Secretin family

Glucagon (1gcn)
Identifiers
SymbolHormone_2
PfamPF00123
InterProIPR000532
PROSITEPDOC00233
SCOP21gcn / SCOPe / SUPFAM
OPM superfamily145
OPM protein1gcn
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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] One such hormone, glucagon, is widely distributed and produced in the alpha-cells of pancreatic islets.[3] It affects glucose metabolism in the liver[4] by inhibiting glycogen synthesis, stimulating glycogenolysis and enhancing gluconeogenesis. It also increases mobilisation of glucose, free fatty acids, and ketone bodies, which are metabolites produced in excess in diabetes mellitus. Glucagon is produced, like other peptide hormones, as part of a larger precursor (preproglucagon), which is cleaved to produce glucagon, glucagon-like protein I, glucagon-like protein II, and glicentin.[5] The structure of glucagon itself is fully conserved in all mammalian species in which it has been studied.[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.

Human hormones from this family

ADCYAP1; GCG; GHRH; GIP; SCT; VIP;

References

  1. ^ 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.
  2. ^ 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.
  3. ^ a b 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.
  4. ^ Lopez LC, Frazier ML, Su CJ, Kumar A, Saunders GF (September 1983). "Mammalian pancreatic preproglucagon contains three glucagon-related peptides". Proceedings of the National Academy of Sciences of the United States of America. 80 (18): 5485–9. Bibcode:1983PNAS...80.5485L. doi:10.1073/pnas.80.18.5485. PMC 384282. PMID 6577439.
  5. ^ 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.
This article incorporates text from the public domain Pfam and InterPro: IPR000532