アミリン (ホルモン)
出典: フリー百科事典『ウィキペディア(Wikipedia)』 (2021/10/23 03:37 UTC 版)
アミリン(英: amylin)または膵島アミロイドポリペプチド(英: islet amyloid polypeptide、略称: IAPP)は、37残基からなるペプチドホルモンである[4]。アミリンは膵臓のβ細胞からインスリンとともに分泌される(インスリン:アミリン比は約100:1)。アミリンは胃の内容物排出速度を低下させて満腹感を促進することで血糖値の調節に関与し、食後の血糖値スパイクを防ぐ。
- ^ a b c GRCh38: Ensembl release 89: ENSG00000121351 - Ensembl, May 2017
- ^ Human PubMed Reference:
- ^ Mouse PubMed Reference:
- ^ “Entrez Gene: IAPP islet amyloid polypeptide”. 2021年10月16日閲覧。
- ^ a b c “Processing of synthetic pro-islet amyloid polypeptide (proIAPP) 'amylin' by recombinant prohormone convertase enzymes, PC2 and PC3, in vitro”. Eur. J. Biochem. 267 (16): 4998–5004. (August 2000). doi:10.1046/j.1432-1327.2000.01548.x. PMID 10931181.
- ^ “islet amyloid polypeptide precursor [Homo sapiens]”. NCBI. 2021年10月17日閲覧。 (the current NCBI RefSeq)
- ^ a b c “Molecular and functional characterization of amylin, a peptide associated with type 2 diabetes mellitus”. Proc. Natl. Acad. Sci. U.S.A. 86 (24): 9662–6. (December 1989). Bibcode: 1989PNAS...86.9662R. doi:10.1073/pnas.86.24.9662. PMC 298561. PMID 2690069 .
- ^ “An islet amyloid peptide is derived from an 89-amino acid precursor by proteolytic processing”. J. Biol. Chem. 263 (33): 17243–6. (November 1988). doi:10.1016/S0021-9258(19)77825-9. PMID 3053705 .
- ^ a b “Role of carboxypeptidase E in processing of pro-islet amyloid polypeptide in {beta}-cells”. Endocrinology 146 (4): 1808–17. (April 2005). doi:10.1210/en.2004-1175. PMID 15618358.
- ^ Defronzo RA (2009). “Banting Lecture. From the triumvirate to the ominous octet: a new paradigm for the treatment of type 2 diabetes mellitus”. Diabetes 58 (4): 773–795. doi:10.2337/db09-9028. PMC 2661582. PMID 19336687 .
- ^ “Islet amyloid and type 2 diabetes mellitus”. N. Engl. J. Med. 343 (6): 411–9. (August 2000). doi:10.1056/NEJM200008103430607. PMID 10933741.
- ^ “TNF-α acutely upregulates amylin expression in murine pancreatic beta cells”. Diabetologia 54 (3): 617–26. (March 2011). doi:10.1007/s00125-010-1972-9. PMID 21116608.
- ^ “Fatty acids induce amylin expression and secretion by pancreatic beta-cells”. Am. J. Physiol. Endocrinol. Metab. 298 (1): E99–E107. (January 2010). doi:10.1152/ajpendo.00242.2009. PMID 19843871.
- ^ a b “Molecular physiology of amylin”. J. Cell. Biochem. 55 Suppl: 19–28. (1994). doi:10.1002/jcb.240550004. PMID 7929615.
- ^ “Amylin replacement with pramlintide as an adjunct to insulin therapy improves long-term glycaemic and weight control in Type 1 diabetes mellitus: a 1-year, randomized controlled trial”. Diabetic Medicine 21 (11): 1204–12. (2004). doi:10.1111/j.1464-5491.2004.01319.x. PMID 15498087.
- ^ “Amyloid fiber formation and membrane disruption are separate processes localized in two distinct regions of IAPP, the type-2-diabetes-related peptide”. J. Am. Chem. Soc. 130 (20): 6424–9. (May 2008). doi:10.1021/ja710484d. PMC 4163023. PMID 18444645 .
- ^ “A single mutation in the nonamyloidogenic region of islet amyloid polypeptide greatly reduces toxicity”. Biochemistry 47 (48): 12680–8. (December 2008). doi:10.1021/bi801427c. PMC 2645932. PMID 18989933 .
- ^ “Structures of rat and human islet amyloid polypeptide IAPP(1-19) in micelles by NMR spectroscopy”. Biochemistry 47 (48): 12689–97. (December 2008). doi:10.1021/bi8014357. PMC 2953382. PMID 18989932 .
