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Gene Review

CAPN2  -  calpain 2, (m/II) large subunit

Homo sapiens

Synonyms: CANP 2, CANP2, CANPL2, CANPml, Calcium-activated neutral proteinase 2, ...
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Disease relevance of CAPN2

  • The rapid autolysis of the 27-Kd subunit to a 18-Kd intermediate when CANP is exposed to calcium may explain differences between our results and previous reports, which describe brain mCANP in other species as a 76-80-Kd monomer or a heterodimer containing 76-80-Kd and 17-20-Kd subunits [1].
  • Vimentin from ascites tumor cells was degraded most rapidly and no difference was observed in degradation velocity between muCANP and mCANP [2].
  • Since the increase in the level of platelet mCANP was found in all affected boys (no false negatives) and obligate carriers, and patients with other myopathic conditions and some neurogenic causes did not show high platelet mCANP activity, this parameter could be considered as a good phenotypic index [3].
  • Increased M-calpain expression in the mesencephalon of patients with Parkinson's disease but not in other neurodegenerative disorders involving the mesencephalon: a role in nerve cell death [4]?

High impact information on CAPN2

  • Molecular downregulation or RNA interference-mediated depletion of mu-calpain (calpain 1) but not M-calpain (calpain 2) blocked IP-9-induced calpain activation and motility [5].
  • In comparison, EGF-induced motility of the same undifferentiated keratinocytes requires the previously described extracellular signal-regulated kinase to the M-calpain pathway [5].
  • A chimeric form (L-mu mCANP) composed by domains I-III of muCANP and domain IV of calpain II (mCANP, the low Ca2+ affinity form) was also expressed in Sf9 cells [6].
  • To understand the mechanism regulating the expression of CANP at the transcriptional level, we isolated a human gene for the large subunit of mCANP (CANP mL) and analyzed its 5'-region [7].
  • The N-terminal half of the human BCCIP ICD shares moderate homology with regions of calmodulin and M-calpain, suggesting that BCCIP may also bind Ca [8].

Biological context of CAPN2

  • Moreover, treatment with the pan-calpain inhibitor ALLN and isoform-specific downregulation of m-calpain (CAPN2) using RNA interference determined m-calpain to be a key component of the EGF-induced force response [9].
  • Transactivation of capn2 by myogenic regulatory factors during myogenesis [10].
  • To study the regulation of m-calpain, the DNA sequence upstream of capn2 was analyzed for promoter elements, revealing the existence of five consensus-binding sites (E-box) for several myogenic regulatory factors and one binding site for myocyte enhancer factor-2 (MEF-2) [10].
  • In all cases, muCANP and mCANP produced different proteolytic peptide fragments, suggesting the different substrate-specificities of these CANPs [2].
  • Unlike SCK, the platelet mCANP of carriers did not overlap that of controls, hence tests are to be carried out to verify its usefulness as an index of carrier state in mutations other than DNA deletion since testing of non-deletion is both costly and has practical limitations [3].

Anatomical context of CAPN2


Associations of CAPN2 with chemical compounds


Other interactions of CAPN2

  • However, our results do not allow conclusions on the function of CAPN1 and CAPN2 in BCCs and SCCs [17].
  • We have analysed the expression of CAP1 and CAPN2 protein and mRNA expression in BCCs and SCCs of human skin [17].

