CAPN2

Calpain 2, (m/II) large subunit, also known as CAPN2, is a human gene.

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: CAPN2 calpain 2, (m/II) large subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=824| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Suzuki K, Sorimachi H, Yoshizawa T, "et al." |title=Calpain: novel family members, activation, and physiologic function. |journal=Biol. Chem. Hoppe-Seyler |volume=376 |issue= 9 |pages= 523–9 |year= 1996 |pmid= 8561910 |doi=
*cite journal | author=Cohen GM |title=Caspases: the executioners of apoptosis. |journal=Biochem. J. |volume=326 ( Pt 1) |issue= |pages= 1–16 |year= 1997 |pmid= 9337844 |doi=
*cite journal | author=Reverter D, Sorimachi H, Bode W |title=The structure of calcium-free human m-calpain: implications for calcium activation and function. |journal=Trends Cardiovasc. Med. |volume=11 |issue= 6 |pages= 222–9 |year= 2001 |pmid= 11673052 |doi=
*cite journal | author=Kopp S |title=Reproducibility of response to a questionnaire on symptoms of masticatory dysfunction. |journal=Community dentistry and oral epidemiology |volume=4 |issue= 5 |pages= 205–9 |year= 1976 |pmid= 1067155 |doi=
*cite journal | author=Adachi Y, Kitahara-Ozawa A, Sugamura K, "et al." |title=Expression of calpain II gene in human hematopoietic system cells infected with human T-cell leukemia virus type I. |journal=J. Biol. Chem. |volume=267 |issue= 27 |pages= 19373–8 |year= 1992 |pmid= 1527057 |doi=
*cite journal | author=Ohno S, Minoshima S, Kudoh J, "et al." |title=Four genes for the calpain family locate on four distinct human chromosomes. |journal=Cytogenet. Cell Genet. |volume=53 |issue= 4 |pages= 225–9 |year= 1990 |pmid= 2209092 |doi=
*cite journal | author=Hata A, Ohno S, Akita Y, Suzuki K |title=Tandemly reiterated negative enhancer-like elements regulate transcription of a human gene for the large subunit of calcium-dependent protease. |journal=J. Biol. Chem. |volume=264 |issue= 11 |pages= 6404–11 |year= 1989 |pmid= 2539381 |doi=
*cite journal | author=Imajoh S, Aoki K, Ohno S, "et al." |title=Molecular cloning of the cDNA for the large subunit of the high-Ca2+-requiring form of human Ca2+-activated neutral protease. |journal=Biochemistry |volume=27 |issue= 21 |pages= 8122–8 |year= 1989 |pmid= 2852952 |doi=
*cite journal | author=Ishiguro H, Higashiyama S, Namikawa C, "et al." |title=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. |journal=Biochemistry |volume=26 |issue= 10 |pages= 2863–70 |year= 1987 |pmid= 3038169 |doi=
*cite journal | author=Srinivasula SM, Fernandes-Alnemri T, Zangrilli J, "et al." |title=The Ced-3/interleukin 1beta converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2alpha are substrates for the apoptotic mediator CPP32. |journal=J. Biol. Chem. |volume=271 |issue= 43 |pages= 27099–106 |year= 1996 |pmid= 8900201 |doi=
*cite journal | author=Corasaniti MT, Navarra M, Catani MV, "et al." |title=NMDA and HIV-1 coat protein, GP120, produce necrotic but not apoptotic cell death in human CHP100 neuroblastoma cultures via a mechanism involving calpain. |journal=Biochem. Biophys. Res. Commun. |volume=229 |issue= 1 |pages= 299–304 |year= 1997 |pmid= 8954122 |doi= 10.1006/bbrc.1996.1796
*cite journal | author=Fujitani K, Kambayashi J, Sakon M, "et al." |title=Identification of mu-, m-calpains and calpastatin and capture of mu-calpain activation in endothelial cells. |journal=J. Cell. Biochem. |volume=66 |issue= 2 |pages= 197–209 |year= 1997 |pmid= 9213221 |doi=
*cite journal | author=Rock MT, Brooks WH, Roszman TL |title=Calcium-dependent signaling pathways in T cells. Potential role of calpain, protein tyrosine phosphatase 1b, and p130Cas in integrin-mediated signaling events. |journal=J. Biol. Chem. |volume=272 |issue= 52 |pages= 33377–83 |year= 1998 |pmid= 9407132 |doi=
*cite journal | author=Ueyama H, Kumamoto T, Fujimoto S, "et al." |title=Expression of three calpain isoform genes in human skeletal muscles. |journal=J. Neurol. Sci. |volume=155 |issue= 2 |pages= 163–9 |year= 1998 |pmid= 9562261 |doi=
*cite journal | author=Strobl S, Fernandez-Catalan C, Braun M, "et al." |title=The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 2 |pages= 588–92 |year= 2000 |pmid= 10639123 |doi=
*cite journal | author=Masumoto H, Nakagawa K, Irie S, "et al." |title=Crystallization and preliminary X-ray analysis of recombinant full-length human m-calpain. |journal=Acta Crystallogr. D Biol. Crystallogr. |volume=56 |issue= Pt 1 |pages= 73–5 |year= 2000 |pmid= 10666632 |doi=
*cite journal | author=Chua BT, Guo K, Li P |title=Direct cleavage by the calcium-activated protease calpain can lead to inactivation of caspases. |journal=J. Biol. Chem. |volume=275 |issue= 7 |pages= 5131–5 |year= 2000 |pmid= 10671558 |doi=
*cite journal | author=Lee MS, Kwon YT, Li M, "et al." |title=Neurotoxicity induces cleavage of p35 to p25 by calpain. |journal=Nature |volume=405 |issue= 6784 |pages= 360–4 |year= 2000 |pmid= 10830966 |doi= 10.1038/35012636

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