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Calpain-1 catalytic subunit(CANP 1) is a protein that in humans is encoded by the CAPN1gene.[5][6][7]
Function
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 1.[7]
^"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.
^Aoki K, Imajoh S, Ohno S, Emori Y, Koike M, Kosaki G, Suzuki K (Oct 1986). "Complete amino acid sequence of the large subunit of the low-Ca2+-requiring form of human Ca2+-activated neutral protease (muCANP) deduced from its cDNA sequence". FEBS Lett. 205 (2): 313–7. doi:10.1016/0014-5793(86)80919-X. PMID3017764. S2CID36697759.
^Ohno S, Minoshima S, Kudoh J, Fukuyama R, Shimizu Y, Ohmi-Imajoh S, Shimizu N, Suzuki K (Nov 1990). "Four genes for the calpain family locate on four distinct human chromosomes". Cytogenet Cell Genet. 53 (4): 225–9. doi:10.1159/000132937. PMID2209092.
Banik NL, DeVries GH, Neuberger T, Russell T, Chakrabarti AK, Hogan EL (1991). "Calcium-activated neutral proteinase (CANP; calpain) activity in Schwann cells: immunofluorescence localization and compartmentation of mu- and mCANP". J. Neurosci. Res. 29 (3): 346–54. doi:10.1002/jnr.490290310. PMID1656060. S2CID40120102.
Sorimachi H, Ohmi S, Emori Y, Kawasaki H, Saido TC, Ohno S, Minami Y, Suzuki K (1990). "A novel member of the calcium-dependent cysteine protease family". Biol. Chem. Hoppe-Seyler. 371 Suppl: 171–6. PMID2400579.
Ishiguro H, Higashiyama S, Namikawa C, Kunimatsu M, Takano E, Tanaka K, Ohkubo I, Murachi T, Sasaki M (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. PMID3038169.
Courseaux A, Grosgeorge J, Gaudray P, Pannett AA, Forbes SA, Williamson C, Bassett D, Thakker RV, Teh BT, Farnebo F, Shepherd J, Skogseid B, Larsson C, Giraud S, Zhang CX, Salandre J, Calender A (1997). "Definition of the minimal MEN1 candidate area based on a 5-Mb integrated map of proximal 11q13. The European Consortium on Men1, (GENEM 1; Groupe d'Etude des Néoplasies Endocriniennes Multiples de type 1)". Genomics. 37 (3): 354–65. doi:10.1006/geno.1996.0570. PMID8938448.
Corasaniti MT, Navarra M, Catani MV, Melino G, Nisticò G, Finazzi-Agrò A (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. PMID8954122.
Stabach PR, Cianci CD, Glantz SB, Zhang Z, Morrow JS (1997). "Site-directed mutagenesis of alpha II spectrin at codon 1175 modulates its mu-calpain susceptibility". Biochemistry. 36 (1): 57–65. doi:10.1021/bi962034i. PMID8993318.
This page was last edited on 10 March 2024, at 02:05