Source:http://linkedlifedata.com/resource/pubmed/id/21297336
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2011-2-7
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pubmed:abstractText |
Protein disulfide isomerase (PDI) is a multifunctional protein that catalyzes disulfide bond formation and assists protein folding, as well as being a structural subunit of microsomal triglyceride transfer protein (MTP) and prolyl 4-hydroxylase (P4HD), and an estrogen and thyroid hormone-binding protein. Previous reports indicate that some endocrine-disrupting chemicals (EDCs) bind to PDI and disturb its functions, and we executed PDI-knockdown to examine the effects of dysfunction of PDI. In this study, the effects of PDI-knockdown were compared among three cell lines: MCF-7, SH-SY5Y and HeLa. PDI-knockdown induced different levels of cytotoxicity among these cell lines. In MCF-7 cells, PDI-knockdown activated apoptotic signaling, causing cytochrome c release from mitochondria and activation of caspase-9, caspase-6, caspase-7 and poly[ADP-ribose]polymerase-1, and the cytotoxicity induced by PDI-knockdown was suppressed by a pan-caspase inhibitor, z-VAD-fmk. These data suggest that cell death induced by PDI-knockdown is caspase-dependent apoptosis in MCF-7 cells.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1880-3989
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
36
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1-7
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pubmed:dateRevised |
2011-7-21
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pubmed:meshHeading |
pubmed-meshheading:21297336-Apoptosis,
pubmed-meshheading:21297336-Caspases,
pubmed-meshheading:21297336-Cell Line, Tumor,
pubmed-meshheading:21297336-Gene Knockdown Techniques,
pubmed-meshheading:21297336-Humans,
pubmed-meshheading:21297336-Protein Disulfide-Isomerases,
pubmed-meshheading:21297336-Signal Transduction
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pubmed:year |
2011
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pubmed:articleTitle |
Protein disulfide isomerase knockdown-induced cell death is cell-line-dependent and involves apoptosis in MCF-7 cells.
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pubmed:affiliation |
Graduate School of Biomedical Sciences, Hiroshima University, Minami-ku, Hiroshima, Japan.
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pubmed:publicationType |
Journal Article
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