Identification of a novel adhesion molecule in human leukocytes by monoclonal antibody LB-2.
Monoclonal antibody LB-2 to a surface antigen on human B cells, lymphoblast, monocytes and vascular endothelial cells largely inhibited adhesion among Epstein Barr virus-immortalized normal B cells (EBV-B) and concanavalin A-stimulated blood mononuclear cells (Con A-BMC) before and after phorbol ester treatment. The antibody inhibited to a lesser extent phorbol ester-induced aggregation of monocytes, U937 cells and fresh BMC and had virtually no inhibitory effect on the adhesion among enriched T cells and granulocytes. A surface glycoprotein band of 84 kDa was obtained from EBV-B cells by immunoprecipitation and gel electrophoresis. Immunological and biochemical studies clearly distinguished this molecule from gp90 and associated glycoproteins which also mediate leukocyte adhesion.
D000911:Antibodies, Monoclonal; D000954:Antigens, Surface / Q000032:analysis*; D002448:Cell Adhesion / Q000187:drug effects; D015815:Cell Adhesion Molecules; D002449:Cell Aggregation; D002460:Cell Line; D006801:Humans; D007962:Leukocytes / Q000032:analysis* / Q000166:cytology; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology
D000911:Antibodies, Monoclonal; D000954:Antigens, Surface; D015815:Cell Adhesion Molecules; D013755:Tetradecanoylphorbol Acetate