EurekaMag.com logo
+ Translate

Regulation of glycogen phosphorylase and glycogen synthase ec 2.4.1.11 by adrenaline in soleus muscle of phosphorylase kinase ec 2.7.1.38 deficient mice


, : Regulation of glycogen phosphorylase and glycogen synthase ec 2.4.1.11 by adrenaline in soleus muscle of phosphorylase kinase ec 2.7.1.38 deficient mice. European Journal of Biochemistry 115(3): 619-626

Mixed skeletal muscles of ICR/IAn mice contain 0.2% of the phosphorylase kinase activity found in C3H/He-mg mice at pH 8.2 in the presence of Ca2+. This lack of activity is caused by the absence of the normal phosphorylase kinase protein. The trace residual activity in ICR/IAn mice has quite different properties from the normal enzyme. It has a much higher activity ratio (pH 6.8/8.2), its activity is less dependent on Ca2+, and it is not activated by cAMP-dependent protein kinase or by trypsin. Its elution behavior on Sepharose 4B differs from the normal enzyme. A consequence of the higher activity ratio (pH 6.8/8.2) and decreased effect of Ca2+ is that mixed skeletal muscles of ICR/IAn mice contain 7% of normal activity at pH 6.8 in the absence of Ca2+. The activity of phosphorylase kinase in C3H/He-mg control mice is 6-fold lower in red oxidative (soleus) muscle and 15-fold lower in cardiac muscle than in mixed skeletal muscle. The trace residual activity in ICR/IAn mice is present at the same level in soleus muscle, cardiac muscle and mixed skeletal muscle. Soleus muscles of ICR/IAn mice contain 1.5% of normal activity at pH 8.2 in the presence of Ca2+ and 30% of normal activity at pH 6.8 in the absence of Ca2+. Cardiac muscle contains 6% of normal activity at pH 8.2 in the presence of Ca2+ and 60% of normal activity at pH 6.8 in the absence of Ca2+. When isolated soleus muscles were incubated with adrenaline [epinephrine], the level of phosphorylase a in ICR/IAn mice rose from 2.8% in the absence of the hormone to 5.7% in the presence of the hormone. The level of phosphorylase a in normal mice varied from 2.4-11.1% in the absence of adrenaline and increased to 17.7-23.9% in the presence of the hormone. The trace phosphorylase kinase activity in ICR/IAn mice apparently is capable of phosphorylating phosphorylase b in vivo. This enzyme apparently is responsible for the very low level of phosphorylase a in resting soleus muscle or ICR/IAn mice and perhaps even in normal mice. Since the residual enzyme cannot be activated by cAMP-dependent protein kinase, the elevation of phosphorylase a by adrenaline may be caused by an inhibition of phosphorylase phosphatase. The possibility that this occurs through the activation of protein phosphatase inhibitor 1 by cAMP-dependent protein kinase is discussed. Incubation of soleus muscles with adrenaline decreased the activity ratio (.+-. glucose 6-phosphate) of glycogen synthase from 0.24-0.08 in ICR/IAn mice and 0.31-0.14 in C3H/He-mg or Swiss albino mice. The inactivation of glycogen synthase by adrenaline in resting soleus muscle apparently does not result from the activation of phosphorylase kinase by cAMP-dependent protein kinase. It is most likely mediated by a direct phosphorylation catalyzed by cAMP-dependent protein kinase, although the activation of protein phosphatase inhibitor 1 may contribute to the effect.

