Identification of laminin alpha 1 and beta 1 chain peptides active for endothelial cell adhesion, tube formation, and aortic sprouting

Laminin-1 is a basement membrane glycoprotein that promotes several biologi cal activities including cell attachment, tumor metastasis, and angiogenesi s. Angiogenesis plays an important role in tissue formation, reproduction, wound healing,;md several pathological conditions. In this study, we screen ed 405 synthetic peptides from the al and pi chains to identify potential s ites on laminin-l active with endothelial cells, Peptides were initially sc reened by testing both endothelial cell adhesion to peptide-coated wells an d tube formation on Matrigel in the presence of soluble peptide. Twenty act ive peptides were identified in these screens, A secondary screen using the rat aortic ring sprouting assay identified 13 of the 20 peptides that stim ulated endothelial sprouting, Several of these active peptides were also fo und to stimulate human umbilical vein endothelial cell migration in Boyden chamber assays. Differences in the amount of peptide needed for the respons e and in the resultant morphologies/responses were observed between the pep tides in all of the assays. Our results suggest that several active domains on laminin-1 may play important roles in stimulating different steps in an giogenesis.