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International Immunology, Vol 10, 1897-1905, Copyright © 1998 by Oxford University Press

ARTICLES

Binding of CD4 ligands induces tyrosine phosphorylation of phosphatidylinositol-3 kinase p110 subunit

F Mazerolles and A Fischer
INSERM U429, Hopital Necker-Enfants Malades, Paris, France.

We have previously reported that different putative CD4 ligands (anti- CD4 antibody, gp160 from HIV, synthetic peptides analogous to the residues 35-46 of HLA class II beta1 chain and residues 134-148 of HLA class II beta2 chain) down-regulate LFA-1-dependent adhesion between CD4+ T cells and HLA class II+ B cells, and also activate p56Ick and the phosphatidylinositol-3 kinase (PI3-kinase) associated with the CD4- p56Ick complex. It was demonstrated that the latter activation was dependent on the CD4-p56Ick association. Since these results suggest a relationship between p56Ick and PI3-kinase, we investigated whether PI3- kinase was tyrosine phosphorylated after CD4 binding and whether this phosphorylation was also dependent on the CD4-p56Ick association. We show herein that CD4 binding increased tyrosine phosphorylation of the catalytic subunit p110 of PI3-kinase but not of the p85 subunit. Association between p56Ick and PI3-kinase was constitutive, and was not modified after CD4 binding. In contrast, p110 tyrosine phosphorylation was inducible, transient and dependent on the CD4-p56Ick association. The role of the tyrosine phosphorylation of p110-PI3-kinase following ligand binding to CD4 is unknown. We speculate that this event could link the activation of p56Ick and of PI3-kinase after CD4 binding.
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