Xenopsin-related peptide generated in avian gastric extracts.
Two avian counterparts to amphibian xenopsin have been identified as H-Phe-His-Pro-Lys-Arg-Pro-Trp-Ile-Leu-OH (XP-2) and its partial sequence H-His-Pro-Lys-Arg-Pro-Trp-Ile-Leu-OH (XP-1) isolated from extracts of turkey proventriculus and skin. Both peptides were shown to be present within these and other tissues primarily (99%) in precursor form(s), from which they were liberated by the action of endogenous enzyme(s) during extraction. Synthetic and native preparations of XP-2 increased vascular permeability in rats and released histamine from isolated rat mast cells at submicromolar concentrations. The ubiquitous distribution of this XP-related sequence and its pharmacologic capabilities suggest potential roles in the general regulation of tissue blood flow and fluid exchange.
Carraway
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Department of Physiology, University of Massachusetts Medical Center, Worcester 01605.
Cochrane
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Mitra
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D000595:Amino Acid Sequence; D000818:Animals; D002199:Capillary Permeability / Q000187:drug effects; D002645:Chickens; D005753:Gastric Mucosa / Q000378:metabolism*; D006636:Histamine Release; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000096:biosynthesis* / Q000494:pharmacology; D010455:Peptides; D051381:Rats; D012867:Skin / Q000378:metabolism; D014422:Turkeys; D029867:Xenopus Proteins
D009842:Oligopeptides; D010455:Peptides; D029867:Xenopus Proteins; C016832:xenopsin