Calpastatin inhibits motor neuron death and increases survival of hSOD1(G93A) mice.
New York City, United States. In J Neurochem, Feb 2016
Given that calpains mediate neurodegeneration in other pathological states and are abnormally activated in ALS, we investigated the possible ameliorative effects of inhibiting calpain overactivation in hSOD1(G93A) transgenic (Tg) mice in vivo by neuron specific overexpression of calpastatin (CAST), the highly selective endogenous inhibitor of calpains.
Targeting host calpain proteases decreases influenza A virus infection.
Hong Kong, Hong Kong. In Am J Physiol Lung Cell Mol Physiol, Feb 2016
Using siRNA gene silencing, specific synthetic inhibitors of calpains and mice overexpressing calpastatin, we found that calpain inhibition dampens IAV replication as well as IAV-triggered secretion of pro-inflammatory mediators and leukocyte infiltration.
Resuscitation of a dead cardiomyocyte.
Louisville, United States. In Heart Fail Rev, Nov 2015
The activation of calpains beyond the calpastatin-mediated inhibition due to extensive calcium harbor can lead to titin degradation, damage to the sarcomere and contractile dysfunction.
Structure-function relationships in calpains.
Kingston, Canada. In Biochem J, 2012
Structures of calpain-2, both Ca2+-free and bound to calpastatin in the activated Ca2+-bound state, have provided a wealth of information about the enzyme's structure-function relationships and activation.
Cleavage of the plasma membrane Na+/Ca2+ exchanger in excitotoxicity.
Leicester, United Kingdom. In Cell, 2005
Inhibition of Ca2+-activated proteases (calpains) by overexpressing their endogenous inhibitor protein, calpastatin or the expression of an NCX isoform not cleaved by calpains, prevented Ca2+ overload and rescued neurons from excitotoxic death.
The calpain system.
Tucson, United States. In Physiol Rev, 2003
The calpain system originally comprised three molecules: two Ca2+-dependent proteases, mu-calpain and m-calpain, and a third polypeptide, calpastatin, whose only known function is to inhibit the two calpains.
A Ca(2+) switch aligns the active site of calpain.
Kingston, Canada. In Cell, 2002
The protease region is not affected by the endogenous inhibitor, calpastatin, and may contribute to calpain-mediated pathologies when the core is released by autoproteolysis.