Source:http://linkedlifedata.com/resource/pubmed/id/14573790
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
12
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| pubmed:dateCreated |
2003-10-23
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| pubmed:abstractText |
Phospholipid scramblase 3 (PLS3) is a newly recognized member of a family of proteins responsible for phospholipid translocation between two lipid compartments. To study PLS3 function in mitochondria, we disrupted its conserved calcium-binding motif yielding an inactive mutant PLS3(F258V). Cells transfected with PLS3(F258V) exhibited reduced proliferative capacity. Mitochondrial analysis revealed that PLS3(F258V)-expressing cells have decreased mitochondrial mass shown by lower cytochrome c and cardiolipin (CL) content, poor mitochondrial respiration, and reduced oxygen consumption and intracellular ATP; whereas wild-type PLS3-transfected cells exhibit increased mitochondrial mass and enhanced respiration. Electron microscopic examination revealed that the mitochondria in PLS3(F258V)-expressing cells have densely packed cristae and are fewer in number and larger than those in control cells. The abnormal mitochondrial metabolism and structure in PLS3(F258V)-expressing cells were associated with decreased sensitivity to UV- and tBid-induced apoptosis and diminished translocation of CL to the mitochondrial outer membrane. In contrast, wild-type PLS3-transfected cells displayed increased sensitivity to apoptosis and enhanced CL translocation. These studies identify PLS3 as a critical regulator of mitochondrial structure and respiration, and CL transport in apoptosis.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cardiolipins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochromes c,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipid Transfer Proteins
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| pubmed:status |
MEDLINE
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| pubmed:month |
Oct
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| pubmed:issn |
1541-7786
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
1
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
892-902
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:14573790-Apoptosis,
pubmed-meshheading:14573790-Cardiolipins,
pubmed-meshheading:14573790-Carrier Proteins,
pubmed-meshheading:14573790-Cell Line, Tumor,
pubmed-meshheading:14573790-Cytochromes c,
pubmed-meshheading:14573790-Flow Cytometry,
pubmed-meshheading:14573790-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:14573790-Gene Expression Regulation, Neoplastic,
pubmed-meshheading:14573790-HeLa Cells,
pubmed-meshheading:14573790-Humans,
pubmed-meshheading:14573790-Membrane Proteins,
pubmed-meshheading:14573790-Microscopy, Electron,
pubmed-meshheading:14573790-Mitochondria,
pubmed-meshheading:14573790-Mutation,
pubmed-meshheading:14573790-Phospholipid Transfer Proteins,
pubmed-meshheading:14573790-Polymerase Chain Reaction,
pubmed-meshheading:14573790-Time Factors,
pubmed-meshheading:14573790-Up-Regulation
|
| pubmed:year |
2003
|
| pubmed:articleTitle |
Phospholipid scramblase 3 controls mitochondrial structure, function, and apoptotic response.
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| pubmed:affiliation |
Huntsman Cancer Institute,, University of Utah, Salt Lake City, UT 84112, USA.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|