Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:4.1.2.13 (aldolase)
 3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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.
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PMID:Platelet-derived growth factor (PDGF) rapidly stimulates binding of glycolytic enzymes to muscle cytoskeleton, prevented by calmodulin antagonists. 785 79

We report here on a novel mechanism involved in epidermal growth factor (EGF) action, which shows that EGF rapidly stimulates binding of the glycolytic enzymes, phosphofructokinase (EC 2.7.1.11), and aldolase (EC 4.1.2.13) to muscle cytoskeleton. This effect was demonstrated both in vivo, in the tibialis anterior muscle from rats injected with EGF, and in vitro, in the isolated rat diaphragm muscle incubated with EGF. The increase in cytoskeleton-bound glycolytic enzymes induced by EGF was prevented, in both the in vivo and in vitro experiments, by treatment with the calmodulin antagonists trifluoperazine or CGS 9343B (a potent and selective inhibitor of calmodulin activity), which strongly suggests that Ca2+ and calmodulin are involved in this effect of EGF. Our previous findings have revealed that insulin or Ca2+ exert a similar rapid stimulation of cytoskeletal glycolysis, which is also calmodulin mediated. We now hypothesize that this may be a general mechanism of signal transduction in the cell, involving Ca(2+)-mobilizing hormones and growth factors, and supplying local ATP, in the vicinity of cytoskeleton-membrane, which is required for the rapid cytoskeletal-membrane rearrangements upon membrane-induced events.
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PMID:Stimulatory effect of epidermal growth factor on binding of glycolytic enzymes to muscles cytoskeleton and the antagonistic action of calmodulin inhibitors. 837 34