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Selective effects of TPA and IL-1 on protein phosphorylation in murine thymocytes
Authors:S Avissar  K H Stenzel  A Novogrodsky
Affiliation:1. The Rogoff-Wellcome Medical Research Institute, Beilinson Medical Center, Petah-Tikva 49100, Israel;2. Tel-Aviv University Sackler School of Medicine, Tel-Aviv, Israel;1. State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu 214122, China;2. International Joint Research Laboratory for Biointerface and Biodetection, and School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China;3. PetroChina Research Institute of Petroleum Exploration & Development, Beijing 10083, China;4. Key Laboratory of Oilfield Chemicals, CNPC, Beijing 10083, China;1. School of Food Science and Technology, Shihezi University, Shihezi, Xinjiang 832003, China;2. College of Animal Science and Technology, Shihezi University, Shihezi, China;3. Key Laboratory of Agricultural Product Processing and Quality Control of Specialty(Co-construction by Ministry and Province), School of Food Science and Technology, Shihezi University, Shihezi, China;4. Key Laboratory for Food Nutrition and Safety Control of Xinjiang Production and Construction Corps,School of Food Science and Technology, Shihezi University, Shihezi, China;1. State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, Jiangsu, 214122, PR China;2. International Joint Research Laboratory for Biointerface and Biodetection, and School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu, 214122, PR China;3. Wuxi Food Safety Inspection and Test Center, 35-210 South Changjiang Road, Wuxi, Jiangsu Province, 214142, PR China
Abstract:Protein kinase C activity was demonstrated in murine thymocytes and the effects of TPA and IL-1 on this enzyme were studied. TPA, but not IL-1, could substitute for diacylglycerol in protein kinase C activation. Although TPA and IL-1 are both potent comitogens for murine thymocytes they markedly differ in their effects on protein phosphorylation and protein kinase C activation. Treatment of intact thymocytes with TPA resulted in a marked increase in the phosphorylation of an endogenous protein with Mr approximately 44,000. Enhanced phosphorylation of this protein was also observed when protein kinase C was activated in thymocyte extracts. In contrast to TPA, IL-1 neither induced phosphorylation of the 44,000-Da protein nor activated protein kinase C. The data suggests that protein kinase C does not mediate the comitogenic effect of IL-1 in murine thymocytes.
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