A peptide fraction from factor VIII reduces PKC activity in cultured endothelial cells.
A peptide fraction of low molecular weight (Vueffe) prepared from bovine Factor VIII by enzymatic hydrolysis with trypsin, reduces significantly (p<0.05) membrane bound protein kinase C (PKC) activity in cultured bovine pulmonary artery endothelial cells grown with enhanced glucose levels (22.2 mM) or stimulated by phorbol 12-myristate 13-acetate (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 suggest that the antihaemorrhagic properties of Vueffe could be related to a decrease in endothelial permeability mediated by PKC.
Pazzagli
L
L
Department of Biochemical Science, University of Florence, Italy.
Cecchi
C
C
Cappugi
G
G
Catalani
R
R
Bertini
M
M
Jollès
P
P
Ramponi
G
G
D000818:Animals; D002417:Cattle; D002460:Cell Line; D002462:Cell Membrane / Q000187:drug effects / Q000201:enzymology; D002463:Cell Membrane Permeability / Q000187:drug effects; D004730:Endothelium, Vascular / Q000166:cytology / Q000201:enzymology*; D005169:Factor VIII / Q000737:chemistry*; D006490:Hemostatics / Q000494:pharmacology; D010446:Peptide Fragments / Q000494:pharmacology*; D010455:Peptides / Q000494:pharmacology*; D011493:Protein Kinase C / Q000037:antagonists & inhibitors*; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology
D006490:Hemostatics; D010446:Peptide Fragments; D010455:Peptides; C082195:Vueffe; D005169:Factor VIII; D011493:Protein Kinase C; D013755:Tetradecanoylphorbol Acetate