Protein kinase C in cytosol and cell membranes of concanavalin A-stimulated rat thymocytes.
In concanavalin A-treated thymus cells and phytohemagglutinin-treated spleen cells, the distribution of protein kinase C is changed. Shortly after addition of plant lectins, the activity of protein kinase C increased in the cytosol and decreased in the particulate fraction. 2 h later, the activity of protein kinase C decreased in the cytosol and increased in the particulate fraction. Membrane binding of protein kinase C and tion of DNA synthesis showed the same dependency on concanavalin A concentration. A long-term membrane binding of protein kinase C seems to be essential for lymphocyte stimulation.
D000818:Animals; D002453:Cell Cycle; D002462:Cell Membrane / Q000201:enzymology; D003208:Concanavalin A / Q000494:pharmacology; D003600:Cytosol / Q000201:enzymology; D008213:Lymphocyte Activation; D008214:Lymphocytes / Q000166:cytology / Q000201:enzymology*; D010042:Ouabain / Q000494:pharmacology; D011493:Protein Kinase C / Q000378:metabolism*; D011691:Puromycin / Q000494:pharmacology; D051381:Rats; D013154:Spleen / Q000166:cytology; D013950:Thymus Gland / Q000166:cytology
D003208:Concanavalin A; D011691:Puromycin; D010042:Ouabain; D011493:Protein Kinase C