منابع مشابه
Calpastatin subdomains A and C are activators of calpain.
The inhibitory domains of calpastatin contain three highly conserved regions, A, B, and C, of which A and C bind calpain in a strictly Ca(2+)-dependent manner but have no inhibitory activity whereas region B inhibits calpain on its own. We synthesized the 19-mer oligopeptides corresponding to regions A and C of human calpastatin domain I and tested their effect on human erythrocyte mu-calpain a...
متن کاملAssociation between Yearling Weight and Calpastatin and Calpain Loci Polymorphism in Iranian Zel Sheep
Genotypes of Iranian Zel sheep for Calpastatin(CAST) locus were determined by polymerase chain reaction-restriction fragment length polymorphism (PCR-RFLP) and polymerase chain reaction-single strand conformation polymorphism (PCR-SSCP) methods and for Calpain(CAPN) locus by PCR-SSCP. Blood samples were collected from 200 purebred Zel sheep of Zel Breeding Station located in Golestan province i...
متن کاملA simple one-step procedure for the separation of calpain I, calpain II and calpastatin.
The soluble fraction from rabbit brain was adsorbed on a column of phenyl-Sepharose. By applying a linear gradient with decreasing salt concentration and increasing pH, it was possible to separate calpain I and calpain II from each other and from the endogenous inhibitor calpastatin. Both enzymes were capable of degrading endogenously labelled neuronal proteins, including slowly axonally transp...
متن کاملCaspase-mediated fragmentation of calpain inhibitor protein calpastatin during apoptosis.
Two cysteine protease families (caspase and calpain) participate in apoptosis. Here we report that the endogenous calpain inhibitor calpastatin is fragmented by caspase(s) to various extents during early apoptosis in two cell types. In anti-fas or staurosporine-treated Jurkat T-cells, the high-molecular-weight form (HMW) of calpastatin (apparent Mr 110 K) was extensively degraded to immunoreact...
متن کاملChanges in intracellular localization of calpastatin during calpain activation.
Localization of the two main components of the Ca(2+)-dependent proteolytic system has been investigated in human neuroblastoma LAN-5 cells. Using a monoclonal antibody which recognizes the N-terminal calpastatin domain, it has been shown that this inhibitory protein is almost completely confined in two granule-like structures not surrounded by membranes. Similar calpastatin distribution has be...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1986
ISSN: 0014-5793
DOI: 10.1016/0014-5793(86)81351-5