| pubmed-article:14594950 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14594950 | lifeskim:mentions | umls-concept:C0521324 | lld:lifeskim |
| pubmed-article:14594950 | lifeskim:mentions | umls-concept:C0006784 | lld:lifeskim |
| pubmed-article:14594950 | lifeskim:mentions | umls-concept:C1413113 | lld:lifeskim |
| pubmed-article:14594950 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:14594950 | lifeskim:mentions | umls-concept:C0439858 | lld:lifeskim |
| pubmed-article:14594950 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:14594950 | pubmed:dateCreated | 2004-1-19 | lld:pubmed |
| pubmed-article:14594950 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14594950 | pubmed:abstractText | p94 (also called calpain 3) is the skeletal muscle-specific calpain and is considered to be a "modulator protease" in various cellular processes. Analysis of p94 at the protein level is an urgent issue because the loss of p94 protease activity causes limb-girdle muscular dystrophy type 2A. In this study, we enzymatically characterized one alternatively spliced variant of p94, p94:exons 6(-)15(-)16(-) (p94delta), which lacks two of the p94-specific insertion sequences. In contrast to p94, which has hardly been studied enzymatically due to its rapid, thorough, and apparently Ca(2+)-independent autolytic activity, p94delta was stably expressed in COS and insect cells. p94delta showed Ca(2+)-dependent caseinolytic and autolytic activities and an inhibitor spectrum similar to those of the conventional calpains. However, calpastatin did not inhibit p94delta and is a substrate for p94delta, which is consistent with the properties of p94, presenting p94 as a possible regulator of the conventional calpain system. We also established a semi-quantitative fluorescence resonance energy transfer assay using the calpastatin sequence specifically to measure p94 activity. This method detects the activity of COS-expressed p94 and p94delta, suggesting that it has potential to evaluate p94 activity in vivo and in the diagnosis of limb-girdle muscular dystrophy type 2A. | lld:pubmed |
| pubmed-article:14594950 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14594950 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14594950 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14594950 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14594950 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14594950 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14594950 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14594950 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14594950 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:14594950 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:14594950 | pubmed:author | pubmed-author:SuzukiKoichiK | lld:pubmed |
| pubmed-article:14594950 | pubmed:author | pubmed-author:LabeitSiegfri... | lld:pubmed |
| pubmed-article:14594950 | pubmed:author | pubmed-author:KakinumaKazum... | lld:pubmed |
| pubmed-article:14594950 | pubmed:author | pubmed-author:SorimachiHiro... | lld:pubmed |
| pubmed-article:14594950 | pubmed:author | pubmed-author:AbeKeikoK | lld:pubmed |
| pubmed-article:14594950 | pubmed:author | pubmed-author:OnoYasukoY | lld:pubmed |
| pubmed-article:14594950 | pubmed:author | pubmed-author:NakagawaKazuh... | lld:pubmed |
| pubmed-article:14594950 | pubmed:author | pubmed-author:ToriiFukuyoF | lld:pubmed |
| pubmed-article:14594950 | pubmed:author | pubmed-author:IrieAkihiroA | lld:pubmed |
| pubmed-article:14594950 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14594950 | pubmed:day | 23 | lld:pubmed |
| pubmed-article:14594950 | pubmed:volume | 279 | lld:pubmed |
| pubmed-article:14594950 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14594950 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14594950 | pubmed:pagination | 2761-71 | lld:pubmed |
| pubmed-article:14594950 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:14594950 | pubmed:meshHeading | pubmed-meshheading:14594950... | lld:pubmed |
| pubmed-article:14594950 | pubmed:meshHeading | pubmed-meshheading:14594950... | lld:pubmed |
| pubmed-article:14594950 | pubmed:meshHeading | pubmed-meshheading:14594950... | lld:pubmed |
| pubmed-article:14594950 | pubmed:meshHeading | pubmed-meshheading:14594950... | lld:pubmed |
| pubmed-article:14594950 | pubmed:meshHeading | pubmed-meshheading:14594950... | lld:pubmed |
| pubmed-article:14594950 | pubmed:meshHeading | pubmed-meshheading:14594950... | lld:pubmed |
| pubmed-article:14594950 | pubmed:meshHeading | pubmed-meshheading:14594950... | lld:pubmed |
| pubmed-article:14594950 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:14594950 | pubmed:articleTitle | Possible regulation of the conventional calpain system by skeletal muscle-specific calpain, p94/calpain 3. | lld:pubmed |
| pubmed-article:14594950 | pubmed:affiliation | Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, University of Tokyo, Tokyo 113-8657, Japan. | lld:pubmed |
| pubmed-article:14594950 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14594950 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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