Human perlecan immunopurified from different endothelial cell sources has different adhesive properties for vascular cells

Perlecan, a major heparan sulfate proteoglycan of vascularized tissues, was immunopurified from media conditioned by human endothelial cells of both a rterial and venous origin. The heparan sulfate moiety of perlecan from cult ured arterial cells differed in amount and/or composition from that produce d by a transformed cell line of venous origin. Both forms of perlecan bound basic fibroblast growth factor with K-d similar to 70 nM. In ELISA experim ents, perlecan and its protein core bound to various extracellular matrix c omponents in a manner that was strongly influenced by the format of the ass ay. Human vascular smooth muscle cells and human endothelial cells adhered to perlecan-coated surfaces, and both cell types adhered better to the veno us cell-derived than to the arterial cell-derived perlecan. Removal of the heparan sulfate chains abolished this difference and increased the ability of both types of perlecan to adhere vascular cells. Denaturation of perleca n and its protein core also rendered each of them more adhesive, indicating the presence of conformation-independent adhesion determinants in the poly peptide sequence. Their location was investigated using recombinant perleca n domains. Overall, our results represent the first demonstration of human perlecan acting as an adhesive molecule for human vascular cells and sugges t that it may play a role in vascular wound healing. (C) 1999 Elsevier Scie nce B.V./International Society of Matrix Biology. All rights reserved.