. 61; no. 3; pp. 283 - 357 |
|---|---|
| Main Authors | , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
American Society for Pharmacology and Experimental Therapeutics
01.09.2009
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| Subjects | |
| Online Access | Get full text |
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| Abstract | Pituitary adenylate cyclase-activating polypeptide (PACAP) is a 38-amino acid C-terminally α-amidated peptide that was first
isolated 20 years ago from an ovine hypothalamic extract on the basis of its ability to stimulate cAMP formation in anterior
pituitary cells ( Miyata et al., 1989 . PACAP belongs to the vasoactive intestinal polypeptide (VIP)-secretin-growth hormone-releasing hormone-glucagon superfamily.
The sequence of PACAP has been remarkably well conserved during evolution from protochordates to mammals, suggesting that
PACAP is involved in the regulation of important biological functions. PACAP is widely distributed in the brain and peripheral
organs, notably in the endocrine pancreas, gonads, respiratory and urogenital tracts. Characterization of the PACAP precursor
has revealed the existence of a PACAP-related peptide, the activity of which remains unknown. Two types of PACAP binding sites
have been characterized: type I binding sites exhibit a high affinity for PACAP and a much lower affinity for VIP, whereas
type II binding sites have similar affinity for PACAP and VIP. Molecular cloning of PACAP receptors has shown the existence
of three distinct receptor subtypes: the PACAP-specific PAC1-R, which is coupled to several transduction systems, and the
PACAP/VIP-indifferent VPAC1-R and VPAC2-R, which are primarily coupled to adenylyl cyclase. PAC1-Rs are particularly abundant
in the brain, the pituitary and the adrenal gland, whereas VPAC receptors are expressed mainly in lung, liver, and testis.
The development of transgenic animal models and specific PACAP receptor ligands has strongly contributed to deciphering the
various actions of PACAP. Consistent with the wide distribution of PACAP and its receptors, the peptide has now been shown
to exert a large array of pharmacological effects and biological functions. The present report reviews the current knowledge
concerning the pleiotropic actions of PACAP and discusses its possible use for future therapeutic applications. |
|---|---|
| AbstractList | Pituitary adenylate cyclase-activating polypeptide (PACAP) is a 38-amino acid C-terminally alpha-amidated peptide that was first isolated 20 years ago from an ovine hypothalamic extract on the basis of its ability to stimulate cAMP formation in anterior pituitary cells (Miyata et al., 1989. PACAP belongs to the vasoactive intestinal polypeptide (VIP)-secretin-growth hormone-releasing hormone-glucagon superfamily. The sequence of PACAP has been remarkably well conserved during evolution from protochordates to mammals, suggesting that PACAP is involved in the regulation of important biological functions. PACAP is widely distributed in the brain and peripheral organs, notably in the endocrine pancreas, gonads, respiratory and urogenital tracts. Characterization of the PACAP precursor has revealed the existence of a PACAP-related peptide, the activity of which remains unknown. Two types of PACAP binding sites have been characterized: type I binding sites exhibit a high affinity for PACAP and a much lower affinity for VIP, whereas type II binding sites have similar affinity for PACAP and VIP. Molecular cloning of PACAP receptors has shown the existence of three distinct receptor subtypes: the PACAP-specific PAC1-R, which is coupled to several transduction systems, and the PACAP/VIP-indifferent VPAC1-R and VPAC2-R, which are primarily coupled to adenylyl cyclase. PAC1-Rs are particularly abundant in the brain, the pituitary and the adrenal gland, whereas VPAC receptors are expressed mainly in lung, liver, and testis. The development of transgenic animal models and specific PACAP receptor ligands has strongly contributed to deciphering the various actions of PACAP. Consistent with the wide distribution of PACAP and its receptors, the peptide has now been shown to exert a large array of pharmacological effects and biological functions. The present report reviews the current knowledge concerning the pleiotropic actions of PACAP and discusses its possible use for future therapeutic applications. Pituitary adenylate cyclase-activating polypeptide (PACAP) is a 38-amino acid C-terminally α-amidated peptide that was first isolated 20 years ago from an ovine hypothalamic extract on the basis of its ability to stimulate cAMP formation in anterior pituitary cells ( Miyata et al., 1989 . PACAP belongs to the vasoactive intestinal polypeptide (VIP)-secretin-growth hormone-releasing hormone-glucagon superfamily. The sequence of PACAP has been remarkably well conserved during evolution from protochordates to mammals, suggesting that PACAP is involved in the regulation of important biological functions. PACAP is widely distributed in the brain and peripheral organs, notably in the endocrine pancreas, gonads, respiratory and urogenital tracts. Characterization of the PACAP precursor has revealed the existence of a PACAP-related peptide, the activity of which remains unknown. Two types of PACAP binding sites have been characterized: type I binding sites exhibit a high affinity for PACAP and a much lower affinity for VIP, whereas type II binding sites have similar affinity for PACAP and VIP. Molecular cloning of PACAP receptors has shown the existence of three distinct receptor subtypes: the PACAP-specific PAC1-R, which is coupled to several transduction systems, and the PACAP/VIP-indifferent VPAC1-R and VPAC2-R, which are primarily coupled to adenylyl cyclase. PAC1-Rs are particularly abundant in the brain, the pituitary and the adrenal gland, whereas VPAC receptors are expressed mainly in lung, liver, and testis. The development of transgenic animal models and specific PACAP receptor ligands has strongly contributed to deciphering the various actions of PACAP. Consistent with the wide distribution of PACAP and its receptors, the peptide has now been shown to exert a large array of pharmacological effects and biological functions. The present report reviews the current knowledge concerning the pleiotropic actions of PACAP and discusses its possible use for future therapeutic applications. |
