scholarly journals L-arginine supplementation attenuates capillary regression without increasing integrated succinate dehydrogenase activity and VEGF expression in skeletal muscle during hindlimb unloading

2016 ◽  
Vol 35 (04) ◽  
pp. 425-432 ◽  
Author(s):  
Kensaku Uchida ◽  
Minoru Tanaka ◽  
Hiroyo Kondo ◽  
Akihiko Ishihara ◽  
Hidemi Fujino
Keyword(s):  
Skeletal Muscle ◽  
Succinate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Hindlimb Unloading ◽  
Vegf Expression ◽  
Succinate Dehydrogenase Activity ◽  
Arginine Supplementation

Intracellular distribution of succinate dehydrogenase activity in skeletal muscle fibers of geese

1984 ◽  
Vol 62 (2) ◽  
pp. 235-240 ◽  
Author(s):  
H. J. Swatland
Keyword(s):  
Skeletal Muscle ◽  
Succinate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Adenosine Triphosphatase ◽  
Muscle Fibers ◽  
Fiber Types ◽  
Succinate Dehydrogenase Activity ◽  
Individual Muscle ◽  
Concentric Zone ◽  
Pectoralis Muscles

Samples of iliotibialis anterior and pectoralis muscles were taken from five ganders (Anser domesticus). Serial transverse sections were reacted for succinate dehydrogenase (SDH) and alkali-stable adenosine triphosphatase (ATPase). The distribution of SDH activity within individual muscle fibers was measured with a scanning photometer. In many individual fibers, SDH activity was stronger in the periphery than in the axis. This gradient was steepest (−0.034 ± 0.019 absorbance units per concentric zone of 2 μm diameter measurements) in pectoralis fibers with strong SDH activity. In the pectoralis, radial gradients were correlated with fiber area so that the smallest fibers tended to have the steepest gradients of SDH activity. However, this relationship was reversed in fibers with strong ATPase and weak SDH activity in the iliotibialis anterior, and the largest fibers tended to have the steepest gradients. In all fiber types of both muscles, fibers with greater mean SDH activity tended to have steeper gradients.

scholarly journals Assay of succinate dehydrogenase activity by the tetrazolium method: evaluation of an improved technique in skeletal muscle fractions.

1980 ◽  
Vol 28 (5) ◽  
pp. 408-412 ◽  
Author(s):  
J D Green ◽  
H T Narahara
Keyword(s):  
Skeletal Muscle ◽  
Ethyl Acetate ◽  
Succinate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Inhibitory Effects ◽  
Succinate Dehydrogenase Activity ◽  
Low Concentrations ◽  
Mitochondrial Fractions ◽  
Mitochondrial Suspension ◽  
Improved Technique

An improved spectrophotometric method for measuring succinate dehydrogenase (EC 1.3.99.1) activity with the use of 2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyltetrazolium chloride (INT) is described. The procedure has been evaluated in mitochondrial fractions and homogenates of frog skeletal muscle. For mitochondrial suspensions, extraction of formazan with alcohol was found to be superior to extraction with ethyl acetate. For homogenates, complete extraction of formazan required sequential treatment with alcohol and ethyl acetate; the generally employed procedure of extracting once with ethyl acetate alone led to serious underestimation of the amount of formazan in the tissue. Observations of mitochondrial suspension incubated with various concentrations of INT led to the selection of 0.8 mM INT for optimal results. Higher concentrations, although commonly used, can exert undesirable inhibitory effects on succinate dehydrogenase activity, especially at low concentrations of mitochondria and after longer periods of incubation. The problem of instability of succinate dehydrogenase was solved by the addition of buffer at pH 7.5.

scholarly journals Skeletal muscle fiber‐type specific succinate dehydrogenase activity in cerebral palsy

2016 ◽  
Vol 55 (1) ◽  
pp. 122-124 ◽  
Author(s):  
Andrew M. Zogby ◽  
Sudarshan Dayanidhi ◽  
Henry G. Chambers ◽  
Simon Schenk ◽  
Richard L. Lieber
Keyword(s):  
Skeletal Muscle ◽  
Cerebral Palsy ◽  
Succinate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Muscle Fiber ◽  
Fiber Type ◽  
Skeletal Muscle Fiber ◽  
Muscle Fiber Type ◽  
Succinate Dehydrogenase Activity

Skeletal Muscle Succinate Dehydrogenase Activity is not Altered in Cerebral Palsy

2015 ◽  
Vol 47 ◽  
pp. 62
Author(s):  
Andrew M. Zogby ◽  
Sudarshan Dayanidhi ◽  
Henry G. Chambers ◽  
Simon Schenk ◽  
Richard L. Lieber
Keyword(s):  
Skeletal Muscle ◽  
Cerebral Palsy ◽  
Succinate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Succinate Dehydrogenase Activity

Myosin heavy chain composition in young and old rat skeletal muscle: effects of endurance exercise

1995 ◽  
Vol 78 (6) ◽  
pp. 2115-2120 ◽  
Author(s):  
V. K. Sullivan ◽  
S. K. Powers ◽  
D. S. Criswell ◽  
N. Tumer ◽  
J. S. Larochelle ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Exercise Training ◽  
Myosin Heavy Chain ◽  
Succinate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Endurance Exercise ◽  
Heavy Chain ◽  
Medial Gastrocnemius ◽  
Type I ◽  
Succinate Dehydrogenase Activity

The objective of this study was to determine the effects of age and exercise on the myosin heavy chain (MHC) composition of skeletal muscle. Young (3 mo) and old (22 mo) female specific pathogen-free barrier-reared Fischer 344 rats were randomly assigned to young untrained or young trained and old untrained or old trained groups, respectively. Young trained and old trained animals performed endurance exercise training on a motorized treadmill for 8 wk. Succinate dehydrogenase activity and MHC isoforms were measured in the plantaris (Plan), lateral and medial gastrocnemius (Gast), and soleus (Sol) muscles. In sedentary animals, aging resulted in a decrease (P < 0.05) in type IIb MHC and an increase (P < 0.05) in type IIa MHC in both the Gast and Plan muscles. Also, aging resulted in a small but significant increase (approximately 4%; P < 0.05) in type I MHC in the Sol. Exercise training resulted in significant (P < 0.05) increases in Gast, Plan, and Sol succinate dehydrogenase activity in both young and old animals. Furthermore, exercise training resulted in a decrease (P < 0.05) in the percentage of type IIb MHC and an increase (P < 0.05) in the percentage of type IIa MHC in the Plan in both young and old animals. These data suggest that there is an age-related shift in locomotor muscle MHC isoforms from a faster to a slower isoform.

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