CD63 associates with CD11/CD18 in large detergent‐resistant complexes after translocation to the cell surface in human neutrophils 1

FEBS Letters

Skubitz, Keith M.¹  Campbell, Kenneth D.¹  Skubitz, Amy P.N.² 

[1] Department of Medicine, The University of Minnesota Medical School, Minneapolis, MN 55455, USA;Department of Laboratory Medicine and Pathology, The University of Minnesota Medical School, Minneapolis, MN 55455, USA

关键词: Inflammation;    Granulocyte;    Integrin;    Neutrophil activation;    Membrane domain;    CD63;    SDS–PAGE;    sodium dodecyl sulfate–polyacrylamide gel electrophoresis;    GPI;    glycosyl-phosphatidylinositol;    DFP;    diisopropylfluorophosphate;    NMS;    normal mouse serum;    PBS;    phosphate buffered saline;    pH 7.4;    Brij solubilization buffer;    20 mM Tris–HCl;    pH 8.2;    150 mM NaCl;    1 mM PMSF;    2 mM MgCl2;    0.02% NaN3 and 1.0% Brij 58;    Brij wash buffer;    20 mM Tris–HCl;    pH 8.2;    150 mM NaCl;    1 mg/ml BSA;    0.5% Brij 58;    2 mM MgCl2;    0.125 mg/ml gelatin;    1 mM PMSF and 0.02% NaN3;   

DOI  :  10.1016/S0014-5793(00)01240-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

CD63 antibody binding to the neutrophil surface triggers a transient activation signal that regulates the adhesive activity and surface expression of CD11/CD18. Gel permeation chromatography demonstrated that all of the cell surface CD11/CD18 associated with CD63 eluted in the void volume, indicating that they were present in large detergent-resistant complexes. In contrast, the majority of the total cellular CD63, CD11 and CD18, which are largely intracellular, was not present in complexes. The data suggest that intracellular CD11, CD18 and CD63 are not in detergent-resistant complexes, but enter such complexes following translocation to the cell surface.

【 授权许可】

Unknown