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Effects of microfilamentous depolymerization by cytochalasin B on cAMP-PKA pathway

机译:细胞松弛素B微丝解聚对cAMP-PKA通路的影响

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摘要

Diacylglycerol (DG) and cAMP, two intracellular second messengers, play important roles in responding to the stimulation of extracellular signal. DG activates protein kinase C (PKC), and cAMP activates protein kinase A (PKA). Activation of these kinases leads to a cascade of phosphorylation of many targets, which regulates the proliferation, differentiation and other physiological functions of cells. We found that cytochalasin B (CB) can not only destroy microfilament (MF), but also stimulate the activity of DG-PKC pathway. It was reported that at early stage from G_0 to S phase, activation of cAMP-PKA pathway promotes the proliferation of hepatocytes. The two pathways may couple in a chain reaction by the action of PKC. Activation of cAMP-PKA pathway is mediated by phosphorylation of G_i protein by PKC. There is still no report about whether reorganization of MF has effects on activation of cAMP-PKA pathway. We have, therefore, directed our efforts towards studying the effects of reorganization of MF by CB on activation of cAMP-PKA pathway at the early stage in the transition from G_0 to S phase.
机译:二酰基甘油(DG)和cAMP,两个细胞内第二信使,在响应细胞外信号的刺激中起重要作用。 DG激活蛋白激酶C(PKC),而cAMP激活蛋白激酶A(PKA)。这些激酶的激活导致许多靶标的磷酸化级联,从而调节细胞的增殖,分化和其他生理功能。我们发现细胞松弛素B(CB)不仅可以破坏微丝(MF),而且可以刺激DG-PKC通路的活性。据报道,在从G_0到S期的早期,cAMP-PKA途径的激活促进肝细胞的增殖。这两个途径可以通过PKC的作用偶联成链反应。 cAMP-PKA途径的激活由PKC磷酸化G_i蛋白介导。尚无关于MF重组是否对cAMP-PKA途径活化有影响的报道。因此,我们致力于研究由CB进行的MF重组对从G_0到S期过渡的早期对cAMP-PKA途径活化的影响。

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