| pubmed-article:16331270 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16331270 | lifeskim:mentions | umls-concept:C0007427 | lld:lifeskim |
| pubmed-article:16331270 | lifeskim:mentions | umls-concept:C0334227 | lld:lifeskim |
| pubmed-article:16331270 | lifeskim:mentions | umls-concept:C1514559 | lld:lifeskim |
| pubmed-article:16331270 | lifeskim:mentions | umls-concept:C0205177 | lld:lifeskim |
| pubmed-article:16331270 | lifeskim:mentions | umls-concept:C2349975 | lld:lifeskim |
| pubmed-article:16331270 | lifeskim:mentions | umls-concept:C0205254 | lld:lifeskim |
| pubmed-article:16331270 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:16331270 | pubmed:dateCreated | 2006-3-24 | lld:pubmed |
| pubmed-article:16331270 | pubmed:abstractText | The aspartic protease cathepsin D (cath-D) is a key mediator of induced-apoptosis and its proteolytic activity has been generally involved in this event. During apoptosis, cath-D is translocated to the cytosol. Because cath-D is one of the lysosomal enzymes that requires a more acidic pH to be proteolytically active relative to the cysteine lysosomal enzymes such as cath-B and -L, it is therefore open to question whether cytosolic cath-D might be able to cleave substrate(s) implicated in the apoptotic cascade. Here, we have investigated the role of wild-type cath-D and its proteolytically inactive counterpart overexpressed by 3Y1-Ad12 cancer cells during chemotherapeutic-induced cytotoxicity and apoptosis, as well as the relevance of cath-D catalytic function. We demonstrate that wild-type or mutated catalytically inactive cath-D strongly enhances chemo-sensitivity and apoptotic response to etoposide. Both wild-type and mutated inactive cath-D are translocated to the cytosol, increasing the release of cytochrome c, the activation of caspases-9 and -3 and the induction of a caspase-dependent apoptosis. In addition, pretreatment of cells with the aspartic protease inhibitor, pepstatin A, does not prevent apoptosis. Interestingly therefore, the stimulatory effect of cath-D on cell death is independent of its catalytic activity. Overall, our results imply that cytosolic cath-D stimulates apoptotic pathways by interacting with a member of the apoptotic machinery rather than by cleaving specific substrate(s). | lld:pubmed |
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| pubmed-article:16331270 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16331270 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16331270 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16331270 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16331270 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:16331270 | pubmed:issn | 0950-9232 | lld:pubmed |
| pubmed-article:16331270 | pubmed:author | pubmed-author:BaghdiguianSS | lld:pubmed |
| pubmed-article:16331270 | pubmed:author | pubmed-author:BerchemGG | lld:pubmed |
| pubmed-article:16331270 | pubmed:author | pubmed-author:Liaudet-Coopm... | lld:pubmed |
| pubmed-article:16331270 | pubmed:author | pubmed-author:BeaujouinMM | lld:pubmed |
| pubmed-article:16331270 | pubmed:author | pubmed-author:Glondu-Lassis... | lld:pubmed |
| pubmed-article:16331270 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16331270 | pubmed:day | 23 | lld:pubmed |
| pubmed-article:16331270 | pubmed:volume | 25 | lld:pubmed |
| pubmed-article:16331270 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16331270 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16331270 | pubmed:pagination | 1967-73 | lld:pubmed |
| pubmed-article:16331270 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:16331270 | pubmed:meshHeading | pubmed-meshheading:16331270... | lld:pubmed |
| pubmed-article:16331270 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16331270 | pubmed:articleTitle | Overexpression of both catalytically active and -inactive cathepsin D by cancer cells enhances apoptosis-dependent chemo-sensitivity. | lld:pubmed |
| pubmed-article:16331270 | pubmed:affiliation | INSERM U540 Endocrinologie Moléculaire et Cellulaire des Cancers, Université Montpellier 1, Montpellier, France. | lld:pubmed |
| pubmed-article:16331270 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16331270 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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