Amilin
Amilin (ostrvaca amiloidnog polipeptida, IAPP) je 37 aminokiselina dug peptidni hormon. On se izlučuje zajedno sa insulinom iz pankreasnih β-ćelija u odnosu od oko 100:1.[1] Amilin učestvuje u glicemičkog regulaciji putem usporavanja gastričkog pražnjenja i promovisanja sitosti, čime sprećava postprandijalna nagla povišenja nivoa krvne glukoze.
| ostrvaca amiloidnog polipeptida | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Dostupne strukture | |||||||||||
| 1KUW, 2G48, 2KB8, 2L86, 3FPO, 3FR1, 3FTH, 3FTK, 3FTL, 3FTR, 3G7V, 3G7W, 3HGZ | |||||||||||
| Identifikatori | |||||||||||
| Simboli | IAPP; DAP; IAP | ||||||||||
| Vanjski ID | OMIM: 147940 MGI: 96382 HomoloGene: 36024 GeneCards: IAPP Gene | ||||||||||
| |||||||||||
| Pregled RNK izražavanja | |||||||||||
 | |||||||||||
| podaci | |||||||||||
| Ortolozi | |||||||||||
| Vrsta | Čovek | Miš | |||||||||
| Entrez | 3375 | 15874 | |||||||||
| Ensembl | ENSG00000121351 | ENSMUSG00000041681 | |||||||||
| UniProt | P10997 | P12968 | |||||||||
| RefSeq (mRNA) | NM_000415.2 | NM_010491.2 | |||||||||
| RefSeq (protein) | NP_000406.1 | NP_034621.1 | |||||||||
| Lokacija (UCSC) |
Chr 12: 21.51 - 21.53 Mb |
Chr 6: 142.3 - 142.3 Mb | |||||||||
| PubMed pretraga | [1] | [2] | |||||||||
IAPP se formira iz 89 aminokiseline duge kodirajuće sekvence. Proostvce amiloidni polipeptid (proIAPP, proamilin, amiloidni polipeptidni prekurzor, proostrvce protein) se formira u pankreasnim beta-ćelijama kao peptid sa 67 aminokiselina, 7404 Daltona težak propeptid i on podleže posttranslacionoj modifikaciji uključujući proteazno presecanje da se formira amilin.[2]
Reference уреди
- ^ „Entrez Gene: IAPP islet amyloid polypeptide”.
- ^ Higham, C. E., Hull, R. L., Lawrie, L., Shennan, K. I. H., Morris, J. F., Birch, N. P., Dochery, K., & Clark, A. (2000). „Processing of synthetic pro-islet amyloid polypeptide (proIAPP) `amylin' by recombinant prohormone convertase enzymes, PC2 and PC3, in vitro.”. 267. European Journal of Biochemistry: 4998—5004. Архивирано из оригинала 20. 03. 2006. г. Приступљено 27. 12. 2012.
Literatura уреди
- Westermark P, Andersson A, Westermark GT (2005). „Is aggregated IAPP a cause of beta-cell failure in transplanted human pancreatic islets?”. Curr. Diab. Rep. 5 (3): 184—8. PMID 15929864. doi:10.1007/s11892-005-0007-2.
- JW, Höppener; Oosterwijk C; Visser-Vernooy HJ (1993). „Characterization of the human islet amyloid polypeptide/amylin gene transcripts: identification of a new polyadenylation site”. Biochem. Biophys. Res. Commun. 189 (3): 1569—77. PMID 1282806. doi:10.1016/0006-291X(92)90255-J.
- JA, Hubbard; Martin SR; Chaplin LC (1991). „Solution structures of calcitonin-gene-related-peptide analogues of calcitonin-gene-related peptide and amylin”. Biochem. J. 275 (Pt 3): 785—8. PMC 1150122
. PMID 2039456. - PC, Butler; Chou J; Carter WB (1990). „Effects of meal ingestion on plasma amylin concentration in NIDDM and nondiabetic humans”. Diabetes. 39 (6): 752—6. PMID 2189768. doi:10.2337/diabetes.39.6.752.
- AD, van Mansfeld; Mosselman S; Höppener JW (1990). „Islet amyloid polypeptide: structure and upstream sequences of the IAPP gene in rat and man”. Biochim. Biophys. Acta. 1087 (2): 235—40. PMID 2223885. doi:10.1016/0167-4781(90)90210-S.
- L, Christmanson; Rorsman F; Stenman G (1990). „The human islet amyloid polypeptide (IAPP) gene. Organization, chromosomal localization and functional identification of a promoter region”. FEBS Lett. 267 (1): 160—6. PMID 2365085. doi:10.1016/0014-5793(90)80314-9.
- A, Clark; Edwards CA; Ostle LR (1989). „Localisation of islet amyloid peptide in lipofuscin bodies and secretory granules of human B-cells and in islets of type-2 diabetic subjects”. Cell Tissue Res. 257 (1): 179—85. PMID 2546670. doi:10.1007/BF00221649.
- M, Nishi; Sanke T; Seino S (1990). „Human islet amyloid polypeptide gene: complete nucleotide sequence, chromosomal localization, and evolutionary history”. Mol. Endocrinol. 3 (11): 1775—81. PMID 2608057. doi:10.1210/mend-3-11-1775.
- Mosselman S, Höppener JW, Lips CJ, Jansz HS (1989). „The complete islet amyloid polypeptide precursor is encoded by two exons”. FEBS Lett. 247 (1): 154—8. PMID 2651160. doi:10.1016/0014-5793(89)81260-8.
- P, Westermark; Wernstedt C; Wilander E (1987). „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”. Proc. Natl. Acad. Sci. U.S.A. 84 (11): 3881—5. PMC 304980 . PMID 3035556. doi:10.1073/pnas.84.11.3881.
- S, Mosselman; Höppener JW; Zandberg J (1988). „Islet amyloid polypeptide: identification and chromosomal localization of the human gene”. FEBS Lett. 239 (2): 227—32. PMID 3181427. doi:10.1016/0014-5793(88)80922-0.
- GJ, Cooper; Willis AC; Clark A (1988). „Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients”. Proc. Natl. Acad. Sci. U.S.A. 84 (23): 8628—32. PMC 299599 . PMID 3317417. doi:10.1073/pnas.84.23.8628.
- Westermark P, Wernstedt C, Wilander E, Sletten K (1986). „A novel peptide in the calcitonin gene related peptide family as an amyloid fibril protein in the endocrine pancreas”. Biochem. Biophys. Res. Commun. 140 (3): 827—31. PMID 3535798. doi:10.1016/0006-291X(86)90708-4.
- JW, Höppener; Verbeek JS; EJ, de Koning (1994). „Chronic overproduction of islet amyloid polypeptide/amylin in transgenic mice: lysosomal localization of human islet amyloid polypeptide and lack of marked hyperglycaemia or hyperinsulinaemia”. Diabetologia. 36 (12): 1258—65. PMID 8307253. doi:10.1007/BF00400803.
- Lim YA, Ittner LM, Lim YL, Götz J (2008). „Human but not rat amylin shares neurotoxic properties with Abeta42 in long-term hippocampal and cortical cultures”. FEBS Lett. 582 (15): 2188—2194. PMID 18486611. doi:10.1016/j.febslet.2008.05.006.
Vidi još уреди
Spoljašnje veze уреди
- amylin на US National Library of Medicine Medical Subject Headings (MeSH)
- „Amylin Nucleation Site”. PDB entry 1KUW. RCSB Protein Data Bank. Архивирано из оригинала 16. 04. 2008. г. Приступљено 28. 5. 2008.