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Control glycogen synthesis

Regulation of glycogen phosphorylase in muscle is accomplished by many of the same enzymes that control glycogen synthesis. Phosphorylase kinase converts the dimeric phosphorylase from the inactive to the active form by Mg + and ATP-dependent phosphorylation of two identical serine residues. The principal enzyme that removes this phosphate may be protein phosphatase-1 (phosphorylase phosphatase). [Pg.288]

Glycogen phosphorylase isoenzymes have been isolated from liver, brain and skeletal muscle. All forms are subject to covalent control with conversion of the inactive forms (GP-b) to the active forms (GP-a) by phosphorylation on specific serine residues. This phosphorylation step, mediated by the enzyme phosphorylase kinase, is initiated by glucagon stimulation of the hepatocyte. Indeed, the same cAMP cascade which inhibits glycogen synthesis simultaneously stimulates glycogenolysis, giving us an excellent example of reciprocal control. [Pg.213]

Glucagon stimulation of liver cells in particular leads to phosphorylation of regulatory enzymes whereas insulin has the opposite effect. So, after a meal, we would expect glycolysis and glycogen synthesis to operate very efficiently so the control enzymes will be dephosphorylated. [Pg.320]

FIGURE 15-36 Control of glycogen synthesis from blood glucose in myocytes. Insulin affects three of the five steps in this pathway, but it is the effects on transport and hexokinase activity, not the change in glycogen synthase activity, that increase the flux toward glycogen. [Pg.596]

Alston, S., Hampson, L., Gomez-Foix, A.M., Gninovart, J.J., Aglus, L. (2001) Hepatic glycogen synthesis is highly sensitive to phosphorylase activity evidence from metabolic control analysis. J. Biol. Chem. 276, 23,858-23,866. [Pg.598]

Shulinan, R.G., Block, G., Rothman, D.L. (1995) In vivo regulation of muscle glycogen synthase and the control of glycogen synthesis. Proc. Natl. Acad. Sci. USA 92, 8535-8542. [Pg.598]

Review of the use of NMR to measure metabolite concentrations during glycogen synthesis, interpreted by metabolic control analysis. [Pg.598]

In a placebo-controlled study in six patients with type 2 diabetes mellitus thalidomide 150 mg/day for 3 weeks reduced insulin-stimulated glucose uptake by 31% and glycogen synthesis by 48% (1115). However, it had no effect on rates of glycolysis, carbohydrate oxidation, non-oxidative glycolysis, lipolysis, free fatty acid oxidation, or re-esterification. The authors concluded that thalidomide increases insulin resistance in obese patients with type 2 diabetes. [Pg.651]

Glycogen degradation and glycogen synthesis are controlled both by allosteric regulation and by hormonal control. [Pg.305]

Fig. 4. Dual control of glycogen degradation and glycogen synthesis by protein kinase A. Fig. 4. Dual control of glycogen degradation and glycogen synthesis by protein kinase A.
Phosphorylation or glycosylation may be used to activate Rapid or deactivate an enzyme. In the response to insulin, the phosphorylation of multiple enzymes, including glycogen synthase, helps control the synthesis or degradation of glycogen and allows the ceU to respond to changes in blood sugar. [Pg.157]


See other pages where Control glycogen synthesis is mentioned: [Pg.704]    [Pg.765]    [Pg.403]    [Pg.345]    [Pg.704]    [Pg.765]    [Pg.403]    [Pg.345]    [Pg.111]    [Pg.137]    [Pg.150]    [Pg.190]    [Pg.161]    [Pg.65]    [Pg.195]    [Pg.223]    [Pg.148]    [Pg.93]    [Pg.110]    [Pg.120]    [Pg.230]    [Pg.129]    [Pg.1667]    [Pg.288]    [Pg.309]    [Pg.194]    [Pg.145]    [Pg.242]    [Pg.329]    [Pg.329]    [Pg.55]    [Pg.131]    [Pg.127]    [Pg.2032]    [Pg.864]    [Pg.883]    [Pg.883]    [Pg.885]    [Pg.1253]    [Pg.23]   
See also in sourсe #XX -- [ Pg.33 , Pg.329 ]




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