Regulation of fat body glycogen phosphorylase activity during refeeding inManduca sexta larvae

1992 ◽  
Vol 19 (4) ◽  
pp. 225-235 ◽  
Author(s):  
Karl J. Siegert ◽  
William Mordue
Keyword(s):  
Glycogen Phosphorylase ◽  
Fat Body ◽  
Phosphorylase Activity ◽  
Glycogen Phosphorylase Activity

scholarly journals Regulation of locust fat-body phosphorylase

1973 ◽  
Vol 135 (1) ◽  
pp. 37-41 ◽  
Author(s):  
S. W. Applebaum ◽  
H. M. Schlesinger
Keyword(s):  
Glycogen Phosphorylase ◽  
Fat Body ◽  
Competitive Inhibitor ◽  
Differential Centrifugation ◽  
Phosphorylase Activity ◽  
Optimum Activity ◽  
Ph Values ◽  
Glycogen Phosphorylase Activity ◽  
Glycogen Particles

1. Glycogen phosphorylase of locust fat-body was partially purified by differential centrifugation and dissociation from glycogen particles at two pH values. 2. Optimum activity was obtained at pH6.6–6.7. 3. The calculated apparent Km values for glycogen and glucose 1-phosphate were 0.08% and 10–13mm respectively. 4. 5′-AMP activated in the range 5μm–1mm. 5. Glucose 6-phosphate is a competitive inhibitor for the substrate glucose 1-phosphate (Ki=1.7mm). 5′-AMP abolishes this inhibition. Glucose weakly inhibits (Ki=25–30mm), but trehalose does not inhibit even at 100mm. 6. It is suggested that glucose 6-phosphate is a major regulator of glycogen phosphorylase activity in locust fat-body.

Glycogen Phosphorylase in the Fat Body of Two Cockroach Species, Periplaneta americana and Nauphoeta cinerea: Isolation, Partial Characterization of Three Forms and Activation by Hypertrehalosaemic Hormones

1991 ◽  
Vol 46 (1-2) ◽  
pp. 149-162 ◽  
Author(s):  
Gerd Gäde
Keyword(s):  
Anion Exchange ◽  
Glycogen Phosphorylase ◽  
Periplaneta Americana ◽  
Fat Body ◽  
Phosphorylase Kinase ◽  
Phosphorylase Activity ◽  
Strong Inhibitor ◽  
Nauphoeta Cinerea ◽  
Crude Extracts ◽  
Fat Bodies

The presence of endogenous phosphorylase kinase and phosphorylase phosphatase in crude extracts of fat bodies from the cockroaches Nauphoeta cinerea and Periplaneta americana is demonstrated in vitro by activation/inactivation of glycogen phosphorylase under appropriate conditions. Fractionation of fat body extracts of both cockroach species on an anion-exchange medium results in the elution of three peaks with phosphorylase activity. According to their AMP dependency these activity peaks are designated as phosphorylase b (inactive without AMP), phosphorylase ab (active without AMP, but several stimulated with AMP) and phosphorylase a (active without AMP). It is shown chromatographically that incubating crude extracts of fat bodies from both cockroaches, under conditions where the phosphorylase kinase is active, results in all phosphorylase b being converted to the ab- or a-form , whereas under conditions where the phosphorylase phosphatase is active all phophorylase a is converted to the ab- or b-form . Endogenous phosphorylase kinase of N. cinerea crude fat body extract can convert vertebrate phosphorylase b into the a-form , and, conversely, vertebrate muscle p hosphorylase kinase and phosphorylase phosphatase, respectively, are able to convert partially purified N. cinerea phosphorylase aborb and the ab- und a-form , respectively. In resting cockroaches most of the phosphorylase activity resides in the b-form and only a small fraction (10% ) in the a-form , whereas between 26% (N . cinerea) and 35% (P. americana) occurs in the ab-form . Injection of endogenous hypertrehalosaemic peptides into N. cinerea (the decapeptide Bld-HrTH ) or P. americana (the two octapeptides Pea-CAH -I and II) causes interconversion of phosphorylase; after injection, mainly (60% ) phosphorylase a is present, while 25% and 15% exists in the ab- und b-form , respectively. Purification of the three phosphorylase forms from N. cinerea is achieved by anion-exchange chromatography on DEAE-Sephacel followed by affinity chromatography on AMP-Sepharose. The final specific activities are 2.1, 6.9 and 27.2 U /mg protein for the a-, ab- und b-form . The molecular mass of the active molecules on gel filtration is between 173,000 and 177,000, and SDS gel electrophoresis reveals a subunit mass of 87,100, suggesting a homodimeric structure for all three form s. Kinetic studies show hyperbolic saturation curves for the substrates glycogen and Pi respectively, with Kᴍ-values of 0.021, 0.019 and 0.073% for glycogen and 8.3, 6.3 and 17.9 mᴍ for Pi (a-, ab- and b-form ). Phosphorylase a exhibits a more or less hyperbolic response to AMP and needs 70 |iM A M P for m axim al stim ulation. The kinetics for the ab- and b-form s are sigm oidal and maximal activities are displayed at about 3 mᴍ (half-maximum activation as calculated from Hill plots are 55 and 280 μᴍ for the ab- und b-form , respectively). Caffeine is a strong inhibitor of the b-form , but has only a slight inhibiting effect (10 -20 % ) on the ab- and a-form in the presence of AMP.

Regulation of muscle glycogen phosphorylase activity following short-term endurance training

1996 ◽  
Vol 270 (2) ◽  
pp. E328-E335 ◽  
Author(s):  
A. Chesley ◽  
G. J. Heigenhauser ◽  
L. L. Spriet
Keyword(s):  
Endurance Training ◽  
Muscle Glycogen ◽  
Glycogen Phosphorylase ◽  
Citrate Synthase ◽  
Phosphorylase Activity ◽  
Short Term ◽  
Mitochondrial Potential ◽  
Before And After ◽  
Glycogen Phosphorylase Activity ◽  
Muscle Biopsies

The purpose of this study was to examine the regulation (hormonal, substrate, and allosteric) of muscle glycogen phosphorylase (Phos) activity and glycogenolysis after short-term endurance training. Eight untrained males completed 6 days of cycle exercise (2 h/day) at 65% of maximal O2 uptake (Vo2max). Before and after training subjects cycled for 15 min at 80% of Vo2max, and muscle biopsies and blood samples were obtained at 0 and 30 s, 7.5 and 15 min, and 0, 5, 10, and 15 min of exercise. Vo2max was unchanged with training but citrate synthase (CS) activity increased by 20%. Muscle glycogenolysis was reduced by 42% during the 15-min exercise challenge following training (198.8 +/- 36.9 vs. 115.4 +/- 25.1 mmol/kg dry muscle), and plasma epinephrine was blunted at 15 min of exercise. The Phos a mole fraction was unaffected by training. Muscle phosphocreatine utilization and free Pi and AMP accumulations were reduced with training at 7.5 and 15 min of exercise. It is concluded that posttransformational control of Phos, exerted by reductions in substrate (free Pi) and allosteric modulator (free AMP) contents, is responsible for a blunted muscle glycogenolysis after 6 days of endurance training. The increase in CS activity suggests that the reduction of muscle glycogenolysis was due in part to an enhanced mitochondrial potential.

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