Association of rabbit muscle glycolytic enzymes with filamentous actin

Westrin, Hjalmar; Backman, Lars

doi:10.1111/j.1432-1033.1983.tb07757.x

Cited by 45 publications

(12 citation statements)

References 25 publications

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“…Elevated activities of PK and 3-GAPDH (the latter in females only) were found in the Endo and Mid regions, which is not in concert with the changes in glucose uptake. However, the possible compartmentalization of glycolytic ATP production (36,59) may be changed due to training, and this cannot be shown by the methods used in this study. Increased LDH activity, especially in right ventricles, may be related to the enhanced ability of trained rats to use lactic acid as a myocardial energy fuel during exercise.…”

Section: Effects Of Training On Glycolytic Enzymescontrasting

confidence: 50%

“…This explanation is opposed by the fact that regional distribution of glucose uptake during perfusion is similar to in vivo distribution (55). Perfusion may also influence the binding of glycolytic enzymes on the filamentous or membranous structures of the myocardial ceils (36,59) or wash out possible factors regulating enzyme activities.…”

Section: Effect Of Perfusion On Enzyme Activitiesmentioning

confidence: 99%

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Effect of chronic exercise on glucose uptake and activities of glycolytic enzymes measured regionally in rat heart

et al. 1989

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Regional glucose uptake in perfused hearts, and the activities of several glycolytic enzymes contributing to the glucose metabolism in perfused and nonperfused hearts were studied in male and female rats after 8-9 weeks of swimming training. The left ventricular glucose uptake showed a transmural gradient in the sedentary animals, the subendocardial uptake being 30% and 12% higher than that of the subepicardial layer in the males and females, respectively. Swimming exercise abolished the left ventricular glucose uptake gradient in male rats, and in female rats an opposite gradient was found, the subepicardial uptake being 23% higher than the subendocardial uptake. The activities of phosphofructokinase and 3-phosphoglyceraldehyde dehydrogenase also showed transmural gradients in the left ventricles. Training did not abolish these gradients. Training-induced changes in the activities of phosphofructokinase, 3-phosphoglyceraldehyde dehydrogenase, pyruvate kinase, lactate dehydrogenase, glucose-6-phosphate dehydrogenase, citrate synthase, and malate dehydrogenase were found in certain sites of the myocardium. Perfusion of isolated hearts for 50 min with insulin-containing Krebs-Ringer buffer especially affected the activities of phosphofructokinase, lactate dehydrogenase, and citrate synthase, increasing these activities in the left ventricles and decreasing them in the atria. These results indicate that there are regional differences between male and female rats in the cardiac glucose uptake rate after swimming training.

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Section: Effects Of Training On Glycolytic Enzymescontrasting

confidence: 50%

Section: Effect Of Perfusion On Enzyme Activitiesmentioning

confidence: 99%

Effect of chronic exercise on glucose uptake and activities of glycolytic enzymes measured regionally in rat heart

et al. 1989

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“…These results indicate that GPD associates with actin. Previous reports also show that some glycolytic enzymes containing GPD bind to actin (Masters, 1981;Westrin and Backman, 1983). Schmitz and BereiterHahn (2002) reported on the molecular interaction between GPD and actin.…”

Section: Resultsmentioning

confidence: 95%

Molecular Interaction Studies Evaluating the Gelation of Myosin B with Glyceraldehyde 3-phosphate Dehydrogenase after Succinylation

Sakamoto

Sasaki

Nakade

et al. 2013

FSTR

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Previously, it was clarified that myofibril gelation was enhanced by the basic protein glyceraldehyde 3-phosphate dehydrogenase (GPD). In this study, the mechanism of the gel-enhancing action of GPD to myosin B was evaluated through the study of the surface properties of GPD. GPD and myosin B were prepared from pork loin. Succinylated GPD (S-GPD) was successfully prepared without any loss of solubility at a weight ratio (succinic anhydrate to GPD) of 1.0. Though gelation of myosin B alone required a minimum protein concentration of 4.0% (w/v), the addition of GPD enhanced the gelation of myosin B at a concentration of 3.5% (w/v). Furthermore, GPD increased the gel strength drastically at concentrations above 4.5% (w/v). On the other hand, the addition of S-GPD did not improve the gelling property of myosin B. SDS-PAGE showed molecular interaction between GPD and myosin B, but not between S-GPD and myosin B. However, in the case of GPD, the GPD band became insoluble under coexistence of GPD with myosin B. Meanwhile, the myosin heavy chain was partially soluble. Furthermore, actin and GPD bands became thicker in the insoluble fraction after mixing of G-actin and GPD. These results indicate that positive charges on the surface of GPD are necessary to enhance the gelation of myosin B.

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“…Some investigators consider PFK to have the high capability of associating with F-actin (Clarke & Masters, 1975) and marked effects of F-actin and reconstituted thin filaments on the catalytic properties of PFK were revealed (Liou & Anderson, 1980). However, other authors failed to demonstrate any PFK-association with actin (Bronstein & Knull, 1981;Westrin & Backman, 1983). It is worth noting that the precise determination of the amount of the bound PFK is much hindered due to its strong tendency to self-association and inactivation.…”

Section: Introductionmentioning

confidence: 99%

Localization of binding sites of F-protein (phosphofructokinase) on the myosin molecule

Freydina

Shpagina

Podlubnaya

1986

J Muscle Res Cell Motil

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To determine the location of F-protein binding sites on myosin, the interaction of F-protein with myosin and its proteolytic fragments in 0.1 M KCl, 10 mM potassium phosphate, pH 6.5, has been investigated using sedimentation, electron microscopy and optical diffraction methods. Sedimentation experiments show that F-protein can bind to myosin and myosin rod rather than to light meromyosin or subfragment-1. The F-protein binding to myosin and rod is of a similar character. The calculated values of the constants of F-protein binding to myosin and rod are 2.6 X 10(5) M-1 and 2.1 X 10(5) M-1, respectively. The binding sites are probably located on the subfragment-2 portion of the myosin molecule. The number of the F-protein binding sites calculated per chain weight of 80,000 is 5 +/- 1. Electron microscopic observations confirm the sedimentation results. F-protein does not bind to light meromyosin paracrystals, but decorates myosin and rod filaments with the interval of 14.3 nm regardless of whether F-protein is added prior to or after filamentogenesis. The comparison of optical diffraction patterns obtained from myosin and rod filaments with those from decorated ones reveals the marked enhancement of meridional reflection at (14.3 nm)-1 in the latter case. Neither the increase in ionic strength from 0.1 to 0.15 and pH from 6.5 to 7.3 nor substitution of potassium phosphate buffer by imidazole-HCl buffer, or Tris-HCl influences F-protein binding to myosin and rod filaments as visualized by electron microscopy. The possible significance of F-protein location in the thick filament structure is discussed.

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Association of rabbit muscle glycolytic enzymes with filamentous actin

Cited by 45 publications

References 25 publications

Effect of chronic exercise on glucose uptake and activities of glycolytic enzymes measured regionally in rat heart

Effect of chronic exercise on glucose uptake and activities of glycolytic enzymes measured regionally in rat heart

Molecular Interaction Studies Evaluating the Gelation of Myosin B with Glyceraldehyde 3-phosphate Dehydrogenase after Succinylation

Localization of binding sites of F-protein (phosphofructokinase) on the myosin molecule

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