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PubMed1980

The role of calcium in alpha-adrenergic inactivation of glycogen synthase in rat hepatocytes and its inhibition by insulin.

The effects of epinephrine, vasopressin, and A23187 on glycogen synthase and phosphorylase were examined in isolated rat liver parenchymal cells from fed animals. In normal calcium-containing hepatocytes, epinephrine, vasopressin, and A23187 were more potent at inactivating glycogen synthase, previously activated with 30 mM glucose, than at activating phosphorylase. In calcium-depleted hepatocytes (cells washed and incubated with 1 mM EGTA), the effect of epinephrine on both enzyme activities was impaired, while the effects of vasopressin and A23187 were completely abolished. Insulin was more effective at inhibiting the effects of epinephrine in calcium-depleted cells, but it was without effect on vasopressin and A23187 actions. The ability of epinephrine, vasopressin, and A23187 to elicit calcium efflux from cells was not altered by the presence of 30 mM glucose. These findings are consistent with the idea that the alpha-adrenergic inactivation of liver glycogen synthase may be a result of the increased stimulation of a calcium-dependent protein kinase, possibly phosphorylase b kinase.

Animals↗

PubMed1975

On the mechanism of the glycogenolytic effect of dinitrophenol. Activity of phosphofructokinase in perfused hearts.

To explain the mechanism of DNP action the contents of ATP, ADP, AMP and G-6-P were determined in perfused rat hearts in a period of time in which the rate of the glycogenolysis was increased. The levels of these metabolytes in the extract were consistent with an increase of the phosphofructokinase activity. On the other hand, the finding of higher activity of phosphyrylase beta kinase in DNP-poisoned animals could be explained as due to the low content of G-6-P in the perfused hearts subjected to the action of the drug.

Adenine Nucleotides↗

PubMed1986

Interaction of immobilized phosphofructokinase with soluble muscle proteins.

Selected glycolytic enzymes (including phosphoglucose isomerase, aldolase, glyceraldehyde phosphate dehydrogenase, enolase, pyruvate kinase and lactate dehydrogenase), as well as glycogen phosphorylase, creatine kinase, and adenylate kinase, bound to phosphofructokinase immobilized on an agarose gel. The affinity of phosphofructokinase to these various proteins differed, with phosphorylase exhibiting the strongest binding. Binding was reversed either by: (1) elution with high-ionic-strength buffer (0.4 M KCl); (2) the addition of a 5-10 mM concentration of ATP; or (3) high concentrations of fructose 6-phosphate (5 mM).

Animals↗

PubMed1977

[The role of 3',5'-AMP in regulation of activity of histidase from rat liver and skin].

A dependence of activity of histidase from rat liver and skin on the agents affecting the activity of the adenylate cyclase systeme was studied in vitro. Under conditions optimal for the activity of liver phosphorylase protein kinase the skin extract histidase was activated 2-3-fold. This is indicative of a possibility of regulation of the skin histidase activity via the adenylate cyclase system by modification of enzyme by phosphorylation-dephosphorylation, which is performed by 3':5'-AMP-dependent protein kinase. Theophylline at concentrations of 10(-4) M and 10(-3) M activates partially purified histidase (both liver and skin forms), probably in the course of direct interaction with the enzyme.

Adenylyl Cyclases↗

PubMed1979

Activation of AMP aminohydrolase during skeletal-muscle contraction.

AMP aminohydrolase activity is enhanced by 60% after 5 s tetanic stimulation of phosphorylase kinase-deficient mouse muscle and after 60 s tetanus in normal mice. During the recovery from tetanus the activity in the contralateral leg is similarly enhanced. The activation is stable to 1000-fold dilution and has a half-life of approx. 1 h.

AMP Deaminase↗

PubMed1973

A phosphorylated light-chain component of myosin from skeletal muscle.

