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Gene Review

CAPN1  -  calpain 1, (mu/I) large subunit

Bos taurus

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Disease relevance of CAPN1


High impact information on CAPN1

  • CANP1 was maximally active at 700 microM while CANP2 exhibited highest activity at 2 microM CaCl2 [2].
  • A calcium-activated neutral proteinase (CANP)-specific endogenous inhibitor (calpastatin) was purified from bovine brain by successive column chromatography [3].
  • The inhibitor formed a complex with CANP and the inactive complex was dissociated into active fractions of enzyme and calpastatin in the presence of EGTA [3].
  • We found mu-CANP activity in a crude CANP fraction extracted from the peripheral nerve, which degraded the neurofilament (Nf) triplet (200 K, 160 K, 68 K), especially the 160 K component, at Ca2+ concentrations of 50 microM and 0.1 mM [4].
  • Calcium-activated neutral protease with low affinity for calcium (CANP II, Mr 76,000) can be purified to apparent homogeneity by casein affinity chromatography but contains cyclic-AMP dependent protein kinase activity [5].

Biological context of CAPN1

  • Two previously identified single-nucleotide polymorphism markers located within the micromolar calcium-activated neutral protease gene (CAPN1) were evaluated for their association with variation in meat tenderness using one commercial sample of Simmental x Angus crossbred calves and one multibreed, crossbred research herd [6].
  • Animals inheriting the CC genotype at CAPN1 had meat that was more tender than those inheriting the TT genotype [7].
  • Two previously reported and two new SNP in the CAPN1 gene were used as markers on chromosome 29 [8].
  • One marker (termed 4751) was associated with shear force on postmortem d 7 (P < 0.01), 14 (P = 0.015), and 21 (P < 0.001) in this population, demonstrating that genetic variation important for tenderness segregates in Bos indicus cattle at or near CAPN1 [9].
  • Allele frequencies of the SNP in TG and CAPN1 were different in this Brahman population than in reported allele frequencies in Bos taurus populations [8].

Anatomical context of CAPN1


Associations of CAPN1 with chemical compounds

  • This affinity purified CANP had properties previously described for other CANPs: heterodimer of 80 and 30 kDa; neutral pH optimum; activation by millimolar Ca2+; and inhibition by an endogenous, heat-stable proteinaceous inhibitor, by leupeptin, and by sulfhydryl alkylating agents [12].
  • Treatment of whole homogenate and myelin with 0.1% Triton X-100 increased the CANP activity by tenfold [10].
  • Myelin prepared by the method of Norton and Poduslo as well as by a modified method, was shown to contain most (more than 50%) of homogenate mM CANP activity [11].
  • PI stimulated both m- and muCANP in a concentration-dependent manner, while phosphatidylcholine was least effective [13].

Other interactions of CAPN1

  • The objective of this study was to assess the association of single nucleotide polymorphisms (SNP) developed at the calpastatin (CAST) and mu-calpain (CAPN1) genes with meat tenderness and palatability traits in populations with diverse genetic backgrounds [7].

Analytical, diagnostic and therapeutic context of CAPN1

  • The SDS-PAGE analysis of the enzyme fractions has shown a major band at 66-68,000 daltons and two minor bands at 60,000 and 48-50,000 daltons for CANP I; a major band at 48-50,000 daltons and a minor band at 30-32,000 daltons for CANP II and a predominant doublet at 30-32,000 daltons with a minor band at 48-50,000 daltons for CANP III [14].


  1. Purification of calcium-activated neutral proteinase (CANP) from purified myelin of bovine brain white matter. Chakrabarti, A.K., Banik, N.L. Neurochem. Res. (1988) [Pubmed]
  2. Purification and characterization of two forms of Ca2+-activated neutral protease from calf brain. Malik, M.N., Fenko, M.D., Iqbal, K., Wisniewski, H.M. J. Biol. Chem. (1983) [Pubmed]
  3. Purification of an endogenous 68 kD inhibitor of calcium-activated neutral proteinase (CANP) from bovine brain: immunoblot identification and characterization. Banik, N.L., Chakrabarti, A.K., Hogan, E.L. J. Neurosci. Res. (1990) [Pubmed]
  4. Calcium-activated neutral protease in the peripheral nerve, which requires microM order Ca2+, and its effect on the neurofilament triplet. Kamakura, K., Ishiura, S., Suzuki, K., Sugita, H., Toyokura, Y. J. Neurosci. Res. (1985) [Pubmed]
  5. Characterization of calcium-activated neutral protease (CANP)-associated protein kinase from bovine brain and its phosphorylation of neurofilaments. Zimmerman, U.J., Schlaepfer, W.W. Biochem. Biophys. Res. Commun. (1985) [Pubmed]
  6. Association of markers in the bovine CAPN1 gene with meat tenderness in large crossbred populations that sample influential industry sires. Page, B.T., Casas, E., Quaas, R.L., Thallman, R.M., Wheeler, T.L., Shackelford, S.D., Koohmaraie, M., White, S.N., Bennett, G.L., Keele, J.W., Dikeman, M.E., Smith, T.P. J. Anim. Sci. (2004) [Pubmed]
  7. Effects of calpastatin and micro-calpain markers in beef cattle on tenderness traits. Casas, E., White, S.N., Wheeler, T.L., Shackelford, S.D., Koohmaraie, M., Riley, D.G., Chase, C.C., Johnson, D.D., Smith, T.P. J. Anim. Sci. (2006) [Pubmed]
  8. Assessment of single nucleotide polymorphisms in genes residing on chromosomes 14 and 29 for association with carcass composition traits in Bos indicus cattle. Casas, E., White, S.N., Riley, D.G., Smith, T.P., Brenneman, R.A., Olson, T.A., Johnson, D.D., Coleman, S.W., Bennett, G.L., Chase, C.C. J. Anim. Sci. (2005) [Pubmed]
  9. A new single nucleotide polymorphism in CAPN1 extends the current tenderness marker test to include cattle of Bos indicus, Bos taurus, and crossbred descent. White, S.N., Casas, E., Wheeler, T.L., Shackelford, S.D., Koohmaraie, M., Riley, D.G., Chase, C.C., Johnson, D.D., Keele, J.W., Smith, T.P. J. Anim. Sci. (2005) [Pubmed]
  10. The regional and subcellular distribution of calcium activated neutral proteinase (CANP) in the bovine central nervous system. Chakrabarti, A.K., Banik, N.L., Powers, J.M., Hogan, E.L. Neurochem. Res. (1989) [Pubmed]
  11. Distribution of calcium activated neutral proteinase (mM CANP) in myelin and cytosolic fractions in bovine brain white matter. Banik, N.L., Chakrabarti, A.K., Hogan, E.L. Life Sci. (1987) [Pubmed]
  12. Calcium-activated neutral protease purified from beef lung: properties and use in defining structure of epidermal growth factor receptors. King, L.E., Gates, R.E. Arch. Biochem. Biophys. (1985) [Pubmed]
  13. Regulation of the calcium-activated neutral proteinase (CANP) of bovine brain by myelin lipids. Chakrabarti, A.K., Dasgupta, S., Banik, N.L., Hogan, E.L. Biochim. Biophys. Acta (1990) [Pubmed]
  14. Purification of a calcium-activated neutral proteinase from bovine brain. Banik, N.L., Hogan, E.L., Jenkins, M.G., McDonald, J.K., McAlhaney, W.W., Sostek, M.B. Neurochem. Res. (1983) [Pubmed]
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