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Pancreatic hormone
Introduction
Pancreatic hormones (PP)[1] are peptides synthesized in pancreatic islets of Langherhans, which acts as a regulator of pancreatic and gastrointestinal functions.
The hormone is produced as a larger propeptide, which is enzymatically cleaved to yield the mature active peptide: this is 36 amino acids in length[2] and has an amidated C terminus[3]. The hormone has a globular structure, residues 2-8 forming a left-handed poly-proline-II-like helix, residues 9-13 a beta turn, and 14-32 an alpha-helix,held close to the first helix by hydrophobic interactions[2]. Unlike glucagon, another peptide hormone, the structure of pancreatic peptide is preserved in aqueous solution[4]. Both N and C termini are required for activity: receptor binding and activation functions may reside in the N and C termini respectively[2].
Subfamilies
Subfamilies
References
References
- ↑ Humbel RE, Blundell TL (1980). “Hormone families:
pancreatic hormones and homologous growth factors”. Nature. 287 (5785): 781–787. doi:10.1038/287781a0. PMID 6107857. line feed character in
|title=at position 18 (help) - ↑ 2.0 2.1 2.2 Martin J, Allen J, Novotny J, Heinrich G (1987). “Molecular structure of mammalian neuropeptide Y: analysis by molecular cloning and computer-aided comparison with crystal structure of avian homologue”. Proc. Natl. Acad. Sci. U.S.A. 84 (8): 2532–2536. doi:10.1073/pnas.84.8.2532. PMID 3031687.
- ↑ Mutt V, Sillard R, Agerberth B, Jornvall H (1989). “Sheep neuropeptide Y. A third structural type of a highly conserved peptide”. FEBS Lett. 258 (2): 263–265. doi:10.1016/0014-5793(89)81669-2. PMID 2599092.
- ↑ Conlon JM, Thim L, Bjenning C, Moon TW, Youson JH (1991). “Neuropeptide Y-related peptides from the pancreas of a teleostean (eel), holostean (bowfin) and elasmobranch (skate) fish”. Peptides. 12 (2): 221–226. doi:10.1016/0196-9781(91)90003-8. PMID 2067973.
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