- ^ “Membrane Fragmentation by an Amyloidogenic Fragment of Human Islet Amyloid Polypeptide Detected by Solid-State NMR Spectroscopy of Membrane Nanotubes”. Biochim. Biophys. Acta 1768 (9): 2026–9. (September 2007). doi:10.1016/j.bbamem.2007.07.001. PMC 2042489. PMID 17662957 .
- ^ Palmieri, Leonardo C; Melo-Ferreira, Bruno; Braga, Carolina A; Fontes, Giselle N; Mattos, Luana J; Lima, Luis Mauricio (2013). “Stepwise oligomerization of murine amylin and assembly of amyloid fibrils”. Biophys Chem 181: 135–144. doi:10.1016/j.bpc.2013.07.013. PMID 23974296.
- ^ Erthal, Luiza C; Marques, Adriana F; Almeida, Fábio C; Melo, Gustavo L; Carvalho, Camila M; Palmieri, Leonardo C; Cabral, Kátia M; Fontes, Giselle N; Lima, Luis Mauricio (2016). “Regulation of the assembly and amyloid aggregation of murine amylin by zinc”. Biophys. Chem. 218: 58–70. doi:10.1016/j.bpc.2016.09.008. PMID 27693831.
- ^ “Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients”. Proc Natl Acad Sci USA 84 (23): 8628–32. (1987). Bibcode: 1987PNAS...84.8628C. doi:10.1073/pnas.84.23.8628. PMC 299599. PMID 3317417 .
- ^ “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 USA 84 (11): 3881–3885. (1987). Bibcode: 1987PNAS...84.3881W. doi:10.1073/pnas.84.11.3881. PMC 304980. PMID 3035556 .
- ^ “Aberrant processing of human proislet amyloid polypeptide results in increased amyloid formation”. Diabetes 54 (7): 2117–25. (July 2005). doi:10.2337/diabetes.54.7.2117. PMID 15983213.
- ^ a b c “Impaired NH2-terminal processing of human proislet amyloid polypeptide by the prohormone convertase PC2 leads to amyloid formation and cell death”. Diabetes 55 (8): 2192–201. (August 2006). doi:10.2337/db05-1566. PMID 16873681.
- ^ a b “Intracellular amyloid-like deposits contain unprocessed pro-islet amyloid polypeptide (proIAPP) in beta cells of transgenic mice overexpressing the gene for human IAPP and transplanted human islets”. Diabetologia 49 (6): 1237–46. (June 2006). doi:10.1007/s00125-006-0206-7. PMID 16570161.
- ^ Hayden MR (September 2002). “Islet amyloid, metabolic syndrome, and the natural progressive history of type 2 diabetes mellitus”. JOP 3 (5): 126–38. PMID 12221327.
- ^ “Abeta and human amylin share a common toxicity pathway via mitochondrial dysfunction”. Proteomics 10 (8): 1621–33. (April 2010). doi:10.1002/pmic.200900651. PMID 20186753.
- ^ “Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus”. Nature 368 (6473): 756–60. (April 1994). Bibcode: 1994Natur.368..756L. doi:10.1038/368756a0. PMID 8152488.
- ^ “Leptin responsiveness restored by amylin agonism in diet-induced obesity: evidence from nonclinical and clinical studies”. Proc. Natl. Acad. Sci. U.S.A. 105 (20): 7257–62. (May 2008). Bibcode: 2008PNAS..105.7257R. doi:10.1073/pnas.0706473105. PMC 2438237. PMID 18458326 .
- ^ Facebook (2011年3月16日). “Amylin halts trial of weight-loss therapy” (英語). San Diego Union-Tribune. 2021年10月23日閲覧。
- ^ “【武田薬品/アミリン】抗肥満薬「プラムリンタイド/メトレレプチン」の開発を中止|薬事日報ウェブサイト”. 2021年10月23日閲覧。
- ^ “SYMLIN (pramlintide acetate)”. Amylin Pharmaceuticals, Inc. (2006年). 2008年5月28日閲覧。
- ^ “Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism”. Nature 443 (7113): 870–4. (October 2006). Bibcode: 2006Natur.443..870S. doi:10.1038/nature05143. PMC 3366509. PMID 17051221 .
- ^ Suva, Manoj (July 2015). “Role of Amylin in Obesity”. Journal of PharmaSciTech 5: 5–10 .
- ^ “Amylin receptors: molecular composition and pharmacology”. Biochem. Soc. Trans. 32 (Pt 5): 865–7. (November 2004). doi:10.1042/BST0320865. PMID 15494035.
- 1 アミリン (ホルモン)とは
- 2 アミリン (ホルモン)の概要
- 3 合成
- 4 構造
- 5 薬理
- 6 外部リンク
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