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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

Activators of protein kinase C down-regulate and phosphorylate the T3/T-cell antigen receptor complex of human T lymphocytes.

As judged by indirect immunofluorescence, phorbol 12,13-dibutyrate and 1-oleoyl-2-acetylglycerol induced a rapid, concentration-dependent decrease of about 50% in the surface expression of the T3 antigen on human T lymphoblasts, and of T3 and the T-cell antigen receptor on HPB-ALL cells. Direct binding experiments using 125I-labeled antibody indicated that the reduction in T3 expression corresponded to a decrease in the number of antigen molecules rather than a change in their affinity. Biochemical analyses revealed that phorbol dibutyrate induced a rapid, prominent phosphorylation of the T3 Mr 26,000 gamma chain and to a lesser extent of the Mr 21,000 delta chain. No phosphorylation of the T3 epsilon chain or of the alpha and beta subunits of the T-cell antigen receptor was detected. The data suggest that protein kinase C induces a phosphorylation of the T3 gamma and delta chains that may lead to the down-regulation of the T3/T-cell antigen receptor complex.[1]

References

  1. Activators of protein kinase C down-regulate and phosphorylate the T3/T-cell antigen receptor complex of human T lymphocytes. Cantrell, D.A., Davies, A.A., Crumpton, M.J. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
 
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