| pubmed-article:11781251 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11781251 | lifeskim:mentions | umls-concept:C1517806 | lld:lifeskim |
| pubmed-article:11781251 | lifeskim:mentions | umls-concept:C0010749 | lld:lifeskim |
| pubmed-article:11781251 | lifeskim:mentions | umls-concept:C0092801 | lld:lifeskim |
| pubmed-article:11781251 | lifeskim:mentions | umls-concept:C0678226 | lld:lifeskim |
| pubmed-article:11781251 | lifeskim:mentions | umls-concept:C0030685 | lld:lifeskim |
| pubmed-article:11781251 | lifeskim:mentions | umls-concept:C0683598 | lld:lifeskim |
| pubmed-article:11781251 | lifeskim:mentions | umls-concept:C0680255 | lld:lifeskim |
| pubmed-article:11781251 | lifeskim:mentions | umls-concept:C0391871 | lld:lifeskim |
| pubmed-article:11781251 | lifeskim:mentions | umls-concept:C1283071 | lld:lifeskim |
| pubmed-article:11781251 | lifeskim:mentions | umls-concept:C1963578 | lld:lifeskim |
| pubmed-article:11781251 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:11781251 | pubmed:dateCreated | 2002-1-8 | lld:pubmed |
| pubmed-article:11781251 | pubmed:abstractText | The purine nucleoside 2-chlorodeoxyadenosine (CdA) is often used in leukemia therapy. Its efficacy, however, is compromised by the emergence of resistant cells. In the present study, 3 CdA-resistant cell lines were generated and characterized. Their ability to accumulate 2-chloroadenosine triphosphate (CdATP) varied, reflecting differences in activities of deoxycytidine kinase (dCK) and deoxyguanosine kinase (dGK). Nonetheless, the selected lines were uniformly resistant to CdA-induced apoptosis, as assessed by caspase activation and DNA fragmentation. In contrast, cytosols from resistant cells were capable of robust caspase activation when incubated in the presence of cytochrome c and dATP. Moreover, replacement of dATP with CdATP also resulted in caspase activation in the parental and some of the resistant cell lines. Strikingly, CdA-induced decreases in mitochondrial transmembrane potential and release of cytochrome c from mitochondria were observed in the parental cells but not in any resistant lines. The lack of cytochrome c release correlated with an increased ability of mitochondria from resistant cells to sequester free Ca2+. Consistent with this enhanced Ca2+ buffering capacity, an early increase in cytosolic Ca2+ after CdA treatment of parental cells but not resistant cells was detected. Furthermore, CdA-resistant cells were selectively cross-resistant to thapsigargin but not to staurosporine- or Fas-induced apoptosis. In addition, CdA-induced caspase-3 activation and DNA fragmentation were inhibited by the Ca2+ chelator BAPTA-AM in sensitive cells. Taken together, the data indicate that the mechanism of resistance to CdA may be dictated by changes in Ca2+-sensitive mitochondrial events. | lld:pubmed |
| pubmed-article:11781251 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11781251 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11781251 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:11781251 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11781251 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11781251 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11781251 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11781251 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11781251 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11781251 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11781251 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11781251 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11781251 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11781251 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11781251 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11781251 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11781251 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11781251 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11781251 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11781251 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11781251 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11781251 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11781251 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:11781251 | pubmed:issn | 0006-4971 | lld:pubmed |
| pubmed-article:11781251 | pubmed:author | pubmed-author:KaufmannScott... | lld:pubmed |
| pubmed-article:11781251 | pubmed:author | pubmed-author:ChandraJoyaJ | lld:pubmed |
| pubmed-article:11781251 | pubmed:author | pubmed-author:ManssonEmmaE | lld:pubmed |
| pubmed-article:11781251 | pubmed:author | pubmed-author:GogvadzeVladi... | lld:pubmed |
| pubmed-article:11781251 | pubmed:author | pubmed-author:AlbertioniFre... | lld:pubmed |
| pubmed-article:11781251 | pubmed:author | pubmed-author:OrreniusStenS | lld:pubmed |
| pubmed-article:11781251 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11781251 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:11781251 | pubmed:volume | 99 | lld:pubmed |
| pubmed-article:11781251 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11781251 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11781251 | pubmed:pagination | 655-63 | lld:pubmed |
| pubmed-article:11781251 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:11781251 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11781251 | pubmed:articleTitle | Resistance of leukemic cells to 2-chlorodeoxyadenosine is due to a lack of calcium-dependent cytochrome c release. | lld:pubmed |
| pubmed-article:11781251 | pubmed:affiliation | Institute for Environmental Medicine, Division of Toxicology, and Department of Medicine, Karolinska Institutet, Stockholm, Sweden. chandra.joya@mayo.edu | lld:pubmed |
| pubmed-article:11781251 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11781251 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
