Platelet-derived growth factor (PDGF) rapidly stimulates binding of glycolytic enzymes to muscle cytoskeleton, prevented by calmodulin antagonists.

Platelet-derived growth factor (PDGF) rapidly stimulates binding of glycolytic enzymes to muscle cytoskeleton, prevented by calmodulin antagonists.
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血小板源性生长因子 (PDGF) 快速刺激糖酵解酶与肌肉细胞骨架的结合,而钙调蛋白拮抗剂可阻止这种结合。

DOI:
10.1006/bmmb.1994.1054
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发表时间:
1994
期刊:
Biochemical Medicine and Metabolic Biology
影响因子:
--
通讯作者:
R. Beitner
R. Beitner
中科院分区:
--
文献类型:
--
作者:
T. Livnat;M. Chen;R. Beitner

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已知糖酵解酶是通过与细胞骨架的可逆结合来控制的。我们之前的实验表明,胰岛素、表皮生长因子(EGF)和Ca2+诱导糖酵解酶与肌肉细胞骨架结合的快速和短暂刺激。我们在这里表明,血小板衍生生长因子(PDGF)发挥类似的作用。PDGF存在于大鼠膈肌中孵育,导致磷酸果糖激酶(EC 2.7.11)和醛缩酶(EC 4.1.2.13)与肌肉细胞骨架结合的快速和短暂刺激。钙调素拮抗剂三氟拉嗪或CGS 9343B(一种有效的选择性钙调素活性抑制剂)可以阻止PDGF诱导的细胞骨架结合糖酵解酶的增加,这强烈表明Ca(2+)-钙调素参与了PDGF的这种作用。同样,我们之前发现胰岛素、EGF或Ca2+对细胞骨架结合糖酵解酶的刺激也是钙调素介导的。目前和以往的研究结果表明,Ca(2+)-钙调素介导的细胞骨架结合糖酵解酶的快速增加可能是细胞中胰岛素、生长因子和其他Ca(2+)-动员激素信号转导的一般机制。加速的细胞骨架糖酵解将提供局部ATP,这是生长因子或激素与其受体结合后细胞骨架-膜快速重排所必需的。
Glycolytic enzymes are known to be controlled by reversible binding to cytoskeleton. Our previous experiments have shown that insulin, epidermal growth factor (EGF), and Ca2+ induce a rapid and transient stimulation of binding of glycolytic enzymes to muscle cytoskeleton. We show here that platelet-derived growth factor (PDGF) exerts a similar action. Incubation of rat diaphragm muscle in the presence of PDGF resulted in rapid and transient stimulation of binding of phosphofructokinase (EC 2.7.11) and aldolase (EC 4.1.2.13) to muscle cytoskeleton. The increase in cytoskeleton-bound glycolytic enzymes induced by PDGF was prevented by treatment with the calmodulin antagonists trifluoperazine or CGS 9343B (a potent and selective inhibitor of calmodulin activity), which strongly suggests that Ca(2+)-calmodulin is involved in this effect of PDGF. Similarly, we previously found that stimulation of cytoskeleton-bound glycolytic enzymes exerted by insulin, EGF, or Ca2+, was also calmodulin mediated. The present and previous results suggest that the rapid, Ca(2+)-calmodulin-mediated increase in cytoskeleton-bound glycolytic enzymes, may be a general mechanism in the cell, in signal transduction of insulin, growth factors, and other Ca(2+)-mobilizing hormones. The accelerated cytoskeletal glycolysis will provide local ATP, which is required for the rapid cytoskeletal-membrane rearrangements following binding of growth factor or hormone to its receptor.