| pubmed-article:9252247 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9252247 | lifeskim:mentions | umls-concept:C0033692 | lld:lifeskim |
| pubmed-article:9252247 | lifeskim:mentions | umls-concept:C1257792 | lld:lifeskim |
| pubmed-article:9252247 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
| pubmed-article:9252247 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
| pubmed-article:9252247 | lifeskim:mentions | umls-concept:C0031586 | lld:lifeskim |
| pubmed-article:9252247 | lifeskim:mentions | umls-concept:C0332293 | lld:lifeskim |
| pubmed-article:9252247 | lifeskim:mentions | umls-concept:C2349975 | lld:lifeskim |
| pubmed-article:9252247 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:9252247 | pubmed:dateCreated | 1997-8-29 | lld:pubmed |
| pubmed-article:9252247 | pubmed:abstractText | We investigated the biosynthesis of proteoglycans (PG) in endothelial cells following their treatment with phorbol 12-myristate 13-acetate (PMA). Confluent cultures of bovine aortic endothelial cells were incubated in the presence and absence of PMA (100 ng/ml) and then pulsed with [35S]sulfate, [3H]glucosamine, or [35S]sulfate plus [3H]leucine for varying times in the absence of PMA. Alternatively, confluent endothelial cells were simultaneously incubated with PMA and [35S]sulfate for varying times. The metabolically labeled PG in the cell layer and medium were analyzed. Both short-term and prolonged exposure of endothelial cells to PMA significantly stimulated PG synthesis, regardless of the experimental conditions. [35S]sulfate incorporation into newly synthesized PG in PMA-treated cells also increased by 1.7-fold and 3.6-fold over control cells, following a 15-min and 30-min pulse, respectively. Cycloheximide markedly inhibited the increased synthesis of PG in PMA-treated cells, while actinomycin D produced a moderate inhibition. PG secretion was increased in PMA-treated cells compared with control cells, while there was no significant difference in PG degradation between the two cultures. PG from control and PMA-treated endothelial cell cultures did not differ in composition or hydrodynamic sizes. The incorporation of [3H]leucine into total cellular proteins decreased significantly following exposure of endothelial cells to PMA. Endothelial cells exposed to PMA for 3 h had significantly more protein kinase C (PKC) activity than did control cells. Inhibition of PKC by calphostin C abolished the PMA-mediated stimulation of PG synthesis in endothelial cells. The results indicate that PMA stimulates PG synthesis in endothelial cells either directly or indirectly through a PKC dependent mechanism. | lld:pubmed |
| pubmed-article:9252247 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9252247 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9252247 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9252247 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9252247 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9252247 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9252247 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9252247 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9252247 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9252247 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9252247 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9252247 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9252247 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9252247 | pubmed:issn | 0024-3205 | lld:pubmed |
| pubmed-article:9252247 | pubmed:author | pubmed-author:GlancyD LDL | lld:pubmed |
| pubmed-article:9252247 | pubmed:author | pubmed-author:VijayagopalPP | lld:pubmed |
| pubmed-article:9252247 | pubmed:author | pubmed-author:FigueroaJ EJE | lld:pubmed |
| pubmed-article:9252247 | pubmed:author | pubmed-author:SmartF WFW | lld:pubmed |
| pubmed-article:9252247 | pubmed:author | pubmed-author:TaxSS | lld:pubmed |
| pubmed-article:9252247 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9252247 | pubmed:volume | 61 | lld:pubmed |
| pubmed-article:9252247 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9252247 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9252247 | pubmed:pagination | 723-38 | lld:pubmed |
| pubmed-article:9252247 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:9252247 | pubmed:meshHeading | pubmed-meshheading:9252247-... | lld:pubmed |
| pubmed-article:9252247 | pubmed:meshHeading | pubmed-meshheading:9252247-... | lld:pubmed |
| pubmed-article:9252247 | pubmed:meshHeading | pubmed-meshheading:9252247-... | lld:pubmed |
| pubmed-article:9252247 | pubmed:meshHeading | pubmed-meshheading:9252247-... | lld:pubmed |
| pubmed-article:9252247 | pubmed:meshHeading | pubmed-meshheading:9252247-... | lld:pubmed |
| pubmed-article:9252247 | pubmed:meshHeading | pubmed-meshheading:9252247-... | lld:pubmed |
| pubmed-article:9252247 | pubmed:meshHeading | pubmed-meshheading:9252247-... | lld:pubmed |
| pubmed-article:9252247 | pubmed:meshHeading | pubmed-meshheading:9252247-... | lld:pubmed |
| pubmed-article:9252247 | pubmed:meshHeading | pubmed-meshheading:9252247-... | lld:pubmed |
| pubmed-article:9252247 | pubmed:meshHeading | pubmed-meshheading:9252247-... | lld:pubmed |
| pubmed-article:9252247 | pubmed:meshHeading | pubmed-meshheading:9252247-... | lld:pubmed |
| pubmed-article:9252247 | pubmed:meshHeading | pubmed-meshheading:9252247-... | lld:pubmed |
| pubmed-article:9252247 | pubmed:meshHeading | pubmed-meshheading:9252247-... | lld:pubmed |
| pubmed-article:9252247 | pubmed:meshHeading | pubmed-meshheading:9252247-... | lld:pubmed |
| pubmed-article:9252247 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9252247 | pubmed:articleTitle | Enhanced synthesis of proteoglycans by vascular endothelial cells treated with phorbol ester. | lld:pubmed |
| pubmed-article:9252247 | pubmed:affiliation | Ochsner Medical Institutions, Department of Medicine, Louisiana State University Medical Center, New Orleans 70112, USA. | lld:pubmed |
| pubmed-article:9252247 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9252247 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9252247 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
