CAPN2

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Calpain 2, (m/II) large subunit
Protein CAPN2 PDB 1df0.png
PDB rendering based on 1df0.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols CAPN2 ; CANP2; CANPL2; CANPml; mCANP
External IDs OMIM114230 MGI88264 HomoloGene1326 ChEMBL: 2382 GeneCards: CAPN2 Gene
EC number 3.4.22.53
RNA expression pattern
PBB GE CAPN2 208683 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 824 12334
Ensembl ENSG00000162909 ENSMUSG00000026509
UniProt P17655 O08529
RefSeq (mRNA) NM_001146068 NM_009794
RefSeq (protein) NP_001139540 NP_033924
Location (UCSC) Chr 1:
223.89 – 223.96 Mb
Chr 1:
182.47 – 182.52 Mb
PubMed search [1] [2]

Calpain-2 catalytic subunit is a protein that in humans is encoded by the CAPN2 gene.[1][2]

The calpains, calcium-activated neutral proteases, are nonlysosomal, intracellular cysteine proteases. The mammalian calpains include ubiquitous, stomach-specific, and muscle-specific proteins. The ubiquitous enzymes consist of heterodimers with distinct large, catalytic subunits associated with a common small, regulatory subunit. This gene encodes the large subunit of the ubiquitous enzyme, calpain 2. Multiple heterogeneous transcriptional start sites in the 5' UTR have been reported.[3]

Interactions[edit]

CAPN2 has been shown to interact with Bcl-2.[4]

References[edit]

  1. ^ Imajoh S, Aoki K, Ohno S, Emori Y, Kawasaki H, Sugihara H, Suzuki K (May 1989). "Molecular cloning of the cDNA for the large subunit of the high-Ca2+-requiring form of human Ca2+-activated neutral protease". Biochemistry 27 (21): 8122–8. doi:10.1021/bi00421a022. PMID 2852952. 
  2. ^ Hata A, Ohno S, Akita Y, Suzuki K (May 1989). "Tandemly reiterated negative enhancer-like elements regulate transcription of a human gene for the large subunit of calcium-dependent protease". J Biol Chem 264 (11): 6404–11. PMID 2539381. 
  3. ^ "Entrez Gene: CAPN2 calpain 2, (m/II) large subunit". 
  4. ^ Gil-Parrado, Shirley; Fernández-Montalván Amaury, Assfalg-Machleidt Irmgard, Popp Oliver, Bestvater Felix, Holloschi Andreas, Knoch Tobias A, Auerswald Ennes A, Welsh Katherine, Reed John C, Fritz Hans, Fuentes-Prior Pablo, Spiess Eberhard, Salvesen Guy S, Machleidt Werner (Jul 2002). "Ionomycin-activated calpain triggers apoptosis. A probable role for Bcl-2 family members". J. Biol. Chem. (United States) 277 (30): 27217–26. doi:10.1074/jbc.M202945200. ISSN 0021-9258. PMID 12000759. 

Further reading[edit]

  • Suzuki K, Sorimachi H, Yoshizawa T et al. (1996). "Calpain: novel family members, activation, and physiologic function". Biol. Chem. Hoppe-Seyler 376 (9): 523–9. PMID 8561910. 
  • Cohen GM (1997). "Caspases: the executioners of apoptosis". Biochem. J. 326 (Pt 1): 1–16. PMC 1218630. PMID 9337844. 
  • Reverter D, Sorimachi H, Bode W (2001). "The structure of calcium-free human m-calpain: implications for calcium activation and function". Trends Cardiovasc. Med. 11 (6): 222–9. doi:10.1016/S1050-1738(01)00112-8. PMID 11673052. 
  • Kopp S (1976). "Reproducibility of response to a questionnaire on symptoms of masticatory dysfunction". Community dentistry and oral epidemiology 4 (5): 205–9. doi:10.1111/j.1600-0528.1976.tb00985.x. PMID 1067155. 
  • Adachi Y, Kitahara-Ozawa A, Sugamura K et al. (1992). "Expression of calpain II gene in human hematopoietic system cells infected with human T-cell leukemia virus type I". J. Biol. Chem. 267 (27): 19373–8. PMID 1527057. 
  • Ohno S, Minoshima S, Kudoh J et al. (1990). "Four genes for the calpain family locate on four distinct human chromosomes". Cytogenet. Cell Genet. 53 (4): 225–9. doi:10.1159/000132937. PMID 2209092. 
  • Ishiguro H, Higashiyama S, Namikawa C et al. (1987). "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 26 (10): 2863–70. doi:10.1021/bi00384a030. PMID 3038169. 
  • Srinivasula SM, Fernandes-Alnemri T, Zangrilli J et al. (1996). "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. 271 (43): 27099–106. doi:10.1074/jbc.271.43.27099. PMID 8900201. 
  • Corasaniti MT, Navarra M, Catani MV et al. (1997). "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. 229 (1): 299–304. doi:10.1006/bbrc.1996.1796. PMID 8954122. 
  • Fujitani K, Kambayashi J, Sakon M et al. (1997). "Identification of mu-, m-calpains and calpastatin and capture of mu-calpain activation in endothelial cells". J. Cell. Biochem. 66 (2): 197–209. doi:10.1002/(SICI)1097-4644(19970801)66:2<197::AID-JCB7>3.0.CO;2-L. PMID 9213221. 
  • Rock MT, Brooks WH, Roszman TL (1998). "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. 272 (52): 33377–83. doi:10.1074/jbc.272.52.33377. PMID 9407132. 
  • Ueyama H, Kumamoto T, Fujimoto S et al. (1998). "Expression of three calpain isoform genes in human skeletal muscles". J. Neurol. Sci. 155 (2): 163–9. doi:10.1016/S0022-510X(97)00309-2. PMID 9562261. 
  • Strobl S, Fernandez-Catalan C, Braun M et al. (2000). "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. 97 (2): 588–92. doi:10.1073/pnas.97.2.588. PMC 15374. PMID 10639123. 
  • Masumoto H, Nakagawa K, Irie S et al. (2000). "Crystallization and preliminary X-ray analysis of recombinant full-length human m-calpain". Acta Crystallogr. D Biol. Crystallogr. 56 (Pt 1): 73–5. doi:10.1107/S0907444999013748. PMID 10666632. 
  • Chua BT, Guo K, Li P (2000). "Direct cleavage by the calcium-activated protease calpain can lead to inactivation of caspases". J. Biol. Chem. 275 (7): 5131–5. doi:10.1074/jbc.275.7.5131. PMID 10671558. 
  • Lee MS, Kwon YT, Li M et al. (2000). "Neurotoxicity induces cleavage of p35 to p25 by calpain". Nature 405 (6784): 360–4. doi:10.1038/35012636. PMID 10830966. 

External links[edit]

  • The MEROPS online database for peptidases and their inhibitors: C02.002