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.
A PEPTIDE FRACTION FROM FACTOR VIII REDUCES PKC ACTIVITY IN CULTURED ENDOTHELIAL CELLS / L. PAZZAGLI; C. CECCHI; G. CAPPUGI; R. CATALANI; P. JOLLES; G. RAMPONI. - In: LIFE SCIENCES. - ISSN 0024-3205. - STAMPA. - 62:(1998), pp. 829-837.
A PEPTIDE FRACTION FROM FACTOR VIII REDUCES PKC ACTIVITY IN CULTURED ENDOTHELIAL CELLS
PAZZAGLI, LUIGIA;CECCHI, CRISTINA;CAPPUGI, GIANNI;RAMPONI, GIAMPIETRO
1998
Abstract
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.File | Dimensione | Formato | |
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Pazzagli 1998 Life Sci.pdf
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