Amylin

from Wikipedia, the free encyclopedia
Islet amyloid polypeptide
Islet amyloid polypeptide
Primary structure of amylin with a disulfide bridge and cleavage sites
Properties of human protein
Mass / length primary structure 37 aa; 3.9 kDa
Precursor (89 aa; 9.8 kDa)
Identifier
Gene names IAPP  ; IAP; DAP; AMYLIN
External IDs
Occurrence
Parent taxon Euteleostomi
Orthologue
human mouse
Entrez 3375 15874
Ensemble ENSG00000121351 ENSMUSG00000041681
UniProt P10997 P12968
Refseq (mRNA) NM_000415 NM_010491
Refseq (protein) NP_000406 NP_034621
Gene locus Chr 12: 21.42 - 21.42 Mb Chr 6: 142.26 - 142.26 Mb
PubMed search 3375 15874

Amylin , also called islet amyloid polypeptide (IAPP), is a peptide hormone which is produced by the β cells of the pancreas together with insulin (but only in one hundredth of the amount of insulin). If the pancreas becomes inoperable (e.g. due to diabetes), like insulin, it is no longer produced. It is a major component of the amyloid deposits in the islets of Langerhans . B. found in type II diabetes mellitus .

function

Amylin is part of the endocrine system and intervenes in the metabolism of carbohydrates . It supplements the insulin here. Although the full function of amylin is not yet fully understood, it is believed that amylin stabilizes blood sugar levels by inhibiting the release of glucagon .

structure

The primary structure of the human peptide consists of 37 amino acids with a disulfide bridge between the cysteines Cys-2 and Cys-7. The gene is on chromosome 12 .

pharmacology

Amylin plays a role in the long-term regulation of food intake, which is why its use as an appetite suppressant is being investigated. For this reason, it may also be used as a treatment for type 1 and 2 diabetes. Furthermore, one publication shows a positive influence on the reduction of osteoporosis .

Individual evidence

  1. ↑ tumaini.de: Amylin ( Memento from November 9, 2007 in the Internet Archive )
  2. ↑ UniProt P10997
  3. ↑ medicalforum.ch: Regulation of food intake by amylin and related peptides. (PDF; 85 kB)
  4. ↑ Medizin-aspekte.de: Amylin prevents bone loss in osteoporosis. ( Memento from August 19, 2007 in the Internet Archive )

literature

  • GJ Cooper, AC Willis, A. Clark, RC Turner, RB Sim, KB Reid: Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients. In: Proc Natl Acad Sci U.S.A. 84 (23), 1987 Dec, pp. 8628-8632. PMID 3317417
  • P. Westermark, C. Wernstedt, E. Wilander, DW Hayden, TD O'Brien, KH Johnson: Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells . In: Proc Natl Acad Sci U.S.A. 84 (11), 1987 Jun, pp. 3881-3885. PMID 3035556