Bombesin-like peptides

Bombesin-like peptides comprise a large family of peptides which were initially isolated from amphibian skin, where they stimulate smooth muscle contraction. They were later found to be widely distributed in mammalian neural and endocrine cells.

Bombesin-like peptide
Identifiers
SymbolBombesin
PfamPF02044
InterProIPR000874
PROSITEPDOC00230

The amphibian peptides which belong to this family are currently classified into three subfamilies;[1][2] the Bombesin group, which includes bombesin and alytesin; the Ranatensin group, which includes ranatensins, litorin, and Rohdei litorin; and the Phyllolitorin group, which includes Leu(8)- and Phe(8)-phyllolitorins.

In mammals and birds two categories of bombesin-like peptides are known,[3][4] gastrin-releasing peptide (GRP), which stimulates the release of gastrin as well as other gastrointestinal hormones, and neuromedin B (NMB), a neuropeptide whose function is not yet clear. Bombesin-like peptides, like many other active peptides, are synthesized as larger protein precursors that are enzymatically converted to their mature forms. The final peptides are eight to fourteen residues long.

References
  1. Erspamer V, Erspamer GF, Mazzanti G, Endean R (1984). "Active peptides in the skins of one hundred amphibian species from Australia and Papua New Guinea". Comp. Biochem. Physiol. 77 (1): 99–108. doi:10.1016/0742-8413(84)90137-3. PMID 6141890.
  2. Erspamer V, Melchiorri P, Falconieri Erspamer G, Montecucchi PC, de Castiglione R (1985). "Phyllomedusa skin: a huge factory and store-house of a variety of active peptides". Peptides. 6: 7–12. doi:10.1016/0196-9781(85)90343-2. PMID 3868775.
  3. Battey J, Wada E (1991). "Two distinct receptor subtypes for mammalian bombesin-like peptides". Trends Neurosci. 14 (12): 524–528. doi:10.1016/0166-2236(91)90005-F. PMID 1726343.
  4. Chin WW, Krane IM, Naylor SL, Helin-Davis D, Spindel ER (1988). "Molecular cloning of cDNAs encoding the human bombesin-like peptide neuromedin B. Chromosomal localization and comparison to cDNAs encoding its amphibian homolog ranatensin". J. Biol. Chem. 263 (26): 13317–13323. PMID 2458345.
This article incorporates text from the public domain Pfam and InterPro: IPR000874
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