A PEPTIDE FRACTION FROM FACTOR-VIII REDUCES PKC ACTIVITY IN CULTURED ENDOTHELIAL-CELLS

A peptide fraction of low molecular weight (Vueffe(R)) prepared from b ovine Factor VIII by enzymatic hydrolysis with trypsin, reduces signif icantly (p<0.05) membrane bound protein kinase C (PKC) activity in cul tured bovine pulmonary artery endothelial cells grown with enhanced gl ucose levels (22.2 mM) or stimulated by phorbol 12-myristate 13-acetat e (PMA). The activation of PKC is a common pathway by which mediators increase transendothelial permeability during tissue inflammation and in the development of diabetic vascular complications. Our results sug gest that the antihaemorrhagic properties of Vueffe could be related t o a decrease in endothelial permeability mediated by PKC.