Pancreatic hormone
Oxford Dictionary of Biochemistry:
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pancreatic hormone
or pancreatic polypeptide
abbr.: PP; a polypeptide present in the PP cells of the pancreas. Avian pancreatic polypeptide, known as aPP (from chicken and turkey pancreas), and bovine, human, ovine, and porcine homologues, known as bPP, hPP, oPP, and pPP, respectively, have been identified. All contain 36 amino-acid residues with C-terminal tyrosinamide and show considerable sequence homology. The plasma PP level rises rapidly after feeding, especially with protein foods, and with fasting, exercise, and hypoglycemia. The hormone decreases food absorption and pancreatic exocrine secretion. The sequence of human PP is: APLEPVYPGDNATPEQMAQYAADLRRYINMLTRPRY(NH2).
abbr.: PP; a polypeptide present in the PP cells of the pancreas. Avian pancreatic polypeptide, known as aPP (from chicken and turkey pancreas), and bovine, human, ovine, and porcine homologues, known as bPP, hPP, oPP, and pPP, respectively, have been identified. All contain 36 amino-acid residues with C-terminal tyrosinamide and show considerable sequence homology. The plasma PP level rises rapidly after feeding, especially with protein foods, and with fasting, exercise, and hypoglycemia. The hormone decreases food absorption and pancreatic exocrine secretion. The sequence of human PP is: APLEPVYPGDNATPEQMAQYAADLRRYINMLTRPRY(NH2).
| pancreatic diabetes, pancreatic cholera, pancreatic DNase I | |
| pancreatic islet, pancreatic juice, pancreatic lipase |
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Pancreatic hormone
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| Pancreatic hormone peptide | |||||||||
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| Structure of avian pancreatic polypeptide.[1] | |||||||||
| Identifiers | |||||||||
| Symbol | Hormone_3 | ||||||||
| Pfam | PF00159 | ||||||||
| InterPro | IPR001955 | ||||||||
| PROSITE | PDOC00238 | ||||||||
| SCOP | 1ppt | ||||||||
| OPM protein | 1icy | ||||||||
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Pancreatic hormones (PP)[2] are peptides synthesized in pancreatic islets of Langerhans, 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[3] and has an amidated C terminus.[4] 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.[3] Unlike glucagon, another peptide hormone, the structure of pancreatic peptide is preserved in aqueous solution.[5] Both N and C termini are required for activity: receptor binding and activation functions may reside in the N and C termini respectively.[3]
Subfamilies
Human proteins containing this domain
References
- ^ Blundell TL, Pitts JE, Tickle IJ, Wood SP, Wu CW (July 1981). "X-ray analysis (1. 4-A resolution) of avian pancreatic polypeptide: Small globular protein hormone". Proc. Natl. Acad. Sci. U.S.A. 78 (7): 4175–4179. doi:10.1073/pnas.78.7.4175. PMC 319751. PMID 16593056. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=319751.
- ^ Humbel RE, Blundell TL (1980). "Hormone families: pancreatic hormones and homologous growth factors". Nature 287 (5785): 781–787. doi:10.1038/287781a0. PMID 6107857.
- ^ a b c 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. PMC 304688. PMID 3031687. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=304688.
- ^ 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.
This article includes text from the public domain Pfam and InterPro IPR001955
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