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CD63 associates with CD11/CD18 in large detergent-resistant complexes after translocation to the cell surface in

K M Skubitz1, K D Campbell, A P Skubitz

  • 1Department of Medicine, The University of Minnesota Medical School, Minneapolis, MN 55455, USA. skubi001@tc.umn.edu

FEBS Letters
|March 10, 2000
PubMed

Insights

Neutrophil activation by CD63 antibody binding leads to CD11/CD18 complex formation. Intracellular proteins CD63, CD11, and CD18 associate into these complexes upon cell surface translocation.

Area of Science:

  • Immunology
  • Cell Biology
  • Biochemistry

Background:

  • CD63 is a tetraspanin protein involved in various cellular processes.
  • CD11/CD18 integrins are crucial for neutrophil adhesion and immune responses.
  • The relationship between CD63 and CD11/CD18 complex formation was not fully understood.

Purpose of the Study:

  • To investigate the role of CD63 in regulating CD11/CD18 adhesive activity.
  • To determine if CD63 and CD11/CD18 form detergent-resistant complexes (DRCs).
  • To elucidate the state of intracellular versus cell surface CD63, CD11, and CD18 in relation to DRCs.

Main Methods:

  • Neutrophil activation via CD63 antibody binding.
  • Gel permeation chromatography to analyze protein complexes.
  • Detergent solubility assays to identify DRCs.

Main Results:

  • CD63 antibody binding induced transient neutrophil activation, regulating CD11/CD18.
  • Cell surface CD11/CD18 associated with CD63 were found in large DRCs.
  • Intracellular CD63, CD11, and CD18 were predominantly not part of DRCs.

Conclusions:

  • Neutrophil surface CD63 triggers signaling that impacts CD11/CD18 adhesive function.
  • CD11/CD18 and CD63 associate into large detergent-resistant complexes upon cell surface expression.
  • Intracellular CD11, CD18, and CD63 exist as non-complexed proteins before translocation to the cell surface.

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