Amylin
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
- ↑ tumaini.de: Amylin ( Memento from November 9, 2007 in the Internet Archive )
- ↑ UniProt P10997
- ↑ medicalforum.ch: Regulation of food intake by amylin and related peptides. (PDF; 85 kB)
- ↑ 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