1. The low-molecular-weight components of myosin from rabbit skeletal muscle migrated as four bands on polyacrylamide-gel electrophoresis in 8m-urea but only as three in systems containing sodium dodecyl sulphate. The two bands of intermediate mobility in 8m-urea (Ml(2) and Ml(3)) had identical mobilities in sodium dodecyl sulphate. 2. The isolation of pure samples of all four low-molecular-weight components by DEAE-Sephadex chromatography is described. 3. The amino acid compositions of components Ml(2) and Ml(3) were identical. Further analyses showed the presence of 1 mol of phosphate/18500g of component Ml(2) and less than 10% of this amount in component Ml(3). Neither light component contained ribose. 4. Alkaline phosphatase from Escherichia coli converted component Ml(2) into Ml(3). Incubation with crude preparations of phosphorylase b kinase or protein kinase in the presence of ATP converted component Ml(3) into Ml(2). 5. Phosphorylation of component Ml(3) with the kinases isolated from skeletal muscle and [gamma-(32)P]ATP gave incorporation of (32)P only into component Ml(2) whether whole myosin or separated low-molecular-weight components were used. 6. High-voltage electrophoresis at pH6.5 and pH1.8 of a chymotryptic digest of (32)P-labelled component Ml(2) yielded one major radioactive peptide containing serine phosphate. 7. The amino acid sequence of this peptide was shown to be: Arg-Ala-Ala-Ala-Glu-Gly-Gly-(Ser,Ser(P))-Asn-Val-Phe. This sequence shows no obvious similarity to the site phosphorylated in the conversion of phosphorylase b into phosphorylase a by phosphorylase b kinase. 8. Evidence suggests that in vivo all the 18500-molecular-weight light chain is in the phosphorylated form. The extent of dephosphorylation that occurred during myosin extraction depended on the conditions employed.

Alkaline Phosphatase↗

PubMed1984

Effects of adrenalectomy on activation of glycogen phosphorylase in rat myocardium.

Adrenalectomy causes a depressed glycogenolytic response to catecholamines in myocardium. Total phosphorylase activity (a + b) is 20% lower in isolated, perfused hearts from adrenalectomized (ADX) rats compared with hearts from sham-operated (sham) rats even though the basal activity ratios (-AMP/+AMP) do not differ. In response to epinephrine (50 nM), the sham group has a higher activity ratio than the ADX group (0.23 vs. 0.16); the difference in specific activities of phosphorylase a in the two groups is even greater, 87 versus 49 U/mg protein. The glycogen content of the heart is 30% lower in the ADX group. Adrenalectomy does not alter the accumulation of cAMP and activation of cAMP-dependent protein kinase caused by epinephrine. Although rat heart contains a heat-stable phosphatase inhibitor, the activity of this inhibitor, as judged by phosphorylase phosphatase activity, is not altered by epinephrine stimulation or by adrenalectomy. Epinephrine perfusion increases the activity ratios (pH 6.8:8.2) of phosphorylase kinase equally in sham and ADX hearts; however, the specific activities of phosphorylase kinase (basal and hormone-stimulated) at either pH are lower after adrenalectomy. The sensitivity of phosphorylase kinase activity to stimulation by calcium is the same in the sham and ADX groups. A radioimmunoassay for phosphorylase kinase detects 10% less of this enzyme in hearts from adrenalectomized animals. Specific activities at pH 6.8 and 8.2 based on the quantity of phosphorylase kinase detected by radioimmunoassay suggest a lower phosphorylation state in the ADX group. Decreases in quantities of phosphorylase and phosphorylase kinase and enzyme dissociation due to glycogen depletion could all contribute to a depressed glycogenolytic response in the ADX group.

Adrenal Glands↗

PubMed1982

Reconstitution of a Mg-ATP-dependent protein phosphatase and its activation through a phosphorylation mechanism.

A Mg-ATP-dependent protein phosphatase has been reconstituted from the catalytic subunit of protein phosphatase-1 and inhibitor-2, and consists of a 1:1 complex between these proteins. Activation of this enzyme by glycogen synthase kinase-3 and Mg-ATP results from the phosphorylation of inhibitor-2 on a threonine residue(s) and is accompanied by the dissociation of the complex. The results prove that protein phosphatase-1 and the Mg-ATP-dependent protein phosphatase contain the same catalytic subunit, and that they are interconvertible forms of the same enzyme.

