| pubmed-article:19126538 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19126538 | lifeskim:mentions | umls-concept:C0006675 | lld:lifeskim |
| pubmed-article:19126538 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
| pubmed-article:19126538 | lifeskim:mentions | umls-concept:C0300926 | lld:lifeskim |
| pubmed-article:19126538 | lifeskim:mentions | umls-concept:C2753858 | lld:lifeskim |
| pubmed-article:19126538 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:19126538 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:19126538 | pubmed:dateCreated | 2009-3-9 | lld:pubmed |
| pubmed-article:19126538 | pubmed:abstractText | A hallmark of apoptotic cells is the Ca2+-dependent appearance of phosphatidylserine (PS) at the cell surface as a result of its redistribution from the inner-to-outer plasma membrane leaflet. Although endoplasmic reticulum and mitochondrial Ca2+ are known to participate in apoptosis, their role in PS externalization has not been established. In this study, several organelle-specific fluorescent markers and Ca2+-sensitive probes were used to identify the source of Ca2+ critical to PS externalization. By employing Rhod-2AM, fluorescein-labeled high molecular weight dextran, and Calcium Green 1, we provide evidence that lysosomes respond to apoptotic stimuli by releasing their luminal Ca2+ to the cytosol. Cells treated with the cytosolic phospholipase A2 inhibitor, cPLA2alpha, had no effect on caspase activation but exhibited a significant decrease in lysosomal Ca2+ release and externalization of PS in response to apoptotic stimuli. Similarly, cells depleted of lysosomal Ca2+ underwent programmed cell death yet failed to externalize PS. These data indicate that although Ca2+ release from other intracellular organelles to the cytosol is adequate for apoptosis, the release of Ca2+ from lysosomes is critical for PS externalization. | lld:pubmed |
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| pubmed-article:19126538 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19126538 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19126538 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:19126538 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19126538 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:19126538 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:19126538 | pubmed:author | pubmed-author:MirnikjooBana... | lld:pubmed |
| pubmed-article:19126538 | pubmed:author | pubmed-author:Balasubramani... | lld:pubmed |
| pubmed-article:19126538 | pubmed:author | pubmed-author:SchroitAlan... | lld:pubmed |
| pubmed-article:19126538 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:19126538 | pubmed:day | 13 | lld:pubmed |
| pubmed-article:19126538 | pubmed:volume | 284 | lld:pubmed |
| pubmed-article:19126538 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19126538 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19126538 | pubmed:pagination | 6918-23 | lld:pubmed |
| pubmed-article:19126538 | pubmed:dateRevised | 2010-9-23 | lld:pubmed |
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| pubmed-article:19126538 | pubmed:meshHeading | pubmed-meshheading:19126538... | lld:pubmed |
| pubmed-article:19126538 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19126538 | pubmed:articleTitle | Mobilization of lysosomal calcium regulates the externalization of phosphatidylserine during apoptosis. | lld:pubmed |
| pubmed-article:19126538 | pubmed:affiliation | Department of Cancer Biology, University of Texas, M. D. Anderson Cancer Center, Houston, Texas 77030, USA. | lld:pubmed |
| pubmed-article:19126538 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19126538 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:19126538 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:19126538 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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