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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Vascular endothelial growth factor stimulates prostacyclin production and activation of cytosolic phospholipase A2 in endothelial cells via p42/ p44 mitogen-activated protein kinase.

Vascular endothelial growth factor (VEGF) stimulated a time- and concentration-dependent increase in PGI2 synthesis in human umbilical vein endothelial cells with a mean maximum increase of 2-fold above basal levels at 25 ng/ml after 60 min. VEGF also rapidly stimulated the release of arachidonic acid and phosphorylation and activation of cytosolic phospholipase A2 ( cPLA2). The VEGF-related factor, placenta growth factor (PIGF), had little effect on PGI2 synthesis, arachidonic acid release or cPLA2 activation. PD98059, a selective inhibitor of MAP kinase kinase, caused complete inhibition of VEGF-stimulated MAP kinase activity, PGI2 synthesis and cPLA2 gel retardation, but had no effect on VEGF- induced vWF secretion. These findings provide the first evidence that VEGF can stimulate PGI2 synthesis via cPLA2- mediated arachidonic acid release and indicate that VEGF stimulation of this biosynthetic pathway may occur, at least in part, via activation of p42/ p44 MAP kinases.[1]

References

  1. Vascular endothelial growth factor stimulates prostacyclin production and activation of cytosolic phospholipase A2 in endothelial cells via p42/p44 mitogen-activated protein kinase. Wheeler-Jones, C., Abu-Ghazaleh, R., Cospedal, R., Houliston, R.A., Martin, J., Zachary, I. FEBS Lett. (1997) [Pubmed]
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