| Author | David Vaudry Olivier Wurtz Alain Fournier Hitoshi Hashimoto Ludovic Galas Hubert Vaudry Anthony Falluel-Morel Billy K. C. Chow Steve Bourgault Magali Basille Delphine Burel |
| Author_xml | – sequence: 1 givenname: David surname: Vaudry fullname: Vaudry, David email: david.vaudry@univ-rouen.fr organization: Institut National de la Santé et de la Recherche Médicale U413, European Institute for Peptide Research (Institut Fédératif de Recherches Multidisciplinaires sur les Peptides 23), Mont-Saint-Aignan, France. david.vaudry@univ-rouen.fr – sequence: 2 givenname: Anthony surname: Falluel-Morel fullname: Falluel-Morel, Anthony – sequence: 3 givenname: Steve surname: Bourgault fullname: Bourgault, Steve – sequence: 4 givenname: Magali surname: Basille fullname: Basille, Magali – sequence: 5 givenname: Delphine surname: Burel fullname: Burel, Delphine – sequence: 6 givenname: Olivier surname: Wurtz fullname: Wurtz, Olivier – sequence: 7 givenname: Alain surname: Fournier fullname: Fournier, Alain – sequence: 8 givenname: Billy K C surname: Chow fullname: Chow, Billy K C – sequence: 9 givenname: Hitoshi surname: Hashimoto fullname: Hashimoto, Hitoshi – sequence: 10 givenname: Ludovic surname: Galas fullname: Galas, Ludovic – sequence: 11 givenname: Hubert surname: Vaudry fullname: Vaudry, Hubert |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/19805477$$D View this record in MEDLINE/PubMed https://hal.science/hal-02058111$$DView record in HAL |
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25 2019081415461045000_61.3.283.527 2019081415461045000_61.3.283.769 2019081415461045000_61.3.283.1302 2019081415461045000_61.3.283.524 2019081415461045000_61.3.283.766 2019081415461045000_61.3.283.1307 2019081415461045000_61.3.283.525 2019081415461045000_61.3.283.767 2019081415461045000_61.3.283.764 2019081415461045000_61.3.283.1305 2019081415461045000_61.3.283.523 2019081415461045000_61.3.283.765 2019081415461045000_61.3.283.1306 2019081415461045000_61.3.283.520 2019081415461045000_61.3.283.762 2019081415461045000_61.3.283.521 2019081415461045000_61.3.283.763 2019081415461045000_61.3.283.760 2019081415461045000_61.3.283.761 (2019081415461045000_61.3.283.323) 2000; 20 (2019081415461045000_61.3.283.161) 1998; 275 (2019081415461045000_61.3.283.436) 2002; 22 (2019081415461045000_61.3.283.1380) 1995; 55 2019081415461045000_61.3.283.539 2019081415461045000_61.3.283.537 2019081415461045000_61.3.283.779 2019081415461045000_61.3.283.538 2019081415461045000_61.3.283.535 2019081415461045000_61.3.283.777 2019081415461045000_61.3.283.536 2019081415461045000_61.3.283.778 2019081415461045000_61.3.283.533 2019081415461045000_61.3.283.776 2019081415461045000_61.3.283.531 2019081415461045000_61.3.283.773 2019081415461045000_61.3.283.532 2019081415461045000_61.3.283.774 2019081415461045000_61.3.283.771 2019081415461045000_61.3.283.530 2019081415461045000_61.3.283.772 2019081415461045000_61.3.283.770 (2019081415461045000_61.3.283.221) 1999; 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71 2019081415461045000_61.3.283.1310 2019081415461045000_61.3.283.319 2019081415461045000_61.3.283.1315 2019081415461045000_61.3.283.317 2019081415461045000_61.3.283.559 2019081415461045000_61.3.283.1313 2019081415461045000_61.3.283.315 2019081415461045000_61.3.283.557 2019081415461045000_61.3.283.799 2019081415461045000_61.3.283.1318 2019081415461045000_61.3.283.316 2019081415461045000_61.3.283.1319 2019081415461045000_61.3.283.313 (2019081415461045000_61.3.283.504) 1992; 1129 2019081415461045000_61.3.283.555 2019081415461045000_61.3.283.797 2019081415461045000_61.3.283.1316 2019081415461045000_61.3.283.556 2019081415461045000_61.3.283.1317 2019081415461045000_61.3.283.311 2019081415461045000_61.3.283.553 2019081415461045000_61.3.283.795 2019081415461045000_61.3.283.312 2019081415461045000_61.3.283.554 (2019081415461045000_61.3.283.918) 2008; 275 (2019081415461045000_61.3.283.1038) 1994; 267 2019081415461045000_61.3.283.551 2019081415461045000_61.3.283.793 2019081415461045000_61.3.283.310 2019081415461045000_61.3.283.552 2019081415461045 |
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| Snippet | Pituitary adenylate cyclase-activating polypeptide (PACAP) is a 38-amino acid C-terminally α-amidated peptide that was first
isolated 20 years ago from an... Pituitary adenylate cyclase-activating polypeptide (PACAP) is a 38-amino acid C-terminally alpha-amidated peptide that was first isolated 20 years ago from an... |
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| SubjectTerms | Animals Humans Life Sciences Neurons and Cognition Pituitary Adenylate Cyclase-Activating Polypeptide - chemistry Pituitary Adenylate Cyclase-Activating Polypeptide - pharmacology Pituitary Adenylate Cyclase-Activating Polypeptide - physiology Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide - chemistry Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide - physiology |
| Title | Pituitary Adenylate Cyclase-Activating Polypeptide and Its Receptors: 20 Years after the Discovery |
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