CAPN2
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
CAPN2 has been shown to interact with Bcl-2.[4]
References
- ^ 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.
- ^ 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.
- ^ "Entrez Gene: CAPN2 calpain 2, (m/II) large subunit". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=824.
- ^ 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
- 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) (Pt 1): 1–16. PMC 1218630. PMID 9337844. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1218630.
- 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=15374.
- 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
- The MEROPS online database for peptidases and their inhibitors: C02.002
|
PDB gallery
|
|
|
|
1df0: CRYSTAL STRUCTURE OF M-CALPAIN
|
|
|
1kfu: Crystal Structure of Human m-Calpain Form II
|
|
|
1kfx: Crystal Structure of Human m-Calpain Form I
|
|
|
1mdw: Crystal Structure of Calcium-Bound Protease Core of Calpain II Reveals the Basis for Intrinsic Inactivation
|
|
|
1u5i: Crystal Structure analysis of rat m-calpain mutant Lys10 Thr
|
|
|
|
|
|
|
| Caspase |
|
|
| Fruit-derived |
|
|
| Calpain |
|
|
| Cathepsin |
|
|
| Other |
|
|
|
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
|
|