鈣蛋白酶2催化亞基
外觀
鈣蛋白酶2催化亞基(英語:Calpain-2 catalytic subunit)是人類中由CAPN2基因編碼的蛋白質。[5][6]
功能
[編輯]鈣蛋白酶是鈣激活的中性蛋白酶,是非溶酶體的細胞內半胱氨酸蛋白酶。哺乳動物鈣蛋白酶包括普遍存在的胃特異性和肌肉特異性蛋白質。普遍存在的酶由異二聚體組成,這些異二聚體具有與常見的小調節亞基相關的獨特的大催化亞基。該基因編碼普遍存在的酶鈣蛋白酶2的大亞基。已報道5' UTR中存在多個異質轉錄起始位點。[7]
相互作用
[編輯]參考資料
[編輯]- ^ 1.0 1.1 1.2 GRCh38: Ensembl release 89: ENSG00000162909 - Ensembl, May 2017
- ^ 2.0 2.1 2.2 GRCm38: Ensembl release 89: ENSMUSG00000026509 - Ensembl, May 2017
- ^ Human PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Mouse PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Imajoh S, Aoki K, Ohno S, Emori Y, Kawasaki H, Sugihara H, Suzuki K. Molecular cloning of the cDNA for the large subunit of the high-Ca2+-requiring form of human Ca2+-activated neutral protease. Biochemistry. 1988, 27 (21): 8122–8. PMID 2852952. doi:10.1021/bi00421a022.
- ^ Hata A, Ohno S, Akita Y, Suzuki K. Tandemly reiterated negative enhancer-like elements regulate transcription of a human gene for the large subunit of calcium-dependent protease. J. Biol. Chem. May 1989, 264 (11): 6404–11. PMID 2539381. doi:10.1016/S0021-9258(18)83364-6 .
- ^ Entrez Gene: CAPN2 calpain 2, (m/II) large subunit.
- ^ Gil-Parrado S, Fernández-Montalván A, Assfalg-Machleidt I, Popp O, Bestvater F, Holloschi A, Knoch TA, Auerswald EA, Welsh K, Reed JC, Fritz H, Fuentes-Prior P, Spiess E, Salvesen GS, Machleidt W. Ionomycin-activated calpain triggers apoptosis. A probable role for Bcl-2 family members. J. Biol. Chem. Jul 2002, 277 (30): 27217–26. PMID 12000759. doi:10.1074/jbc.M202945200 .
延伸閱讀
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- Cohen GM. Caspases: the executioners of apoptosis. Biochem. J. 1997, 326 (Pt 1): 1–16. PMC 1218630 . PMID 9337844. doi:10.1042/bj3260001.
- Reverter D, Sorimachi H, Bode W. The structure of calcium-free human m-calpain: implications for calcium activation and function. Trends Cardiovasc. Med. 2001, 11 (6): 222–9. PMID 11673052. doi:10.1016/S1050-1738(01)00112-8.
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- Adachi Y, Kitahara-Ozawa A, Sugamura K, Lee WJ, Yodoi J, Maki M, Murachi T, Hatanaka M. Expression of calpain II gene in human hematopoietic system cells infected with human T-cell leukemia virus type I. J. Biol. Chem. 1992, 267 (27): 19373–8. PMID 1527057. doi:10.1016/S0021-9258(18)41785-1 .
- Ohno S, Minoshima S, Kudoh J, Fukuyama R, Shimizu Y, Ohmi-Imajoh S, Shimizu N, Suzuki K. Four genes for the calpain family locate on four distinct human chromosomes. Cytogenet. Cell Genet. 1990, 53 (4): 225–9. PMID 2209092. doi:10.1159/000132937.
- Ishiguro H, Higashiyama S, Namikawa C, Kunimatsu M, Takano E, Tanaka K, Ohkubo I, Murachi T, Sasaki M. Interaction of human calpains I and II with high molecular weight and low molecular weight kininogens and their heavy chain: mechanism of interaction and the role of divalent cations. Biochemistry. 1987, 26 (10): 2863–70. PMID 3038169. doi:10.1021/bi00384a030.
- Srinivasula SM, Fernandes-Alnemri T, Zangrilli J, Robertson N, Armstrong RC, Wang L, Trapani JA, Tomaselli KJ, Litwack G, Alnemri ES. The Ced-3/interleukin 1beta converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2alpha are substrates for the apoptotic mediator CPP32. J. Biol. Chem. 1996, 271 (43): 27099–106. PMID 8900201. doi:10.1074/jbc.271.43.27099 .
- Corasaniti MT, Navarra M, Catani MV, Melino G, Nisticò G, Finazzi-Agrò A. NMDA and HIV-1 coat protein, GP120, produce necrotic but not apoptotic cell death in human CHP100 neuroblastoma cultures via a mechanism involving calpain. Biochem. Biophys. Res. Commun. 1996, 229 (1): 299–304. PMID 8954122. doi:10.1006/bbrc.1996.1796.
- Fujitani K, Kambayashi J, Sakon M, Ohmi SI, Kawashima S, Yukawa M, Yano Y, Miyoshi H, Ikeda M, Shinoki N, Monden M. Identification of mu-, m-calpains and calpastatin and capture of mu-calpain activation in endothelial cells. J. Cell. Biochem. 1997, 66 (2): 197–209. PMID 9213221. S2CID 85163404. doi:10.1002/(SICI)1097-4644(19970801)66:2<197::AID-JCB7>3.0.CO;2-L.
- Rock MT, Brooks WH, Roszman TL. Calcium-dependent signaling pathways in T cells. Potential role of calpain, protein tyrosine phosphatase 1b, and p130Cas in integrin-mediated signaling events. J. Biol. Chem. 1997, 272 (52): 33377–83. PMID 9407132. doi:10.1074/jbc.272.52.33377 .
- Ueyama H, Kumamoto T, Fujimoto S, Murakami T, Tsuda T. Expression of three calpain isoform genes in human skeletal muscles. J. Neurol. Sci. 1998, 155 (2): 163–9. PMID 9562261. S2CID 205898607. doi:10.1016/S0022-510X(97)00309-2.
- Strobl S, Fernandez-Catalan C, Braun M, Huber R, Masumoto H, Nakagawa K, Irie A, Sorimachi H, Bourenkow G, Bartunik H, Suzuki K, Bode W. The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium. Proc. Natl. Acad. Sci. U.S.A. 2000, 97 (2): 588–92. Bibcode:2000PNAS...97..588S. PMC 15374 . PMID 10639123. doi:10.1073/pnas.97.2.588 .
- Masumoto H, Nakagawa K, Irie S, Sorimachi H, Suzuki K, Bourenkov GP, Bartunik H, Fernandez-Catalan C, Bode W, Strobl S. Crystallization and preliminary X-ray analysis of recombinant full-length human m-calpain. Acta Crystallogr. D. 2000, 56 (Pt 1): 73–5. Bibcode:2000AcCrD..56...73M. PMID 10666632. doi:10.1107/S0907444999013748.
- Chua BT, Guo K, Li P. Direct cleavage by the calcium-activated protease calpain can lead to inactivation of caspases. J. Biol. Chem. 2000, 275 (7): 5131–5. PMID 10671558. doi:10.1074/jbc.275.7.5131 .
- Lee MS, Kwon YT, Li M, Peng J, Friedlander RM, Tsai LH. Neurotoxicity induces cleavage of p35 to p25 by calpain. Nature. 2000, 405 (6784): 360–4. Bibcode:2000Natur.405..360L. PMID 10830966. S2CID 205006589. doi:10.1038/35012636.