Adenosine Triphosphate↗

PubMedDate not supplied

[The characteristics of the interaction of glycogenolytic enzymes with glycogen in endothermic and ectothermic animals].

It has been shown that the dependence of glycogenphosphorylase kinase activity on the quantity of glycogen added corresponds to the glycogenphosphorylase saturation curve by glycogen obtained during investigation of complex formation with the muscle glycogenphosphorylase of the animals: rat, frog Rana temporaria and fish Raja clavata under identical conditions. We suggest that glycogenolytic enzymes organize regular structure on glycogen particle. Glycogenphosphorylases of heat-loving animals have high affinity to glycogen that is accounted for necessity to keep the structure in natural conditions.

Adenosine Triphosphate↗

PubMed1982

Detection of glycogen in a glycogen storage disease by 13C nuclear magnetic resonance.

The livers of gsd/gsd rats homozygous for the glycogen storage disease phosphorylase b kinase deficiency were observed by 13C NMR using a surface coil. Clear signals were detected from glycogen. The concentration of glycogen as determined by NMR was approximately 3-times that found in normal strains agreeing well with chemical determinations. Starvation did not significantly reduce the glycogen content of the livers with glycogen storage disease whereas it reduced the signal below detectability in normal rats. Difference spectra of starved normal rats from fed gsd/gsd rats gave spectra similar in appearance to that of purified glycogen. Glycogen both in vivo and in vitro is fully visible using 13C NMR.

Animals↗

PubMed1982

Blood glucose of mother and fetus late pregnancy of rats with glycogen storage disorder.

The gsd/gsd rat is unable to mobilize liver glycogen due to an absence of phosphorylase b kinase activity. Unlike the normal rat, the maternal gsd/gsd rat cannot maintain its blood glucose concentration in late pregnancy, and values of 3.25 +/- 0.22 mM were found just before birth. The blood glucose of the gsd/gsd fetus falls to 1.76 +/- 0.09 mM at day 19 of gestation and does not rise appreciably again before birth. In contrast, normal fetal rats show a steady rise in blood glucose from hypoglycemic levels at day 19 to a value of 5.70 +/- 0.12 mM on the day of birth. These results indicate that the normal fetal rat contributes towards the regulation of its own glucose in late gestation by utilizing its liver glycogen stores.

Animals↗

PubMed1990

[Activities of enzymes converting 5-fluorouracil to 5-fluorouridine-5' monophosphate and 5-fluorodeoxyuridine-5' monophosphate in subcultured cell lines and solid tumor tissues].

The activities of five enzymes, orotate phosphoribosyltransferase (OPRTase), uridine kinase (UR kinase), thymidine kinase (TdR kinase), uridine phosphorylase (UR Prylase) and thymidine phosphorylase (TdR Prylase), were examined in subcultured human acute leukemia cell lines (HL-60, CCRF-CEM), subcultured human solid tumor cell lines (Colo-205, HeLa-S3) and human cancerous tissues with a view to compare the activation of 5-fluorouracil in them. There was no significant difference in the activity of any enzyme between HL-60 and CCRF-CEM, Colo-205 and HeLa-S3, and human lung cancerous tissue and human colon cancerous tissue. Compared between the acute leukemia cell lines and the solid tumor cell lines, the UR kinase activity was high in both cell lines. The OPRTase and UR Prylase activities were low in the solid tumor cell lines. In the cancerous tissues, both the UR kinase and TdR kinase activities were low, but the UR Prylase and TdR Prylase activities were markedly high. The results suggest that the intracellular activation of 5-fluorouracil varies with different human cancerous cells. When the anti-cancer activity of 5-fluorouracil is tested in vitro, the difference of fluoropyrimidine metabolism in subcultured cell lines from that in the cancerous tissue should be taken in account.

Fluorouracil↗

PubMed1991