Calpain-1 catalytic subunit explained

Calpain-1 catalytic subunit (CANP 1) is a protein that in humans is encoded by the CAPN1 gene.^{[1] [2] [3]}

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.

Interactions

CAPN1 has been shown to interact with PSEN2.^[4]

Further reading

• Suzuki K, Sorimachi H, Yoshizawa T, Kinbara K, Ishiura S . Calpain: novel family members, activation, and physiologic function . Biol. Chem. Hoppe-Seyler . 376 . 9 . 523–9 . 1996 . 8561910 . 10.1515/bchm3.1995.376.9.523.
• Huang Y, Wang KK . The calpain family and human disease . Trends in Molecular Medicine . 7 . 8 . 355–62 . 2001 . 11516996 . 10.1016/S1471-4914(01)02049-4 .
• Goll DE, Thompson VF, Li H, Wei W, Cong J . The calpain system . Physiol. Rev. . 83 . 3 . 731–801 . 2003 . 12843408 . 10.1152/physrev.00029.2002 .
• Banik NL, DeVries GH, Neuberger T, Russell T, Chakrabarti AK, Hogan EL . 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 . 1991 . 1656060 . 10.1002/jnr.490290310 . 40120102 .
• Sorimachi H, Ohmi S, Emori Y, Kawasaki H, Saido TC, Ohno S, Minami Y, Suzuki K . A novel member of the calcium-dependent cysteine protease family . Biol. Chem. Hoppe-Seyler . 371 Suppl . 171–6 . 1990 . 2400579 .
• Harris AS, Croall DE, Morrow JS . The calmodulin-binding site in alpha-fodrin is near the calcium-dependent protease-I cleavage site . J. Biol. Chem. . 263 . 30 . 15754–61 . 1988 . 10.1016/S0021-9258(19)37652-5 . 2844821 . free .
• 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 . 26 . 10 . 2863–70 . 1987 . 3038169 . 10.1021/bi00384a030 .
• Morishita R, Nakayama H, Isobe T, Matsuda T, Hashimoto Y, Okano T, Fukada Y, Mizuno K, Ohno S, Kozawa O . Primary structure of a gamma subunit of G protein, gamma 12, and its phosphorylation by protein kinase C . J. Biol. Chem. . 270 . 49 . 29469–75 . 1996 . 7493986 . 10.1074/jbc.270.49.29469 . free .
• Kavita U, Mizel SB . Differential sensitivity of interleukin-1 alpha and -beta precursor proteins to cleavage by calpain, a calcium-dependent protease . J. Biol. Chem. . 270 . 46 . 27758–65 . 1996 . 7499244 . 10.1074/jbc.270.46.27758 . free .
• Du X, Saido TC, Tsubuki S, Indig FE, Williams MJ, Ginsberg MH . Calpain cleavage of the cytoplasmic domain of the integrin beta 3 subunit . J. Biol. Chem. . 270 . 44 . 26146–51 . 1995 . 7592818 . 10.1074/jbc.270.44.26146 . free .
• Bradford HN, Jameson BA, Adam AA, Wassell RP, Colman RW . Contiguous binding and inhibitory sites on kininogens required for the inhibition of platelet calpain . J. Biol. Chem. . 268 . 35 . 26546–51 . 1994 . 10.1016/S0021-9258(19)74347-6 . 8253784 . free .
• Oda A, Ozaki K, Druker BJ, Miyakawa Y, Miyazaki H, Handa M, Morita H, Ohashi H, Ikeda Y . p120c-cbl is present in human blood platelets and is differentially involved in signaling by thrombopoietin and thrombin . Blood . 88 . 4 . 1330–8 . 1996 . 8695851 . 10.1182/blood.V88.4.1330.bloodjournal8841330. free .
• Zhang W, Lane RD, Mellgren RL . The major calpain isozymes are long-lived proteins. Design of an antisense strategy for calpain depletion in cultured cells . J. Biol. Chem. . 271 . 31 . 18825–30 . 1996 . 8702541 . 10.1074/jbc.271.31.18825 . free .
• 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 . 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 . 1997 . 8938448 . 10.1006/geno.1996.0570 .
• 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. . 229 . 1 . 299–304 . 1997 . 8954122 . 10.1006/bbrc.1996.1796 .
• Stabach PR, Cianci CD, Glantz SB, Zhang Z, Morrow JS . Site-directed mutagenesis of alpha II spectrin at codon 1175 modulates its mu-calpain susceptibility . Biochemistry . 36 . 1 . 57–65 . 1997 . 8993318 . 10.1021/bi962034i .
• Norris FA, Atkins RC, Majerus PW . Inositol polyphosphate 4-phosphatase is inactivated by calpain-mediated proteolysis in stimulated human platelets . J. Biol. Chem. . 272 . 17 . 10987–9 . 1997 . 9110986 . 10.1074/jbc.272.17.10987 . free .

External links

• The MEROPS online database for peptidases and their inhibitors: C02.001

Notes and References

1. Aoki K, Imajoh S, Ohno S, Emori Y, Koike M, Kosaki G, Suzuki K . 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 . Oct 1986 . 3017764 . 10.1016/0014-5793(86)80919-X . 36697759 .
2. 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 . 53 . 4 . 225–9 . Nov 1990 . 2209092 . 10.1159/000132937 .
3. Web site: Entrez Gene: CAPN1 calpain 1, (mu/I) large subunit.
4. Shinozaki K, Maruyama K, Kume H, Tomita T, Saido TC, Iwatsubo T, Obata K . The presenilin 2 loop domain interacts with the mu-calpain C-terminal region . Int. J. Mol. Med. . 1 . 5 . 797–9 . 1998 . 9852298 . 10.3892/ijmm.1.5.797 .