pubmed-article:10731697 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10731697 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:10731697 | lifeskim:mentions | umls-concept:C0039194 | lld:lifeskim |
pubmed-article:10731697 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
pubmed-article:10731697 | lifeskim:mentions | umls-concept:C0205242 | lld:lifeskim |
pubmed-article:10731697 | lifeskim:mentions | umls-concept:C0006784 | lld:lifeskim |
pubmed-article:10731697 | lifeskim:mentions | umls-concept:C0010656 | lld:lifeskim |
pubmed-article:10731697 | lifeskim:mentions | umls-concept:C0054534 | lld:lifeskim |
pubmed-article:10731697 | lifeskim:mentions | umls-concept:C0439148 | lld:lifeskim |
pubmed-article:10731697 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
pubmed-article:10731697 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:10731697 | pubmed:dateCreated | 2000-5-31 | lld:pubmed |
pubmed-article:10731697 | pubmed:abstractText | We have previously reported the activation of procalpain mu (precursor for low-calcium-requiring calpain) in apoptotic cells using a cleavage-site-directed antibody specific to active calpain [Kikuchi, H. and Imajoh-Ohmi, S. (1995) Cell Death Differ. 2, 195-199]. In this study, calpastatin, the endogenous inhibitor protein for calpain, was cleaved to a 90-kDa polypeptide during apoptosis in human Jurkat T cells. The limited proteolysis of calpastatin preceded the autolytic activation of procalpain. Inhibitors for caspases rescued the cells from apoptosis and simultaneously inhibited the cleavage of calpastatin. The full-length recombinant calpastatin was also cleaved by caspase-3 or caspase-7 at Asp-233 into the same size fragment. Cys-241 was also targeted by these caspases in vitro but not in apoptotic cells. Caspase-digested calpastatin lost its amino-terminal inhibitory unit, and inhibited three moles of calpain per mole. Our findings suggest that caspases trigger the decontrol of calpain activity suppression by degrading calpastatin. | lld:pubmed |
pubmed-article:10731697 | pubmed:language | eng | lld:pubmed |
pubmed-article:10731697 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10731697 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10731697 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10731697 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10731697 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10731697 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10731697 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10731697 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:10731697 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:10731697 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10731697 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10731697 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10731697 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:10731697 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:10731697 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10731697 | pubmed:month | Feb | lld:pubmed |
pubmed-article:10731697 | pubmed:issn | 0021-924X | lld:pubmed |
pubmed-article:10731697 | pubmed:author | pubmed-author:KatoMM | lld:pubmed |
pubmed-article:10731697 | pubmed:author | pubmed-author:KikuchiHH | lld:pubmed |
pubmed-article:10731697 | pubmed:author | pubmed-author:NonakaTT | lld:pubmed |
pubmed-article:10731697 | pubmed:author | pubmed-author:MakiMM | lld:pubmed |
pubmed-article:10731697 | pubmed:author | pubmed-author:Imajoh-OhmiSS | lld:pubmed |
pubmed-article:10731697 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10731697 | pubmed:volume | 127 | lld:pubmed |
pubmed-article:10731697 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10731697 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10731697 | pubmed:pagination | 297-305 | lld:pubmed |
pubmed-article:10731697 | pubmed:dateRevised | 2007-12-19 | lld:pubmed |
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pubmed-article:10731697 | pubmed:year | 2000 | lld:pubmed |
pubmed-article:10731697 | pubmed:articleTitle | Caspases cleave the amino-terminal calpain inhibitory unit of calpastatin during apoptosis in human Jurkat T cells. | lld:pubmed |
pubmed-article:10731697 | pubmed:affiliation | Institute of Medical Science, University of Tokyo, Minato-ku, Tokyo 108-8639, Japan. | lld:pubmed |
pubmed-article:10731697 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10731697 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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