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Gene Review

CAST  -  calpastatin

Bos taurus

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Disease relevance of CAST


High impact information on CAST


Biological context of CAST


Anatomical context of CAST


Associations of CAST with chemical compounds

  • 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 [13].
  • The CANPs are cysteine proteinases that have an absolute requirement for Ca(2+) for activity. mu-Calpain and calpastatin were purified by successive chromatographic steps on Toyopearl-Super Q 650S and Pharmacia Mono Q HR 5/5 columns [14].
  • 3. Reduction in [(3)H]-STX binding capacity induced by A23187 or TG was attenuated by Gö6976 (an inhibitor of conventional protein kinase C) or calpastatin peptide (an inhibitor of calpain) [15].
  • This activation of TH by calpain was inhibited by leupeptin and the endogenous inhibitor, calpastatin [12].
  • Clenbuterol administration resulted in an increase in calpastatin levels (P < .05) and a trend (P < 0.1) toward a decrease in mu-calpain activity at 1 d postmortem [16].

Other interactions of CAST

  • 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 [17].

Analytical, diagnostic and therapeutic context of CAST

  • The origin of the two species in porcine heart was examined by RT-PCR and direct sequencing of calpastatin cDNA [5].
  • The presence of multiple species of calpastatin in porcine heart does not appear to be an artifact of the purification procedure since Western blotting revealed the presence of two types of calpastatin in ovine and porcine heart, but only one type in bovine heart and bovine, ovine, and porcine muscle [5].
  • Variation in the ovine calpastatin gene (CAST) was investigated by amplification of a fragment containing the entire exon 6 using polymerase chain reaction (PCR), followed by single-strand conformational polymorphism (PCR-SSCP) analysis and DNA sequencing [18].


  1. Binding of calpain fragments to calpastatin. Nishimura, T., Goll, D.E. J. Biol. Chem. (1991) [Pubmed]
  2. The non-lysosomal, calcium-dependent proteolytic system of mammalian cells. Mellgren, R.L., Renno, W.M., Lane, R.D. Revis. Biol. Celular (1989) [Pubmed]
  3. Involvement of protein kinase-C, calpains, and calpastatin in prostaglandin F2 alpha-induced oxytocin secretion from the bovine corpus luteum. Orwig, K.E., Bertrand, J.E., Ou, B.R., Forsberg, N.E., Stormshak, F. Endocrinology (1994) [Pubmed]
  4. Domain structure of calpain: mapping the binding site for calpastatin. Croall, D.E., McGrody, K.S. Biochemistry (1994) [Pubmed]
  5. An improved purification protocol for heart and skeletal muscle calpastatin reveals two isoforms resulting from alternative splicing. Geesink, G.H., Nonneman, D., Koohmaraie, M. Arch. Biochem. Biophys. (1998) [Pubmed]
  6. Genotypic effects of calpain 1 and calpastatin on the tenderness of cooked M. longissimus dorsi steaks from Jersey x Limousin, Angus and Hereford-cross cattle. Morris, C.A., Cullen, N.G., Hickey, S.M., Dobbie, P.M., Veenvliet, B.A., Manley, T.R., Pitchford, W.S., Kruk, Z.A., Bottema, C.D., Wilson, T. Anim. Genet. (2006) [Pubmed]
  7. Effect of nutrient restriction on calpain and calpastatin content of skeletal muscle from cows and fetuses. Du, M., Zhu, M.J., Means, W.J., Hess, B.W., Ford, S.P. J. Anim. Sci. (2004) [Pubmed]
  8. A DNA polymorphism of the bovine calpastatin gene detected by SSCP analysis. Chung, H.Y., Davis, M.E., Hines, H.C. Anim. Genet. (1999) [Pubmed]
  9. Genetic effects on beef tenderness in Bos indicus composite and Bos taurus cattle. O'Connor, S.F., Tatum, J.D., Wulf, D.M., Green, R.D., Smith, G.C. J. Anim. Sci. (1997) [Pubmed]
  10. The calpain-calpastatin system in vascular smooth muscle. McClelland, P., Hathaway, D.R. FEBS Lett. (1991) [Pubmed]
  11. On the mechanism of binding of calpastatin, the protein inhibitor of calpains, to biologic membranes. Mellgren, R.L. Biochem. Biophys. Res. Commun. (1988) [Pubmed]
  12. Activation of tyrosine hydroxylase by Ca2+-dependent neutral protease, calpain. Togari, A., Ichikawa, S., Nagatsu, T. Biochem. Biophys. Res. Commun. (1986) [Pubmed]
  13. 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]
  14. The purification and characterization of mu-calpain and calpastatin from ostrich brain. Mkwetshana, N., Naudé, R.J., Muramoto, K. Int. J. Biochem. Cell Biol. (2002) [Pubmed]
  15. Heterogeneous increases of cytoplasmic calcium: distinct effects on down-regulation of cell surface sodium channels and sodium channel subunit mRNA levels. Shiraishi, S., Shibuya, I., Uezono, Y., Yokoo, H., Toyohira, Y., Yamamoto, R., Yanagita, T., Kobayashi, H., Wada, A. Br. J. Pharmacol. (2001) [Pubmed]
  16. Effects on meat quality of the use of clenbuterol in veal calves. Geesink, G.H., Smulders, F.J., van Laack, H.L., van der Kolk, J.H., Wensing, T., Breukink, H.J. J. Anim. Sci. (1993) [Pubmed]
  17. 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]
  18. Polymorphism of the ovine calpastatin gene. Zhou, H., Hickford, J.G., Gong, H. Mol. Cell. Probes (2007) [Pubmed]
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