Source:http://linkedlifedata.com/resource/pubmed/id/17267947
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
|
pubmed:dateCreated |
2007-3-27
|
pubmed:abstractText |
Little is known about the regulatory mechanisms of endothelial cell (EC) proliferation by retinal pericytes and vice versa. In a model of coculture with bovine retinal pericytes lasting for 24 h, rat brain ECs showed an increase in arachidonic acid (AA) release, whereas Western blot and RT-PCR analyses revealed that ECs activated the protein expression of cytosolic phospholipase A(2) (cPLA(2)) and its phosphorylated form and calcium-independent intracellular phospholipase A(2) (iPLA(2)). No activation of the same enzymes was seen in companion pericytes. In ECs, the protein level of phosphorylated extracellular signal-regulated kinase (ERK) 1/2 was also enhanced significantly, a finding not observed in cocultured pericytes. The expression of protein kinase C-alpha (PKCalpha) and its phosphorylated form was also enhanced in ECs. Wortmannin, LY294002, and PD98059, used as inhibitors of upstream kinases (the PI3-kinase/Akt/PDK1 or MEK-1 pathway) in cultures, markedly attenuated AA release and the expression of phosphorylated forms of endothelial cPLA(2), PKCalpha, and ERK1/2. By confocal microscopy, activation of PKCalpha in perinuclear regions of ECs grown in coculture as well as strong activation of cPLA(2) in ECs taken from a model of mixed culture were clearly observed. However, no increased expression of both enzymes was found in cocultured pericytes. Our findings indicate that a sequential activation of PKCalpha contributes to endothelial ERK1/2 and cPLA(2) phosphorylation induced by either soluble factors or direct cell-to-cell contact, and that the PKCalpha-cPLA(2) pathway appears to play a key role in the early phase of EC-pericyte interactions regulating blood retina or blood-brain barrier maturation.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Apr
|
pubmed:issn |
0022-2275
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
48
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
782-93
|
pubmed:dateRevised |
2009-11-19
|
pubmed:meshHeading |
pubmed-meshheading:17267947-Animals,
pubmed-meshheading:17267947-Cattle,
pubmed-meshheading:17267947-Cell Communication,
pubmed-meshheading:17267947-Coculture Techniques,
pubmed-meshheading:17267947-Endothelial Cells,
pubmed-meshheading:17267947-Endothelium, Vascular,
pubmed-meshheading:17267947-Gene Expression Regulation,
pubmed-meshheading:17267947-MAP Kinase Signaling System,
pubmed-meshheading:17267947-Pericytes,
pubmed-meshheading:17267947-Phospholipases A,
pubmed-meshheading:17267947-Phospholipases A2,
pubmed-meshheading:17267947-Protein Kinase C-alpha,
pubmed-meshheading:17267947-Rats
|
pubmed:year |
2007
|
pubmed:articleTitle |
Endothelial cell-pericyte cocultures induce PLA2 protein expression through activation of PKCalpha and the MAPK/ERK cascade.
|
pubmed:affiliation |
Department of Biochemistry, University of Catania, 95126 Catania, Italy.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|