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A more recent version of this article appeared on April 1, 2007

Papers In Press, published online ahead of print January 31, 2007
J. Lipid Res., doi:10.1194/jlr.M600489-JLR200
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Submitted on November 15, 2006
Revised on January 12, 2007
Accepted on January 30, 2007

Brain endothelial cell - retinal pericyte co-cultures induce cytosolic PLA2 protein expression through activation of PKCalpha and MAPK/ERK cascade

Carmelina Daniela Anfuso, Gabriella Lupo, Loriana Romeo, Giovanni Giurdanella, Alessia Pascale, Cataldo Tirolo, Bianca Marchetti, and Mario Alberghina

Department of Biochemistry, University of Catania, Catania, Sicily 95125

Corresponding Author: malber{at}unict.it

Little is known about the regulatory mechanisms of endothelial cell proliferation by retinal pericytes and viceversa. In a model of co-culture with bovine retinal pericytes lasting for 24 h, rat brain endothelial cells (ECs) showed an increase in arachidonic acid (AA) release while Western blot and RT-PCR analyses revealed that ECs activated the protein expression of cytosolic phospholipase A2 (cPLA2) and its phosphorylated form, and calcium independent phospholipase A2 (iPLA2). No activation of the same enzymes was seen in companion pericytes. In ECs, the protein level of phosphorylated extracellular signal-regulated kinase ERK1/2 was also significantly enhanced, findings not observed in co-cultured pericytes. The expression of PKCalpha and its phosphorylated form were also enhanced in ECs. Wortmannin and LY294002, and PD98059, used as inhibitors of upstream kinases (the PI3-kinase/Akt/PDK1 or MEK-1 pathways) in cultures, markedly attenuated AA release and the expression of phosphorylated forms of endothelial cPLA2, PKCalpha , and ERK1/2. By confocal microscopy, activation of PKCalpha in perinuclear regions in ECs grown in co-culture as well as strong activation of cPLA2 in ECs taken from a model of mixed culture were clearly observed. However, no increased expression of both enzymes was found in co-cultured pericytes. Our findings conclude that a sequential activation of PKC (alpha contributes to endothelial ERK1/2 and cPLA2 phosphorylation induced by either soluble factors or direct cell-to-cell contact, and that PKCalpha -cPLA2 pathway appears to play a key role in the early phase of endothelial cell-pericyte interactions regulating blood retina or blood brain barrier maturation.


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