title: Vitronectin in the substratum of endothelial cells is cross-linked and phosphorylated.
abstract: Vitronectin (VN), previously shown to be a substrate for purified transglutaminases, was demonstrated in this study to be cross-linked when incubated with HUVEC and EAhy926 cells. The cross-linking was calcium-dependent and required that VN be plated at the substratum of the cells. These cells also phosphorylated VN, but in contrast to a previous study demonstrating a cAMP-dependent protein kinase in platelets, the phosphorylation of VN by was decreased with the addition of 1mM cAMP. The cross-linking of VN by endothelial cells demonstrates that the adhesion of these cells to VN is a dynamic process in which the substratum may be enzymatically altered. Furthermore, the modifications of VN by cross-linking and phosphorylation could modulate the functions of VN and influence events such as endothelial cell proliferation and angiogenesis.
authors.affiliation: Department of Medicine, Duke University Medical Center, Durham, NC 27710.
authors.forename: D C
authors.initials: DC
authors.lastname: Sane
authors.forename: T L
authors.initials: TL
authors.lastname: Moser
authors.forename: C S
authors.initials: CS
authors.lastname: Greenberg
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D002460:Cell Line; D002478:Cells, Cultured; D003432:Cross-Linking Reagents; D000242:Cyclic AMP / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D004730:Endothelium, Vascular / Q000378:metabolism*; D006023:Glycoproteins / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D015151:Immunoblotting; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism; D019096:Vitronectin
chemical_list: D003432:Cross-Linking Reagents; D006023:Glycoproteins; D019096:Vitronectin; D000255:Adenosine Triphosphate; D000242:Cyclic AMP; D011494:Protein Kinases