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- W1020209780 startingPage "69" @default.
- W1020209780 abstract "PACAP (; ) and VIP (; ) are two prominent neuropeptides which have wide distribution in peripheral and central nervous systems and large spectrum of biological actions. The 28-aminoacid peptide VIP was discovered in 1970 () and VIP receptors were shortly described in the seventies (; for review). PACAP was isolated much later in 1989 () as a 38-aminoacid peptide but a shorter form PACAP27 () is also present in various tissues (; ). The sequence of PACAP27 shows 68% identity with that of VIP in humans. Therefore, VIP and PACAP are the most closely related peptides in terms of structure and function in the so-called VIP-secretin family of structurally related peptides that comprises secretin, glucagon and glucagon-like peptides I and II, peptide histidine isoleucineamide (PHI), helodermin, growth hormone-releasing factor (GRF) and gastric inhibitory polypeptide (GIP) (). Soon after the discovery of PACAP, it was shown that PACAP was able to bind with high affinity to the classical VIP receptors (Shivers et al, 1991) and also had a specific receptor for which VIP has a very low affinity (; ). The rapid development of receptor cloning in the nineties provided evidence for three receptor subtypes for PACAP: the so-called VPAC1, VPAC2 and PAC1 receptors (see below). In this context, the present chapter reviews the data regarding the molecular pharmacology and structure-function relationship of PACAP receptors including VPAC1, VPAC2 and PAC1 with special emphasis on receptors from humans and rats." @default.
- W1020209780 created "2016-06-24" @default.
- W1020209780 creator A5012381902 @default.
- W1020209780 creator A5076634867 @default.
- W1020209780 creator A5079930654 @default.
- W1020209780 date "2003-01-01" @default.
- W1020209780 modified "2023-09-26" @default.
- W1020209780 title "Molecular Pharmacology and Structure-Function Analysis of PACAP/Vip Receptors" @default.
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