A family of cell-surface glycoproteins defined by a putative anti-endothelial cell receptor antibody in man.

An efficient immune response depends directly on the ability of lymphocytes and other blood borne leukocytes to leave the blood and enter lymphoid organs and other sites of immune response or inflammation. A new murine mAb termed 515 recognizes a 85- to 90-kDa structure involved in lymphocyte binding to specialized endothelium in postcapillary venules of lymphoid organs (high endothelial venules). In crossed immunoprecipitations followed by SDS-PAGE analysis, 515 appears to be identical to the antilymphocyte homing receptor mAb, Hermes-1. We show here that 515 recognizes peripheral blood leukocytes of all classes examined, but, like Hermes-1, fails to recognize germinal center cells or nearly all cortical (but not medullary) thymocytes. In addition, we demonstrate that 515 recognizes both fibroblasts and epidermal keratinocytes, both in situ and in cultured cell lines. Immunoprecipitation and SDS-PAGE analysis reveals that 515-defined Ag from T lymphocytes, neutrophils, and the epidermal keratinocyte cell line HaCaT are clearly distinct, both before and after treatment with peptide N-glycosidase F, which removes all asparagine-linked oligosaccharides. In contrast, the Mr of 515-defined Ag from T cells and fibroblasts appear indistinguishable. Thus, the 515 mAb recognizes a broadly distributed family of glycoproteins which may be involved in a variety of adhesive functions.