CD157 is part of a supramolecular complex with CD11b/CD18 on the human neutrophil cell surface

J Biol Regul Homeost Agents. 2007;21(1-2):5-11.

Abstract

CD157 is a GPI-anchored cell surface glycoprotein expressed by human peripheral blood neutrophils. Cross-linking of CD157 induces intracellular Ca2+ mobilization and re-shaping in neutrophils, thus regulating their adhesive and migratory properties. Results obtained by immunolocalization and confocal microscopy indicate that CD157 lies in close proximity to the CD11b/CD18 complex which is strongly expressed on the activated neutrophil cell membrane where it plays a predominant role in adhesion. This study analyses the physical association between CD157 and CD18 in human neutrophils by co-immunoprecipitation experiments. The anti-CD157 monoclonal antibody RF3 co-precipitates CD18, and the anti-CD18 antibody TS1/18 co-precipitates CD157 from human neutrophil lysates. These results confirm that CD157 physically interacts with CD11b/CD18 complex in human neutrophils.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ADP-ribosyl Cyclase / immunology
  • ADP-ribosyl Cyclase / metabolism*
  • Antibodies, Monoclonal / immunology
  • Antigens, CD / immunology
  • Antigens, CD / metabolism*
  • Blotting, Western
  • CD11b Antigen / immunology
  • CD11b Antigen / metabolism*
  • CD18 Antigens / immunology
  • CD18 Antigens / metabolism*
  • Flow Cytometry
  • GPI-Linked Proteins
  • Humans
  • Immunoprecipitation
  • Microscopy, Confocal
  • Neutrophils / metabolism*
  • Protein Interaction Mapping

Substances

  • Antibodies, Monoclonal
  • Antigens, CD
  • CD11b Antigen
  • CD18 Antigens
  • GPI-Linked Proteins
  • ITGAM protein, human
  • ADP-ribosyl Cyclase
  • ADP-ribosyl cyclase 2