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首页> 外文期刊>Biochimica et biophysica acta. Biomembranes >Differential signal transduction pathways regulating interleukin-2 synthesis and interleukin-2 receptor expression in stimulated human lymphocytes
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Differential signal transduction pathways regulating interleukin-2 synthesis and interleukin-2 receptor expression in stimulated human lymphocytes

机译：调节人淋巴细胞中白介素2合成和白介素2受体表达的差异信号转导途径

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In human peripheral blood lymphocytes stimulated via the T-cell antigen receptor/CD3 complex IL-2 synthesis and cellular proliferation were effectively inhibited by a concentration of ouabain as low as 50 nM, whilst the expression of high affinity IL-2 receptors was not influenced. Binding of the monoclonal antibody, BMA 031 to the T-cell antigen receptor/CD3 complex resulted in a bimodal activation of protein kinase C. The activation of protein kinase C-α in the early phase of T-lymphocyte activation was not affected by 50 nM ouabain, in contrast sustained activation of protein kinase C-β, between 90–240 min of stimulation was completely abolished by the cardiac glycoside. When protein kinase C was directly activated by PMA + ionomycin, 50 nM ouabain was ineffective in inhibiting protein kinase C activation, as well as subsequent IL-2 synthesis, suggesting that the glycoside interfered with signal transducing mechanism(s) upstream of the activation of protein kinase C. Ouabain had no influence on the elevation of intracellular calcium concentration in BMA 031 stimulated lymphocytes, ruling out the possibility that it interfered with the T-cell antigen receptor dependent phosphatidylinositol response. In contrast, lysophosphatide acyltransferase catalysed elevated incorporation of polyunsaturated fatty acids was effectively inhibited by low concentrations of ouabain in BMA 031-stimulated T-lymphocytes, whereas stimulation with PMA + ionomycin had no influence on the plasma membrane phospholipid fatty acid metabolism. These results suggest, that differential signal transduction pathways are involved in the activation of protein kinases C-α and -β. They implicate that elevated incorporation of polyunsaturated fatty acids into plasma membrane phospholipids might contribute to sustained activation of protein kinase C-β, and establish a link between activation of protein kinase C-β and induction of IL-2 synthesis in human lymphocytes.
机译：在人外周血中，通过T细胞抗原受体/ CD3复合物刺激的淋巴细胞，其哇巴因浓度低至50 nM，IL-2的合成和细胞增殖受到有效抑制，而高亲和力IL-2受体的表达不受影响。单克隆抗体BMA 031与T细胞抗原受体/ CD3复合物的结合导致蛋白激酶C的双峰激活。T淋巴细胞激活早期蛋白激酶C-α的激活不受50的影响相反，nM ouabain蛋白激酶C-β持续活化，强心苷完全消除了90-240分钟之间的刺激。当PMA +离子霉素直接激活蛋白激酶C时，50 nM哇巴因不能有效抑制蛋白激酶C的激活以及随后的IL-2合成，这表明糖苷干扰了蛋白激酶C激活上游的信号转导机制。蛋白激酶C. Ouabain对BMA 031刺激的淋巴细胞内细胞内钙浓度的升高没有影响，排除了它干扰T细胞抗原受体依赖性磷脂酰肌醇反应的可能性。相比之下，BMA 031刺激的T淋巴细胞中低浓度的哇巴因有效抑制了溶血磷脂酰基转移酶催化的多不饱和脂肪酸的高掺入，而PMA +离子霉素的刺激对质膜磷脂脂肪酸代谢没有影响。这些结果表明，差异信号转导途径与蛋白激酶C-α和-β的活化有关。他们暗示多不饱和脂肪酸向质膜磷脂中掺入的增加可能有助于蛋白激酶C-β的持续活化，并在蛋白激酶C-β的活化与人淋巴细胞中IL-2合成的诱导之间建立联系。

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