CD63 associates with CD11/CD18 in large detergent-resistant complexes after translocation to the cell surface in human neutrophils.
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.
Skubitz
K M
KM
Department of Medicine, The University of Minnesota Medical School, Minneapolis, MN 55455, USA. skubi001@tc.umn.edu
Campbell
K D
KD
Skubitz
A P
AP
D015703:Antigens, CD / Q000378:metabolism*; D018845:CD11 Antigens / Q000378:metabolism*; D018821:CD18 Antigens / Q000378:metabolism*; D002462:Cell Membrane / Q000276:immunology; D002850:Chromatography, Gel; D003902:Detergents; D006801:Humans; D015151:Immunoblotting; D009504:Neutrophils / Q000276:immunology*; D010980:Platelet Membrane Glycoproteins / Q000378:metabolism*; D011233:Precipitin Tests; D060149:Tetraspanin 30
D015703:Antigens, CD; D018845:CD11 Antigens; D018821:CD18 Antigens; C554586:CD63 protein, human; D003902:Detergents; D010980:Platelet Membrane Glycoproteins; D060149:Tetraspanin 30