| calcitonin gene-related peptide | <protein> A second product transcribed from the calcitonin gene. Calcitonin gene related peptide is found in a number of tissues including nervous tissue. It is a vasodilator that may participate in the cutaneous triple response. It is a neuropeptide of 37 amino acids with structural homology to salmon calcitonin. Co-localises with substance P in neurons. It occurs as a result of alternative processing of mRNA from the calcitonin gene. The neuropeptide is widely distributed in neural tissue of the brain, gut, perivascular nerves, and other tissue. The peptide produces multiple biological effects and has both circulatory and neurotransmitter modes of action. In particular, it is a potent endogenous vasodilator. Intracerebral administration leads to a rise in noradrenergic sympathetic outflow, a rise in blood pressure and a fall in gastric secretion. Acronym: CGRP (05 May 2002) |
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| vasoactive intestinal peptide | <gastroenterology, protein> Peptide of 28 amino acids, originally isolated from porcine intestine, but later found in the central nervous system where it acts as a neuropeptide and is released by specific interneurons. May also affect behaviour of cells of the immune system. Acronym: VIP (05 Jan 1998) |
| gastrin-releasing peptide | <hormone> A regulatory peptide (27 amino acids) thought to be the mammalian equivalent of bombesin. It elicits gastrin release and regulates gastric acid secretion and motor function. It causes bronchoconstriction and vasodilation in the respiratory tract and stimulates the growth and mitogenesis of cells in culture. Once released from nerves in the antrum of the stomach, the neuropeptide stimulates release of gastrin from the g cells. Chemical name: Gastrin-releasing peptide (12 Dec 1998) |
| receptors, calcitonin gene-related peptide | Cell surface proteins that bind calcitonin gene-related peptide (cgrp) with high affinity and trigger intracellular changes which influence the behaviour of cells. Cgrp receptors are present in both the central nervous system and the periphery and are not the same as calcitonin receptors. (12 Dec 1998) |
| receptors, invertebrate peptide | Cell surface receptors for invertebrate peptide hormones or neuropeptides. (12 Dec 1998) |
| receptors, peptide | Cell surface receptors that bind peptide messengers with high affinity and regulate intracellular signals which influence the behaviour of cells. (12 Dec 1998) |
| receptors, vasoactive intestinal peptide | Cell surface proteins that bind vasoactive intestinal peptide (vip) with high affinity and trigger intracellular changes which influence the behaviour of cells. (12 Dec 1998) |
| glutaminyl-peptide cyclotransferase | <enzyme> Catalyses the formation of 5-oxoprolyl-trna and nh3 from l-glutaminyl-trna; also acts on glutaminyl peptides Registry number: EC 2.3.2.5 Synonym: glutaminyl cyclase, glutaminylpeptide cyclase, glutamine cyclotransferase, glutaminyl-trna cyclotransferase (26 Jun 1999) |
| peptide | <biochemistry> A compound of two or more amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another. (27 Sep 1997) |
| peptide antibiotic lactonase | <enzyme> Peptide lactone and water gives linear peptide Registry number: EC 3.1.1.- (26 Jun 1999) |
| peptide bond | The amide linkage between the carboxyl group of one amino acid and the amino group of another. The linkage does not allow free rotation and can occur in cis or trans configuration, the latter the most common in natural peptides, except for links to the amino group of proline, which are always cis. (18 Nov 1997) |
| peptide chain elongation | The process whereby an amino acid is joined through a substituted amide linkage to a chain of peptides. (12 Dec 1998) |
| peptide chain initiation | The process whereby the formation of a peptide chain is started. This process requires (1) the 30s subunit, (2) the mRNA coding for the polypeptide to be made, (3) met-trnai, (4) initiation factors, and (5) GTP. (12 Dec 1998) |
| peptide chain termination | The process whereby the last amino acid is added to a polypeptide. This termination is signaled by one of three termination triplets in the mRNA, immediately following the last amino acid codon. (12 Dec 1998) |
| peptide deformylase | <enzyme> Fms is a zinc-containing protein showing homologies with zinc aminopeptidases; its enzyme function resembles that of an aminopeptidase; has been sequenced; mol mass 19,207 da Registry number: EC 3.4.11.- Synonym: fms protein, fms gene product (26 Jun 1999) |