Identification of a novel adhesion molecule in human leukocytes by monoclonal antibody LB-2

FEBS Lett. 1987 Jan 5;210(2):127-31. doi: 10.1016/0014-5793(87)81321-2.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Antibodies, Monoclonal
  • Antigens, Surface / analysis*
  • Cell Adhesion / drug effects
  • Cell Adhesion Molecules
  • Cell Aggregation
  • Cell Line
  • Humans
  • Leukocytes / analysis*
  • Leukocytes / cytology
  • Tetradecanoylphorbol Acetate / pharmacology

Substances

  • Antibodies, Monoclonal
  • Antigens, Surface
  • Cell Adhesion Molecules
  • Tetradecanoylphorbol Acetate