Linked Life Data

9252247

Source:http://linkedlifedata.com/resource/pubmed/id/9252247

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1997-8-29
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0024-3205
pubmed:author
pubmed:issnType
Print
pubmed:volume
61
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
723-38
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Enhanced synthesis of proteoglycans by vascular endothelial cells treated with phorbol ester.
pubmed:affiliation
Ochsner Medical Institutions, Department of Medicine, Louisiana State University Medical Center, New Orleans 70112, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't