| pubmed-article:2557910 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2557910 | lifeskim:mentions | umls-concept:C0596981 | lld:lifeskim |
| pubmed-article:2557910 | lifeskim:mentions | umls-concept:C0020291 | lld:lifeskim |
| pubmed-article:2557910 | lifeskim:mentions | umls-concept:C0007582 | lld:lifeskim |
| pubmed-article:2557910 | lifeskim:mentions | umls-concept:C0010531 | lld:lifeskim |
| pubmed-article:2557910 | lifeskim:mentions | umls-concept:C0001128 | lld:lifeskim |
| pubmed-article:2557910 | lifeskim:mentions | umls-concept:C0008387 | lld:lifeskim |
| pubmed-article:2557910 | lifeskim:mentions | umls-concept:C1155502 | lld:lifeskim |
| pubmed-article:2557910 | lifeskim:mentions | umls-concept:C1515877 | lld:lifeskim |
| pubmed-article:2557910 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:2557910 | pubmed:issue | 22 | lld:pubmed |
| pubmed-article:2557910 | pubmed:dateCreated | 1990-2-15 | lld:pubmed |
| pubmed-article:2557910 | pubmed:abstractText | Fluid-phase interactions between hematologic cells and those of the vessel wall were studied in order to define a role for lipoxygenase products as cell signals in the control of vascular cholesterol metabolism. A functional parameter for hydroxy acids in this system has not been previously demonstrated. We report herein for the first time a biochemical effect of lipoxygenase-derived eicosanoids in the modulation of cholesterol metabolism in smooth muscle cells. Products of platelet-neutrophil interactions served as cell signals in vitro to modulate cholesterol metabolism. We demonstrate that 12-HETE, 12,20-DiHETE, and 12-HETE-1,20-dioic acid activate both lysosomal and cytoplasmic cholesteryl ester (CE) hydrolytic activities, although no effect was observed on CE synthetic (ACAT) activity. The platelet lipoxygenase product, 12-HETE, was the most effective stimulator of CE hydrolysis in the smooth muscle cell, and its conversion to 12,20-DiHETE and the dioic acid derivative by the neutrophils was not necessary for the activation of CE hydrolase. A 2-fold enhancement on CE hydrolysis occurred and was independent of any "cross-activation" by hydroxy acids on production of cyclooxygenase or other lipoxygenase products. The activation of cytoplasmic CE hydrolysis had a lesser cofactor dependence on bile salts in the presence of 12-HETE. This suggested a reduced requirement for surface-active agents in an enzyme-substrate interaction where enzymes are hydrolyzing insoluble lipid substrates. Moreover, 12-HETE induced an additive effect with several lipolytic hormones in the activation of CE catabolism.(ABSTRACT TRUNCATED AT 250 WORDS) | lld:pubmed |
| pubmed-article:2557910 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2557910 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2557910 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2557910 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2557910 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2557910 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2557910 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2557910 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2557910 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2557910 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2557910 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2557910 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2557910 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2557910 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:2557910 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:2557910 | pubmed:author | pubmed-author:MarcusA JAJ | lld:pubmed |
| pubmed-article:2557910 | pubmed:author | pubmed-author:HajjarD PDP | lld:pubmed |
| pubmed-article:2557910 | pubmed:author | pubmed-author:EtinginO ROR | lld:pubmed |
| pubmed-article:2557910 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2557910 | pubmed:day | 31 | lld:pubmed |
| pubmed-article:2557910 | pubmed:volume | 28 | lld:pubmed |
| pubmed-article:2557910 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2557910 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2557910 | pubmed:pagination | 8885-91 | lld:pubmed |
| pubmed-article:2557910 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:2557910 | pubmed:meshHeading | pubmed-meshheading:2557910-... | lld:pubmed |
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| pubmed-article:2557910 | pubmed:meshHeading | pubmed-meshheading:2557910-... | lld:pubmed |
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| pubmed-article:2557910 | pubmed:meshHeading | pubmed-meshheading:2557910-... | lld:pubmed |
| pubmed-article:2557910 | pubmed:meshHeading | pubmed-meshheading:2557910-... | lld:pubmed |
| pubmed-article:2557910 | pubmed:meshHeading | pubmed-meshheading:2557910-... | lld:pubmed |
| pubmed-article:2557910 | pubmed:meshHeading | pubmed-meshheading:2557910-... | lld:pubmed |
| pubmed-article:2557910 | pubmed:meshHeading | pubmed-meshheading:2557910-... | lld:pubmed |
| pubmed-article:2557910 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2557910 | pubmed:articleTitle | Platelet-neutrophil-smooth muscle cell interactions: lipoxygenase-derived mono- and dihydroxy acids activate cholesteryl ester hydrolysis by the cyclic AMP dependent protein kinase cascade. | lld:pubmed |
| pubmed-article:2557910 | pubmed:affiliation | Department of Biochemistry, Cornell University Medical College, New York, New York 10021. | lld:pubmed |
| pubmed-article:2557910 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2557910 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2557910 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:2557910 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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