Novel synthetic heparin binding peptides of laminin and fibronectin which promote the adhesion of melanoma cells.
A synthetic peptide derived from the B1 chain of laminin, F-9, as well as two peptides derived from the 33-kilodalton fragment of fibronectin, I and II, directly promoted the adhesion of K-1735-M4 metastatic murine melanoma cells. In competition assays, adhesion of these cells to laminin was inhibited by excess soluble peptide F-9. Peptides F-9, I, and II specifically bound 3H-heparin, both by direct binding assays and indirect competition assays. 3H-heparin binding to peptide F-9 was specific as determined by competition with excess unlabeled heparin, dextran sulfate, and dermatan sulfate. These findings suggest that melanoma cell surface associated heparin-like molecules may act as receptors for these domains of laminin and fibronectin.
Skubitz
A P
AP
Department of Laboratory Medicine and Pathology, University of Minnesota, Minneapolis.
McCarthy
J B
JB
Charonis
A S
AS
Furcht
L T
LT
D000818:Animals; D002448:Cell Adhesion / Q000187:drug effects; D005353:Fibronectins / Q000378:metabolism / Q000494:pharmacology*; D006493:Heparin / Q000378:metabolism*; D007797:Laminin / Q000378:metabolism / Q000494:pharmacology*; D008546:Melanoma, Experimental / Q000473:pathology*; D051379:Mice; D010446:Peptide Fragments / Q000494:pharmacology*; D014407:Tumor Cells, Cultured
D005353:Fibronectins; D007797:Laminin; D010446:Peptide Fragments; D006493:Heparin