title: Elastin repeat peptides as chemoattractants for bovine aortic endothelial cells.
abstract: Cultured bovine aortic endothelial cells migrate toward a concentration gradient of repeating elastin peptides, specifically the repeating nonamers Gly-Phe-Gly-Val-Gly-Ala-Gly-Val-Pro and Gly-Leu-Gly-Val-Gly-Ala-Gly-Val-Pro and the repeating hexamer Val-Gly-Val-Ala-Pro-Gly. Dose-response experiments demonstrate that the peak of activity occurs at 8 x 10(-8) M for the nonapeptides and 1 x 10(-8) M for the hexapeptide. Checkerboard assays establish that the movement is chemotaxis and not chemokinesis. Because of the concentration difference in the responsiveness between the nonapeptide and the hexapeptide, the cells can differentiate between the two types of repeats. The positive control for the chemotaxis studies was fibronectin.
authors: Department of Anesthesiology, School of Medicine, University of Alabama, Birmingham 35294.
authors: M M
authors: MM
authors: Long
authors: V J
authors: VJ
authors: King
authors: K U
authors: KU
authors: Prasad
authors: B A
authors: BA
authors: Freeman
authors: D W
authors: DW
authors: Urry
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002633:Chemotaxis; D004549:Elastin / Q000494:pharmacology*; D004730:Endothelium, Vascular / Q000502:physiology*; D066298:In Vitro Techniques; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D009389:Neovascularization, Pathologic; D009842:Oligopeptides / Q000138:chemical synthesis / Q000494:pharmacology; D013329:Structure-Activity Relationship
chemical_list: D009842:Oligopeptides; D004549:Elastin