Source:http://linkedlifedata.com/resource/pubmed/id/15190260
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
8
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| pubmed:dateCreated |
2004-7-22
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| pubmed:abstractText |
Cyclooxygenase (COX)-1 or -2 and specific prostaglandin (PG) synthases catalyze the formation of various PGs. We investigated the expression and activity of COX-1 and -2 during granulocyte-oriented maturation induced by all-trans-retinoic acid (ATRA) of NB4 cells, originated from a human acute promyelocytic leukemia (APL), and in blasts from APL patients. The expression of COX isoenzymes or prostaglandin synthases was also investigated in circulating granulocytes and human bone marrow. COX-1 was expressed and enzymatically active in NB4 cells and primary blasts. COX-1 mRNA and protein were induced by ATRA. COX-1 protein increased approximately 2-3.5-fold by culture day 3 in NB4 cells and primary blasts, while basal COX-2 expression was very low and unaffected by ATRA. COX-1-dependent PGE(2) biosynthesis increased during differentiation approx. 5-fold. Indomethacin and the selective COX-1 inhibitor SC-560, but not selective COX-2 inhibition, impaired NB4 differentiation, reducing NADPH-oxidase activity, CD11b and CD11c expression. The immunohistochemistry of granulocytes and myeloid precursors in the bone marrow showed a large prevalence of COX-1 as compared to COX-2. In conclusion, COX-1 is induced during ATRA-dependent maturation and appears to contribute to myeloid differentiation both in vitro and ex vivo, and COX-1 activity may potentiate the differentiation of human APL.Leukemia (2004) 18, 1373-1379. doi:10.1038/sj.leu.2403407 Published online 10 June 2004
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cyclooxygenase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclooxygenase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Dinoprostone,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PTGS1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/PTGS2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Prostaglandin-Endoperoxide Synthases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Tretinoin
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| pubmed:status |
MEDLINE
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| pubmed:month |
Aug
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| pubmed:issn |
0887-6924
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
18
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
1373-9
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:15190260-Blood Cells,
pubmed-meshheading:15190260-Bone Marrow Cells,
pubmed-meshheading:15190260-Cell Differentiation,
pubmed-meshheading:15190260-Cell Line, Tumor,
pubmed-meshheading:15190260-Cyclooxygenase 1,
pubmed-meshheading:15190260-Cyclooxygenase 2,
pubmed-meshheading:15190260-Dinoprostone,
pubmed-meshheading:15190260-Granulocytes,
pubmed-meshheading:15190260-Humans,
pubmed-meshheading:15190260-Isoenzymes,
pubmed-meshheading:15190260-Leukemia,
pubmed-meshheading:15190260-Leukemia, Promyelocytic, Acute,
pubmed-meshheading:15190260-Membrane Proteins,
pubmed-meshheading:15190260-Myelopoiesis,
pubmed-meshheading:15190260-Prostaglandin-Endoperoxide Synthases,
pubmed-meshheading:15190260-RNA, Messenger,
pubmed-meshheading:15190260-Tretinoin,
pubmed-meshheading:15190260-Tumor Cells, Cultured,
pubmed-meshheading:15190260-Up-Regulation
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| pubmed:year |
2004
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| pubmed:articleTitle |
Cyclooxygenase-1, but not -2, is upregulated in NB4 leukemic cells and human primary promyelocytic blasts during differentiation.
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| pubmed:affiliation |
Department of Internal Medicine, Catholic University School of Medicine, Rome, Italy. b.rocca@tiscali.it
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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