title: Synthetic peptides of the amino-terminus of fibronectin inhibit endothelial cell growth.
abstract: Amino-terminal and carboxyl-terminal fragments of human plasma fibronectin, at nM concentrations, reversibly inhibit the growth of cultured bovine aortic endothelial cells. To define smaller active peptides, synthetic peptides corresponding to a carboxyl-terminal disulfide bonded loop segment of one of the fragments were tested for activity and found to be active at microM concentrations. The data suggest that the entire loop sequence is required for full expression of endothelial cell growth inhibitory activity in vitro.
authors: Department of Biochemistry, Rush-Presbyterian-St Luke's Med. Ctr., Chicago, Ill 60612.
authors: G A
authors: GA
authors: Homandberg
authors: B M
authors: BM
authors: Dunn
authors: D M
authors: DM
authors: Grant
authors: B
authors: B
authors: Schumacher
authors: D M
authors: DM
authors: Bartley
authors: R
authors: R
authors: Eisenstein
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001011:Aorta; D002417:Cattle; D002455:Cell Division / Q000187:drug effects; D002478:Cells, Cultured; D004220:Disulfides; D004730:Endothelium, Vascular / Q000166:cytology*; D005353:Fibronectins / Q000494:pharmacology*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000494:pharmacology*; D013329:Structure-Activity Relationship
chemical_list: D004220:Disulfides; D005353:Fibronectins; D010446:Peptide Fragments