Analytical, diagnostic and therapeutic context of CAPN2


  1. Calcium-activated neutral proteinase of human brain: subunit structure and enzymatic properties of multiple molecular forms. Vitto, A., Nixon, R.A. J. Neurochem. (1986) [Pubmed]
  2. Hydrolytic and autolytic behavior of two forms of calcium-activated neutral protease (CANP). Inomata, M., Hayashi, M., Nakamura, M., Imahori, K., Kawashima, S. J. Biochem. (1985) [Pubmed]
  3. Importance of monitoring calcium & calcium related properties in carrier detection for Duchenne muscular dystrophy. Jagadeesh, G., Shailaja, B., Moses, L., Kumari, C.K., Anjaneyulu, A., Anandaraj, M.P. Indian J. Med. Res. (1994) [Pubmed]
  4. Increased M-calpain expression in the mesencephalon of patients with Parkinson's disease but not in other neurodegenerative disorders involving the mesencephalon: a role in nerve cell death? Mouatt-Prigent, A., Karlsson, J.O., Agid, Y., Hirsch, E.C. Neuroscience (1996) [Pubmed]
  5. Interferon-inducible protein 9 (CXCL11)-induced cell motility in keratinocytes requires calcium flux-dependent activation of mu-calpain. Satish, L., Blair, H.C., Glading, A., Wells, A. Mol. Cell. Biol. (2005) [Pubmed]
  6. Functional properties of recombinant calpain I and of mutants lacking domains III and IV of the catalytic subunit. Vilei, E.M., Calderara, S., Anagli, J., Berardi, S., Hitomi, K., Maki, M., Carafoli, E. J. Biol. Chem. (1997) [Pubmed]
  7. Tandemly reiterated negative enhancer-like elements regulate transcription of a human gene for the large subunit of calcium-dependent protease. Hata, A., Ohno, S., Akita, Y., Suzuki, K. J. Biol. Chem. (1989) [Pubmed]
  8. Inhibition of breast and brain cancer cell growth by BCCIPalpha, an evolutionarily conserved nuclear protein that interacts with BRCA2. Liu, J., Yuan, Y., Huan, J., Shen, Z. Oncogene (2001) [Pubmed]
  9. Multiple signaling pathways mediate compaction of collagen matrices by EGF-stimulated fibroblasts. Smith, K.D., Wells, A., Lauffenburger, D.A. Exp. Cell Res. (2006) [Pubmed]
  10. Transactivation of capn2 by myogenic regulatory factors during myogenesis. Dedieu, S., Mazères, G., Dourdin, N., Cottin, P., Brustis, J.J. J. Mol. Biol. (2003) [Pubmed]
  11. Immunoassay and activity of calcium-activated neutral proteinase (mCANP): distribution in soluble and membrane-associated fractions in human and mouse brain. Takeuchi, K.H., Saito, K.I., Nixon, R.A. J. Neurochem. (1992) [Pubmed]
  12. Multiple proteases regulate neurite outgrowth in NB2a/dl neuroblastoma cells. Shea, T.B., Beermann, M.L., Nixon, R.A. J. Neurochem. (1991) [Pubmed]
  13. Ganglioside-modulated proteolysis by Ca2(+)-activated neutral proteinase (CANP): a role of glycoconjugates in CANP regulation. Chakrabarti, A.K., Dasgupta, S., Banik, N.L., Hogan, E.L. J. Neurochem. (1990) [Pubmed]
  14. Calcium-activated neutral proteinase (CANP; calpain) activity in Schwann cells: immunofluorescence localization and compartmentation of mu- and mCANP. Banik, N.L., DeVries, G.H., Neuberger, T., Russell, T., Chakrabarti, A.K., Hogan, E.L. J. Neurosci. Res. (1991) [Pubmed]
  15. Generation of spectrin breakdown products in peripheral nerves by addition of M-calpain. Castejon, M.S., Culver, D.G., Glass, J.D. Muscle Nerve (1999) [Pubmed]
  16. Specificity of calcium-activated neutral proteinase (CANP) inhibitors for human mu CANP and mCANP. Saito, K., Nixon, R.A. Neurochem. Res. (1993) [Pubmed]
  17. Different expression patterns of calpain isozymes 1 and 2 (CAPN1 and 2) in squamous cell carcinomas (SCC) and basal cell carcinomas (BCC) of human skin. Reichrath, J., Welter, C., Mitschele, T., Classen, U., Meineke, V., Tilgen, W., Seifert, M. J. Pathol. (2003) [Pubmed]
  18. Externalization of calpain (calcium-dependent neutral cysteine proteinase) in human arthritic cartilage. Szomor, Z., Shimizu, K., Yamamoto, S., Yasuda, T., Ishikawa, H., Nakamura, T. Clinical and experimental rheumatology. (1999) [Pubmed]
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