| pubmed-article:12140766 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12140766 | lifeskim:mentions | umls-concept:C0023418 | lld:lifeskim |
| pubmed-article:12140766 | lifeskim:mentions | umls-concept:C0007600 | lld:lifeskim |
| pubmed-article:12140766 | lifeskim:mentions | umls-concept:C0162638 | lld:lifeskim |
| pubmed-article:12140766 | lifeskim:mentions | umls-concept:C1512310 | lld:lifeskim |
| pubmed-article:12140766 | lifeskim:mentions | umls-concept:C2717971 | lld:lifeskim |
| pubmed-article:12140766 | lifeskim:mentions | umls-concept:C0205419 | lld:lifeskim |
| pubmed-article:12140766 | lifeskim:mentions | umls-concept:C0086597 | lld:lifeskim |
| pubmed-article:12140766 | pubmed:issue | 33 | lld:pubmed |
| pubmed-article:12140766 | pubmed:dateCreated | 2002-7-25 | lld:pubmed |
| pubmed-article:12140766 | pubmed:abstractText | We report here that expression of proteinase 3 (PR3), a serine protease, is down-regulated in the HL60/ADR multidrug resistant variant of the human myelogenous leukemia cell line HL-60, and that down-regulation of PR3 is associated with doxorubicin (DOX) resistance in these cells. To determine whether PR3 is involved in DOX-induced apoptosis in HL-60 cells, and whether its loss causes resistance to DOX, we inhibited PR3 expression by an anti-sense PR3 oligodeoxynucleotide and showed that inhibition of PR3 expression results in a significant reduction in DOX-induced DNA fragmentation and increased resistance to DOX-induced apoptosis. Our results revealed that PR3-mediated DOX-induced apoptosis in HL-60 cells is independent of the loss of mitochondrial membrane potential (deltapsi(m)) and activation of the caspase-8 and -9 pathways. Moreover, while PR3 is involved in the cleavage of caspase-3, PR3-mediated DOX-induced DNA fragmentation and apoptosis were not prevented by a specific inhibitor of caspase-3. These data suggest that activation of caspase-3 alone is not sufficient to trigger PR3-mediated DOX-induced apoptosis. Treatment with an anti-PR3 oligomer significantly decreased reactive oxygen species (ROS) generation in cells treated with low concentrations of DOX, revealing a role for PR3 in enhancing production of DOX-induced ROS. Moreover, DOX-induced apoptosis at 0.001-0.01 microM was only inhibited in HL-60 cells pre-treated with the antioxidant N-acetyl-cysteine in the absence of anti-PR3, revealing that DOX-induced apoptosis in these cells is PR3- and ROS-dependent. Our results show that PR3 is involved in DOX-induced ROS-dependent apoptosis and that its loss is associated with resistance to DOX in HL-60 cells. | lld:pubmed |
| pubmed-article:12140766 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12140766 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12140766 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12140766 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12140766 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12140766 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12140766 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12140766 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12140766 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12140766 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:12140766 | pubmed:issn | 0950-9232 | lld:pubmed |
| pubmed-article:12140766 | pubmed:author | pubmed-author:OgretmenBesim... | lld:pubmed |
| pubmed-article:12140766 | pubmed:author | pubmed-author:GordonJohnJ | lld:pubmed |
| pubmed-article:12140766 | pubmed:author | pubmed-author:SafaAhmad RAR | lld:pubmed |
| pubmed-article:12140766 | pubmed:author | pubmed-author:WuChing-Huang... | lld:pubmed |
| pubmed-article:12140766 | pubmed:author | pubmed-author:RastegarMojga... | lld:pubmed |
| pubmed-article:12140766 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12140766 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:12140766 | pubmed:volume | 21 | lld:pubmed |
| pubmed-article:12140766 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12140766 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12140766 | pubmed:pagination | 5160-74 | lld:pubmed |
| pubmed-article:12140766 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:12140766 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12140766 | pubmed:articleTitle | Proteinase-3, a serine protease which mediates doxorubicin-induced apoptosis in the HL-60 leukemia cell line, is downregulated in its doxorubicin-resistant variant. | lld:pubmed |
| pubmed-article:12140766 | pubmed:affiliation | Department of Pharmacology and Toxicology, Indiana University, 1044 West Walnut R4-119, Indianapolis, Indiana, IN 46202, USA. | lld:pubmed |
| pubmed-article:12140766 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12140766 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12140766 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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