Effect of polymyxin-B on T-lymphocyte protein synthesis.
The role of protein kinase-C (PK-C) protein phosphorylation on the mitogen triggered responses of T-lymphocytes was examined by observing the effect of polymyxin-B (an inhibitor of PK-C) on mitogen induced protein and DNA synthesis. Polymyxin-B inhibited 3H-thymidine incorporation by PHA activated T-lymphocytes over a range of PHA concentrations. 3H-leucine incorporation by PHA activated T-lymphocytes was inhibited by polymyxin-B in a dose dependent manner. A partially purified PK-C fraction from polymyxin-B treated PHA activated T-lymphocytes demonstrated less than 25% of the phosphorylating activity of untreated lymphocytes. These results suggest that protein synthesis during the T-lymphocyte activation process is dependent on PK-C activity.
D001798:Blood Proteins / Q000096:biosynthesis*; D004247:DNA / Q000096:biosynthesis; D006801:Humans; D007930:Leucine / Q000097:blood; D008213:Lymphocyte Activation / Q000187:drug effects; D010766:Phosphorylation; D010835:Phytohemagglutinins / Q000494:pharmacology; D011112:Polymyxin B / Q000494:pharmacology*; D011113:Polymyxins / Q000494:pharmacology*; D011493:Protein Kinase C / Q000097:blood; D013601:T-Lymphocytes / Q000187:drug effects / Q000378:metabolism*; D013936:Thymidine / Q000097:blood
D001798:Blood Proteins; D010835:Phytohemagglutinins; D011113:Polymyxins; D004247:DNA; D011493:Protein Kinase C; D007930:Leucine; D011112:Polymyxin B; D013936:Thymidine