title: In vivo and in vitro phosphorylation of murine lymphocyte differentiation antigen CD5.
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.
authors: Department of Pharmacology, Stanford University School of Medicine, California 94305.
authors: L C
authors: LC
authors: Griffith
authors: H
authors: H
authors: Schulman
authors: M
authors: M
authors: Tagawa
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000943:Antigens, Differentiation / Q000378:metabolism*; D000950:Antigens, Ly / Q000378:metabolism; D018956:CD5 Antigens; D007739:L Cells / Q000378:metabolism; D008214:Lymphocytes / Q000378:metabolism*; D051379:Mice; D008807:Mice, Inbred BALB C; D010750:Phosphoproteins / Q000032:analysis; D010766:Phosphorylation; D011493:Protein Kinase C / Q000502:physiology; D051381:Rats
chemical_list: D000596:Amino Acids; D000943:Antigens, Differentiation; D000950:Antigens, Ly; D018956:CD5 Antigens; D010750:Phosphoproteins; D011493:Protein Kinase C