In vivo and in vitro phosphorylation of murine lymphocyte differentiation antigen CD5 |
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| Authors: | L C Griffith H Schulman M Tagawa |
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| Affiliation: | Department of Pharmacology, Stanford University School of Medicine, California 94305. |
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| Abstract: | Ly-1, the murine lymphocyte differentiation antigen CD5, is phosphorylated constitutively in vivo. This phosphorylation is enhanced by phorbol 12-myristate 13-acetate (PMA) treatment, but not by concanavalin A, Ca2+ ionophore or dibutyryl cAMP. Prolonged PMA treatment abolished PMA-induced Ly-1 phosphorylation but not constitutive phosphorylation, suggesting that protein kinase C (PKC) is responsible for this enhanced phosphorylation, but not the basal phosphorylation of Ly-1. Ly-1 is phosphorylated by PKC added to membranes, further supporting a role for protein kinase C in the in vivo phosphorylation of Ly-1. |
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