(PDF 0-2 workdays service)

Accession: 006288172

Submit PDF Full Text: Here


Submit PDF Full Text

No spam - Every submission is manually reviewed

Due to poor quality, we do not accept files from Researchgate

Submitted PDF Full Texts will always be free for everyone
(We only charge for PDFs that we need to acquire)

Select a PDF file:
Close
Close

Related references

Cohen, P.T.; L.M.rchand Brustel, Y.; Cohen, P., 1981: Regulation of glycogen phosphorylase and glycogen synthase by adrenalin in soleus muscle of phosphorylase-kinase-deficient mice. European Journal of Biochemistry 115(3): 619-625

Franch, J.; Aslesen, R.; Jensen, J., 1999: Regulation of glycogen synthesis in rat skeletal muscle after glycogen-depleting contractile activity: effects of adrenaline on glycogen synthesis and activation of glycogen synthase and glycogen phosphorylase. We investigated the effects of insulin and adrenaline on the rate of glycogen synthesis in skeletal muscles after electrical stimulation in vitro. The contractile activity decreased the glycogen concentration by 62%. After contractile activity, th...

Jensen, J.; Aslesen, R.; Jebens, E.; Skrondal, A., 1999: Adrenaline-mediated glycogen phosphorylase activation is enhanced in rat soleus muscle with increased glycogen content. The effect of glycogen content on the activation of glycogen phosphorylase during adrenaline stimulation was investigated in soleus muscles from Wistar rats. Furthermore, adrenergic activation of glycogen phosphorylase in the slow-twitch oxidative...

Huang, K.P.; Singh, T.J.; Akatsuka, A.; Shapiro, S.G.; Vandenheede, J.R.; Merlevede, W., 1984: Phosphorylation and inactivation of rabbit skeletal muscle glycogen synthase: distinction between kinase Fa-, phosphorylase kinase-, and glycogen synthase (casein) kinase-1-catalyzed reactions. Rabbit skeletal muscle glycogen synthase was phosphorylated by kinase Fa, phosphorylase kinase, and cAMP-independent synthase (casein) kinase-1 to determine the differences among these kinase-catalyzed reactions. The stoichiometry of phosphate inc...

Strickland W.G.; Imazu M.; Chrisman T.D.; Exton J.E., 1983: Regulation of rat liver glycogen synthase roles of calcium phosphorylase kinase and phosphorylase a. MgATP slowed the rate of glycogen synthase activation by glucose in Sephadex filtrates of liver extracts from normal rats. The effect was diminished by ethylene glycol bis(.beta.-aminoethyl ether)-N,N,N',N'-tetraacetic acid (EGTA) and re...

Strickland, W.G.; Imazu, M.; Chrisman, T.D.; Exton, J.H., 1983: Regulation of rat liver glycogen synthase. Roles of Ca2+, phosphorylase kinase, and phosphorylase a. Journal of Biological Chemistry 258(9): 5490-5497

Sambandam, T.; Gunasekaran, M., 1987: Interaction of glycogen phosphorylase, glycogen synthase and phosphorylase kinase in Phymatotrichum omnivorum. Phosphorylation appeared to be active in the early stages of growth of the cotton root disease pathogen [Phymatotrichopsis omnivora]. The release of glucose from glycogen breakdown may inactivate phosphorylase, but with higher levels of kinase act...

Depaoli-Roach, A.A.; Roach, P.J.; Larner, J., 1979: Rabbit skeletal muscle phosphorylase kinase ec 2.7.1.38 comparison of glycogen synthase ec 2.4.1.11 and phosphorylase ec 2.4.1.1 as substrates. The Ca2+-stimulated phosphorylation of rabbit muscle glycogen synthase (EC 2.4.1.11) catalyzed by phosphorylase kinase (EC 2.7.1.38) was characterized and compared with the reaction involving phosphorylase (EC 2.4.1.1). By comparing reaction rates...

DePaoli-Roach, A.A.; Roach, P.J.; Larner, J., 1979: Rabbit skeletal muscle phosphorylase kinase. Comparison of glycogen synthase and phosphorylase as substrates. Journal of Biological Chemistry 254(10): 4212-4219

L.M.rchand-Brustel, Y.; Cohen, P.T.; Cohen, P., 1979: Insulin activates glycogen synthase in phosphorylase kinase deficient mice. Febs Letters 105(2): 235-238