The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

CAST  -  calpastatin

Bos taurus

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of CAST

  • In ovine muscle, changes in the activity of the calcium dependent neutral proteinases (calpains I and II) and their specific inhibitor (calpastatin) accompany beta-agonist-induced hypertrophy [1].
  • Increasing the amount of calpastatin in the incubations limited both the rate and extent of proteolysis of myofibrillar proteins and autolysis of mu-calpain [2].

High impact information on CAST


Chemical compound and disease context of CAST


Biological context of CAST


Anatomical context of CAST

  • Large forms of calpastatin from canine myocardium and rabbit liver also were bound to phosphatidylinositol [8].
  • The binding of large calpastatin to biologic membranes is mediated in part by interaction of an amino terminal region with acidic phospholipids [8].
  • Previously, myocardial calpastatin was shown to be present in preparations of sarcoplasmic reticulum and sarcolemma [8].
  • Longissimus muscle samples were obtained for determining myofibril fragmentation index, Warner-Bratzler shear force, and sensory panel evaluation at 1, 7, and 14 d postmortem, and mu- and m-calpain and calpastatin activities at 24 h postmortem [10].
  • Other traits were analyzed to determine their associations with mu- and m-calpain activity and MFI, including calpastatin activity, percentage of raw and cooked lipids, Warner-Bratzler shear force (WBSF) values after 7, 14, and 21 d of aging, and sensory panel rating of tenderness, juiciness, and connective tissue amount after 14 d of aging [11].

Associations of CAST with chemical compounds


Other interactions of CAST


Analytical, diagnostic and therapeutic context of CAST


  1. Changes in calpain and calpastatin mRNA induced by beta-adrenergic stimulation of bovine skeletal muscle. Parr, T., Bardsley, R.G., Gilmour, R.S., Buttery, P.J. Eur. J. Biochem. (1992) [Pubmed]
  2. Effect of calpastatin on degradation of myofibrillar proteins by mu-calpain under postmortem conditions. Geesink, G.H., Koohmaraie, M. J. Anim. Sci. (1999) [Pubmed]
  3. The bovine calpastatin gene promoter and a new N-terminal region of the protein are targets for cAMP-dependent protein kinase activity. Cong, M., Thompson, V.F., Goll, D.E., Antin, P.B. J. Biol. Chem. (1998) [Pubmed]
  4. Constitutive activity of glycogen synthase kinase-3beta: Positive regulation of steady-state levels of insulin receptor substrates-1 and -2 in adrenal chromaffin cells. Nemoto, T., Yokoo, H., Satoh, S., Yanagita, T., Sugano, T., Yoshikawa, N., Maruta, T., Kobayashi, H., Wada, A. Brain Res. (2006) [Pubmed]
  5. Effect of pH, temperature, and inhibitors on autolysis and catalytic activity of bovine skeletal muscle mu-calpain. Koohmaraie, M. J. Anim. Sci. (1992) [Pubmed]
  6. Bovine skeletal muscle calpastatin: cloning, sequence analysis, and steady-state mRNA expression. Killefer, J., Koohmaraie, M. J. Anim. Sci. (1994) [Pubmed]
  7. Short commuunication: Effect of dietary protein depletion and repletion on skeletal muscle calpastatin during early lactation. Cummins, K.A., Lonergan, S.M., Huff-Lonergan, E. J. Dairy Sci. (2004) [Pubmed]
  8. The binding of large calpastatin to biologic membranes is mediated in part by interaction of an amino terminal region with acidic phospholipids. Mellgren, R.L., Lane, R.D., Mericle, M.T. Biochim. Biophys. Acta (1989) [Pubmed]
  9. Rapid communication: a TaqI restriction fragment length polymorphism in the bovine calpastatin gene. Cockett, N.E., Shay, T.L., Green, R.D., Hancock, D.L. J. Anim. Sci. (1995) [Pubmed]
  10. Meat tenderness and the calpain proteolytic system in longissimus muscle of young bulls and steers. Morgan, J.B., Wheeler, T.L., Koohmaraie, M., Savell, J.W., Crouse, J.D. J. Anim. Sci. (1993) [Pubmed]
  11. Effect of sire on mu- and m-calpain activity and rate of tenderization as indicated by myofibril fragmentation indices of steaks from Brahman cattle. Riley, D.G., Chase, C.C., Pringle, T.D., West, R.L., Johnson, D.D., Olson, T.A., Hammond, A.C., Coleman, S.W. J. Anim. Sci. (2003) [Pubmed]
  12. Freezing and calcium chloride marination effects on beef tenderness and calpastatin activity. Whipple, G., Koohmaraie, M. J. Anim. Sci. (1992) [Pubmed]
  13. 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]
WikiGenes - Universities