ADHESION OF MOUSE HEPATOCYTES TO TYPE-I COLLAGEN - ROLE OF SUPRAMOLECULAR FORMS AND EFFECT OF PROTEOLYTIC DEGRADATION

Mouse hepatocytes were found to adhere much stronger to intact native type I collagen than to native, telopeptide-devoid collagen. Removal of telopeptides (by pepsin treatment) caused disintegration of supramolecular collagen aggregates. Similar differences in hepatocyte adhesion were observed between oligomeric and monomeric collagens separated from intact native preparations. It was concluded that the more active cell binding to intact collagen is due to a higher binding affinity of hepatocytes to supramolecular (oligomeric) forms of type I collagen. Heat denaturation did not affect cell adhesion to intact collagen but restored adhesion to telopeptide-devoid substrates. Cell adhesion to denatured collagen was RGD-dependent whereas adhesion to native substrated proved RGD-independent. These data provide the first evidence of the role of supramolecular arrangement and the effect of proteolytic degradation of type I collagen on its adhesive behavior. © 1993 Academic Press, Inc.