A comparative histochemical study of oxidative enzyme and phosphorylase activity in skeletal muscle

1960 ◽  
Vol 2 (2) ◽  
pp. 105-117 ◽  
Author(s):  
V. Dubowitz ◽  
A. G. Everson Pearse
1965 ◽  
Vol 1965 (6) ◽  
pp. 58-60
Author(s):  
Hitoshi TANABE ◽  
Masanori TOMONAGA ◽  
Osamu WADA ◽  
Masanori UONO

1998 ◽  
Vol 85 (1) ◽  
pp. 210-214 ◽  
Author(s):  
John P. Mattson ◽  
David C. Poole

Skeletal muscle oxidative enzyme capacity is impaired in patients suffering from emphysema and chronic obstructive pulmonary disease. This effect may result as a consequence of the physiological derangements because of the emphysema condition or, alternatively, as a consequence of the reduced physical activity level in these patients. To explore this issue, citrate synthase (CS) activity was measured in selected hindlimb muscles and the diaphragm of Syrian Golden hamsters 6 mo after intratracheal instillation of either saline (Con, n = 7) or elastase [emphysema (Emp); 25 units/100 g body weight, n = 8]. Activity level was monitored, and no difference between groups was found. Excised lung volume increased with emphysema (Con, 1.5 ± 0.3 g; Emp, 3.0 ± 0.3 g, P < 0.002). Emphysema significantly reduced CS activity in the gastrocnemius (Con, 45.1 ± 2.0; Emp, 39.2 ± 0.8 μmol ⋅ min−1 ⋅ g wet wt−1, P < 0.05) and vastus lateralis (Con, 48.5 ± 1.5; Emp, 44.9 ± 0.8 μmol ⋅ min−1 ⋅ g wet wt−1, P < 0.05) but not in the plantaris (Con, 47.4 ± 3.9; Emp, 48.0 ± 2.1 μmol ⋅ min−1 ⋅ g wet wt−1, P < 0.05) muscle. In contrast, CS activity increased in the costal (Con, 61.1 ± 1.8; Emp, 65.1 ± 1.5 μmol ⋅ min−1 ⋅ g wet wt−1, P < 0.05) and crural (Con, 58.5 ± 2.0; Emp, 65.7 ± 2.2 μmol ⋅ min−1 ⋅ g wet wt−1, P < 0.05) regions of the diaphragm. These data indicate that emphysema per se can induce decrements in the oxidative capacity of certain nonventilatory skeletal muscles that may contribute to exercise limitations in the emphysematous patient.


2006 ◽  
Vol 101 (6) ◽  
pp. 1685-1692 ◽  
Author(s):  
Masataka Suwa ◽  
Toru Egashira ◽  
Hiroshi Nakano ◽  
Haruka Sasaki ◽  
Shuzo Kumagai

1992 ◽  
Vol 97 (3) ◽  
pp. 263-267 ◽  
Author(s):  
E. De Santis ◽  
E. Pompili ◽  
G. De Renzis ◽  
A. M. Bondi ◽  
G. Menghi ◽  
...  

1992 ◽  
Vol 284 (3) ◽  
pp. 777-780 ◽  
Author(s):  
P Hespel ◽  
E A Richter

The influence of differences in glycogen concentration on glycogen breakdown and on phosphorylase activity was investigated in perfused contracting rat skeletal muscle. The rats were preconditioned by a combination of swimming exercise and diet (carbohydrate-free or carbohydrate-rich) in order to obtain four sub-groups of rats with varying resting muscle glycogen concentrations (range 10-60 mumol/g wet wt.). Pre-contraction muscle glycogen concentration was closely positively correlated with glycogen breakdown over 15 min of intermittent short tetanic contractions (r = 0.75; P less than 0.001; n = 56) at the same tension development and oxygen uptake. Additional studies in supercompensated and glycogen-depleted hindquarters during electrical stimulation for 20 s or 2 min revealed that the difference in glycogenolytic rate was found at the beginning rather than at the end of the contraction period. Phosphorylase alpha activity was approximately twice as high (P less than 0.001) in supercompensated muscles as in glycogen-depleted muscles after 20 s as well as after 2 min of contractions. It is concluded that glycogen concentration is an important determinant of phosphorylase activity in contracting skeletal muscle, and probably via this mechanism a regulator of glycogenolytic rate during muscle contraction.


1997 ◽  
Vol 83 (1) ◽  
pp. 166-171 ◽  
Author(s):  
Jean-Aimé Simoneau ◽  
David E. Kelley

Simoneau, Jean-Aimé, and David E. Kelley. Altered glycolytic and oxidative capacities of skeletal muscle contribute to insulin resistance in NIDDM. J. Appl. Physiol. 83(1): 166–171, 1997.—The insulin resistance of skeletal muscle in glucose-tolerant obese individuals is associated with reduced activity of oxidative enzymes and a disproportionate increase in activity of glycolytic enzymes. Because non-insulin-dependent diabetes mellitus (NIDDM) is a disorder characterized by even more severe insulin resistance of skeletal muscle and because many individuals with NIDDM are obese, the present study was undertaken to examine whether decreased oxidative and increased glycolytic enzyme activities are also present in NIDDM. Percutaneous biopsy of vatus lateralis muscle was obtained in eight lean (L) and eight obese (O) nondiabetic subjects and in eight obese NIDDM subjects and was assayed for marker enzymes of the glycolytic [phosphofructokinase, glyceraldehyde phosphate dehydrogenase, hexokinase (HK)] and oxidative pathways [citrate synthase (CS), cytochrome- c oxidase], as well as for a glycogenolytic enzyme (glycogen phosphorylase) and a marker of anaerobic ATP resynthesis (creatine kinase). Insulin sensitivity was measured by using the euglycemic clamp technique. Activity for glycolytic enzymes (phosphofructokinase, glyceraldehye phosphate dehydrogenase, HK) was highest in subjects with subjects with NIDDM, following the order of NIDDM > O > L, whereas maximum velocity for oxidative enzymes (CS, cytochrome- c oxidase) was lowest in subjects with NIDDM. The ratio between glycolytic and oxidative enzyme activities within skeletal muscle correlated negatively with insulin sensitivity. The HK/CS ratio had the strongest correlation ( r = −0.60, P < 0.01) with insulin sensitivity. In summary, an imbalance between glycolytic and oxidative enzyme capacities is present in NIDDM subjects and is more severe than in obese or lean glucose-tolerant subjects. The altered ratio between glycolytic and oxidative enzyme activities found in skeletal muscle of individuals with NIDDM suggests that a dysregulation between mitochondrial oxidative capacity and capacity for glycolysis is an important component of the expression of insulin resistance.


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