Secretin family
 | |||||||||
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Symbol | Hormone_2 | ||||||||
| Pfam | PF00123 | ||||||||
| InterPro | IPR000532 | ||||||||
| PROSITE | PDOC00233 | ||||||||
| SCOP2 | 1gcn / SCOPe / SUPFAM | ||||||||
| OPM superfamily | 145 | ||||||||
| OPM protein | 1gcn | ||||||||
| |||||||||
Glucagon/gastric inhibitory polypeptide/secretin/vasoactive intestinal peptide hormones are a family of evolutionarily related peptide hormones that regulate activity of G-protein-coupled receptors from the secretin receptor family. A number of polypeptidic hormones, mainly expressed in the intestine or the pancreas, belong to a group of these structurally related peptides.[1][2]
This family of hormones are produced from (preproglucagon), which is cleaved to produce glucagon, glucagon-like protein I, glucagon-like protein II, and glicentin.[3] Other members of the structurally similar group include secretin, gastric inhibitory peptide, vasoactive intestinal peptide, prealbumin, peptide HI-27, and growth hormone releasing factor.
One hormone, glucagon, is fully conserved in all mammalian species in which it has been studied.[4]
Human hormones from this family
[edit]ADCYAP1; GCG; GHRH; GIP; SCT; VIP;
References
[edit]- ^ Mutt V (1988). "Vasoactive intestinal polypeptide and related peptides. Isolation and chemistry". Annals of the New York Academy of Sciences. 527 (1): 1–19. Bibcode:1988NYASA.527....1M. doi:10.1111/j.1749-6632.1988.tb26968.x. PMID 3133967. S2CID 40431562.
- ^ Bataille D, Blache P, Mercier F, Jarrousse C, Kervran A, Dufour M, Mangeat P, Dubrasquet M, Mallat A, Lotersztajn S (1988). "Glucagon and related peptides. Molecular structure and biological specificity". Annals of the New York Academy of Sciences. 527 (1): 168–85. Bibcode:1988NYASA.527..168B. doi:10.1111/j.1749-6632.1988.tb26980.x. PMID 3291691. S2CID 7798790.
- ^ Pollock HG, Hamilton JW, Rouse JB, Ebner KE, Rawitch AB (July 1988). "Isolation of peptide hormones from the pancreas of the bullfrog (Rana catesbeiana). Amino acid sequences of pancreatic polypeptide, oxyntomodulin, and two glucagon-like peptides". The Journal of Biological Chemistry. 263 (20): 9746–51. doi:10.1016/S0021-9258(19)81581-8. PMID 3260236.
- ^ Conlon JM, Thim L (December 1985). "Primary structure of glucagon from an elasmobranchian fish. Torpedo marmorata". General and Comparative Endocrinology. 60 (3): 398–405. doi:10.1016/0016-6480(85)90073-5. PMID 4076759.