Amilin
| 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:147940MGI:96382HomoloGene:36024GeneCards:IAPP Gene | ||||||||||
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| Pregled RNK izražavanja | |||||||||||
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| 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 | |||||||||
| PubMedpretraga | [1] | [2] | |||||||||
Amilin(ostrvaca amiloidnog polipeptida,IAPP) je 37 aminokiselina dugpeptidni hormon.On se izlučuje zajedno sainsulinomiz pankreasnihβ-ćelijau odnosu od oko 100:1.[1]Amilin učestvuje u glicemičkog regulaciji putem usporavanja gastričkog pražnjenja i promovisanja sitosti, čime sprećavapostprandijalnanagla povišenja nivoa krvneglukoze.
IAPP se formira iz 89 aminokiseline duge kodirajuće sekvence.Proostvce amiloidni polipeptid(proIAPP, proamilin, amiloidni polipeptidni prekurzor, proostrvce protein) se formira u pankreasnimbeta-ćelijamakao peptid sa 67 aminokiselina, 7404 Daltona težak propeptid i on podležeposttranslacionoj modifikacijiuključujući proteazno presecanje da se formira amilin.[2]
Reference
[уреди|уреди извор]- ^„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 изоригинала20. 03. 2006. г.Приступљено27. 12. 2012.
Literatura
[уреди|уреди извор]- 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.PMID15929864.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.PMID1282806.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.PMC1150122
.PMID2039456. - 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.PMID2189768.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.PMID2223885.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.PMID2365085.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.PMID2546670.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.PMID2608057.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.PMID2651160.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.PMC304980 .PMID3035556.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.PMID3181427.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.PMC299599 .PMID3317417.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.PMID3535798.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.PMID8307253.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.PMID18486611.doi:10.1016/j.febslet.2008.05.006.
Vidi još
[уреди|уреди извор]- Pramlintid
- Diabetes melitus tip 2
- Proproteinska konvertaza 2(PC2)
- Proproteinska konvertaza 1/3 (PC1/3)
- Karboksipeptidaza E
Spoljašnje veze
[уреди|уреди извор]- amylinнаUS National Library of Medicine Medical Subject Headings(MeSH)
- „Amylin Nucleation Site”.PDB entry 1KUW.RCSB Protein Data Bank.Архивирано изоригинала16. 04. 2008. г.Приступљено28. 5. 2008.
