| pubmed-article:7755588 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7755588 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:7755588 | lifeskim:mentions | umls-concept:C0077404 | lld:lifeskim |
| pubmed-article:7755588 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
| pubmed-article:7755588 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
| pubmed-article:7755588 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
| pubmed-article:7755588 | lifeskim:mentions | umls-concept:C1709059 | lld:lifeskim |
| pubmed-article:7755588 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:7755588 | lifeskim:mentions | umls-concept:C1120861 | lld:lifeskim |
| pubmed-article:7755588 | pubmed:dateCreated | 1995-6-22 | lld:pubmed |
| pubmed-article:7755588 | pubmed:abstractText | The degradation of troponin (Tn) subunits by calpain was studied by incubating either isolated cardiac Tns or myocardial cryosections with two different calpain isoenzymes isolated from rat skeletal muscle. Western-blot analysis with monoclonal antibodies against TnI and TnT showed that mu-calpain was at least ten times more active than m-calpain in degrading TnI and TnT both in vitro and in situ. TnC was completely resistant to both proteinase forms. Phosphorylation by cyclic AMP-dependent protein kinase (PKA) isolated from rat skeletal muscle reduced the sensitivity of TnI to degradation. This effect in combination with an increased efficiency of the endogenous inhibitor [Salamino, De Tullio, Michetti, Mengotti, Melloni and Pontremoli (1994) Biochem. Biophys. Res. Commun. 199, 1326-1332] probably reduces the proteolytic activity of calpain in cells on PKA stimulation. Conversely, phosphorylation by protein kinase C (PKC) resulted in a twofold increase in the degradation of TnI. Degradation by m-calpain was not modified by Tn phosphorylation. The different sensitivity to mu-calpain might be related to changes in TnI oligomeric structure. Indeed, on PKC phosphorylation, the apparent molecular mass of TnI calculated from the distribution coefficient of Tn complex in Sephadex G-100 matrix was reduced from 90 to 30 kDa suggesting dissociation of the Tn complex. | lld:pubmed |
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| pubmed-article:7755588 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7755588 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7755588 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7755588 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7755588 | pubmed:month | May | lld:pubmed |
| pubmed-article:7755588 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:7755588 | pubmed:author | pubmed-author:PontremoliSS | lld:pubmed |
| pubmed-article:7755588 | pubmed:author | pubmed-author:SchiaffinoSS | lld:pubmed |
| pubmed-article:7755588 | pubmed:author | pubmed-author:MelloniEE | lld:pubmed |
| pubmed-article:7755588 | pubmed:author | pubmed-author:SalaminoFF | lld:pubmed |
| pubmed-article:7755588 | pubmed:author | pubmed-author:SiliprandiNN | lld:pubmed |
| pubmed-article:7755588 | pubmed:author | pubmed-author:De TullioRR | lld:pubmed |
| pubmed-article:7755588 | pubmed:author | pubmed-author:BarbatoRR | lld:pubmed |
| pubmed-article:7755588 | pubmed:author | pubmed-author:Di LisaFF | lld:pubmed |
| pubmed-article:7755588 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7755588 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:7755588 | pubmed:volume | 308 ( Pt 1) | lld:pubmed |
| pubmed-article:7755588 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7755588 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7755588 | pubmed:pagination | 57-61 | lld:pubmed |
| pubmed-article:7755588 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:7755588 | pubmed:meshHeading | pubmed-meshheading:7755588-... | lld:pubmed |
| pubmed-article:7755588 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7755588 | pubmed:articleTitle | Specific degradation of troponin T and I by mu-calpain and its modulation by substrate phosphorylation. | lld:pubmed |
| pubmed-article:7755588 | pubmed:affiliation | Dipartimento di Chimica Biologica, Università di Padova, Italy. | lld:pubmed |
| pubmed-article:7755588 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7755588 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:7755588 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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