Summary In order to identify cell-substrate adhesion receptors on vascular endothelium, murine monoclonal antibodies (MoAb) were raised against human umbilical vein endotheiial cells (HUVE). One anli-HUVE MoAb, RMACl 1. identified the adhesion receptor VLA-2 as it immunoprecipitated a non-covalently linked heterodimer of 160 kD and 130 kD. which was identical to the heterodimer immunoprecipitated by the anti-VLA-2 MoAb. 12F1 and 5E8. Furthermore, proteolytic peptide maps of the VLA-2 a-and [i-chains were highly homologous with those of the RMACl l-recognized molecule. However, unlike other VLA-2 MoAb. RMACl I also identified an 85 kD band which migrated to 90 kD under reducing conditions. This band was most likely a fragment of the 160 kD a-chain as a similar u-chain derived fragment has been demonstrated in the immunoprecipilates of some VLA-4 reactive monoclonals. However the possibility that this may be a novel molecule associated with VLA-2 has not been excluded. M viirn assays of HUVE adhesion to collagen types I and 4, lamininand fibronectin showed that RMACl I blocked adhesion to collagen (types 1 and 4) and laminin, but had no effect on HUVE adhesion to fibronectin. confirming that VLA-2 is a collagen and laminin reeeptor for HUVE.