pubmed-article:2502549 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2502549 | lifeskim:mentions | umls-concept:C0007589 | lld:lifeskim |
pubmed-article:2502549 | lifeskim:mentions | umls-concept:C0282549 | lld:lifeskim |
pubmed-article:2502549 | lifeskim:mentions | umls-concept:C0003693 | lld:lifeskim |
pubmed-article:2502549 | lifeskim:mentions | umls-concept:C0205615 | lld:lifeskim |
pubmed-article:2502549 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
pubmed-article:2502549 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:2502549 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
pubmed-article:2502549 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:2502549 | pubmed:issue | 22 | lld:pubmed |
pubmed-article:2502549 | pubmed:dateCreated | 1989-9-7 | lld:pubmed |
pubmed-article:2502549 | pubmed:abstractText | Exposure of human HL60 cells to dimethyl sulfoxide results in their differentiation to mature granulocyte-like cells that concomitantly acquire the capacity to synthesize leukotrienes. The appearance of 5-lipoxygenase mRNA during differentiation indicated that these cells provide a useful model system for the biosynthesis and regulation of 5-lipoxygenase. Immunoblot analysis of protein from differentiated HL60 cells detected a 78,000-Da species comigrating with 5-lipoxygenase purified from human peripheral blood leukocytes. Metabolic labeling studies indicated that both undifferentiated and differentiated HL60 cells synthesized 5-lipoxygenase; however, the differentiated cells incorporated approximately 4.4-fold more [35S]methionine into 5-lipoxygenase protein than did controls. In addition, the differentiated HL60 cells contained approximately 3.3-fold more 5-lipoxygenase enzyme activity than undifferentiated cells. Metabolic labeling studies failed to demonstrate any post-translational modifications of 5-lipoxygenase, including proteolysis, mannose glycosylation, myristic acid acylation, or phosphorylation. When differentiated HL60 cells were incubated with [35S]methionine for 4 versus 16 h, no difference was observed in the pattern of total radiolabeled supernatant protein; however, there was a significant increase in the incorporation of radioactivity into immunoprecipitable 5-lipoxygenase protein from cells labeled for 16 as compared with 4 h. Pulse-chase studies demonstrated that the t1/2 of 5-lipoxygenase in these cells is approximately 26 h. Activation of differentiated HL60 cells with Ca2+ ionophore A23187 resulted in the loss of 5-lipoxygenase protein and activity from the cytosol and the accumulation of inactive protein in a membrane fraction. Following ionophore stimulation, no augmentation in the rate of 5-lipoxygenase synthesis occurred in order to compensate for the loss of the translocated/inactive enzyme. Finally, additional 5-lipoxygenase was able to translocate to the membrane in response to subsequent ionophore challenges. | lld:pubmed |
pubmed-article:2502549 | pubmed:language | eng | lld:pubmed |
pubmed-article:2502549 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2502549 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2502549 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2502549 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2502549 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2502549 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2502549 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2502549 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2502549 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2502549 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2502549 | pubmed:month | Aug | lld:pubmed |
pubmed-article:2502549 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:2502549 | pubmed:author | pubmed-author:RouzerC ACA | lld:pubmed |
pubmed-article:2502549 | pubmed:author | pubmed-author:KargmanSS | lld:pubmed |
pubmed-article:2502549 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2502549 | pubmed:day | 5 | lld:pubmed |
pubmed-article:2502549 | pubmed:volume | 264 | lld:pubmed |
pubmed-article:2502549 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2502549 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2502549 | pubmed:pagination | 13313-20 | lld:pubmed |
pubmed-article:2502549 | pubmed:dateRevised | 2004-11-17 | lld:pubmed |
pubmed-article:2502549 | pubmed:meshHeading | pubmed-meshheading:2502549-... | lld:pubmed |
pubmed-article:2502549 | pubmed:meshHeading | pubmed-meshheading:2502549-... | lld:pubmed |
pubmed-article:2502549 | pubmed:meshHeading | pubmed-meshheading:2502549-... | lld:pubmed |
pubmed-article:2502549 | pubmed:meshHeading | pubmed-meshheading:2502549-... | lld:pubmed |
pubmed-article:2502549 | pubmed:meshHeading | pubmed-meshheading:2502549-... | lld:pubmed |
pubmed-article:2502549 | pubmed:meshHeading | pubmed-meshheading:2502549-... | lld:pubmed |
pubmed-article:2502549 | pubmed:meshHeading | pubmed-meshheading:2502549-... | lld:pubmed |
pubmed-article:2502549 | pubmed:meshHeading | pubmed-meshheading:2502549-... | lld:pubmed |
pubmed-article:2502549 | pubmed:meshHeading | pubmed-meshheading:2502549-... | lld:pubmed |
pubmed-article:2502549 | pubmed:meshHeading | pubmed-meshheading:2502549-... | lld:pubmed |
pubmed-article:2502549 | pubmed:meshHeading | pubmed-meshheading:2502549-... | lld:pubmed |
pubmed-article:2502549 | pubmed:meshHeading | pubmed-meshheading:2502549-... | lld:pubmed |
pubmed-article:2502549 | pubmed:meshHeading | pubmed-meshheading:2502549-... | lld:pubmed |
pubmed-article:2502549 | pubmed:meshHeading | pubmed-meshheading:2502549-... | lld:pubmed |
pubmed-article:2502549 | pubmed:meshHeading | pubmed-meshheading:2502549-... | lld:pubmed |
pubmed-article:2502549 | pubmed:meshHeading | pubmed-meshheading:2502549-... | lld:pubmed |
pubmed-article:2502549 | pubmed:year | 1989 | lld:pubmed |
pubmed-article:2502549 | pubmed:articleTitle | Studies on the regulation, biosynthesis, and activation of 5-lipoxygenase in differentiated HL60 cells. | lld:pubmed |
pubmed-article:2502549 | pubmed:affiliation | Merck Frosst Canada Inc., Pointe Claire-Dorval, Quebec, Canada. | lld:pubmed |
pubmed-article:2502549 | pubmed:publicationType | Journal Article | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2502549 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2502549 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2502549 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2502549 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2502549 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2502549 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2502549 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2502549 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2502549 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2502549 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2502549 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2502549 | lld:pubmed |