Glycogen Phosphorylase Activity in Biopsy Samples and Single Muscle Fibres of Musculus Quadriceps Femoris of Man at Rest

Harris, RC; Essén, Birgitta; Hultman, E.

doi:10.1080/00365517609054473

Cited by 27 publications

(15 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Despite a 32.5% increase in Phos activity in type I fibres in elderly subjects, higher activities were again noted in type II compared with type I fibres. The higher activity in type II fibres, particularly in younger subjects is consistent with previous work (Harris et al 1976;Schantz and Henriksson 1987). The present data suggest a greater variation with ageing in the enzymic distribution and ratio of these enzymes between fibre types.…”

Section: Discussionsupporting

confidence: 93%

See 1 more Smart Citation

Carnosine, taurine and enzyme activities of human skeletal muscle fibres from elderly subjects with osteoarthritis and young moderately active subjects

et al. 2006

View full text Add to dashboard Cite

Ageing is associated with a reduction in muscle carnosine (beta-alanyl-L-histidine), but there are no data on the changes specifically in type I and type II muscle fibres. Given the higher carnosine content of type II fibers, changes observed in whole muscle may be secondary to a shift in fibre composition. Carnosine, beta-alanine, histidine, taurine, and citrate synthase (CS) and glycogen phosphorylase (Phos), were measured in pools of single muscle fibres from freeze-dried muscle biopsies of vastus lateralis of nine elderly sedentary subjects (65-80 years) with osteoarthritis of the knee and undergoing total knee replacement, and nine young moderately active healthy subjects (20-35 years). Fibres were characterised as type I or II by myosin ATPase activity. Carnosine was 53.2% lower in type II fibres of older subjects resulting in an estimated 7% (and most probably still higher) decline in intracellular physico-chemical buffering capacity. Younger subjects showed higher CS activities in type I and higher Phos activities in type II fibres. These differences were less apparent in elderly subjects. Possible causes for the change in the carnosine content are reduced physical activity, reduced meat intake, or the result of progressive denervation.

show abstract

Section: Discussionsupporting

confidence: 93%

“…Still earlier studies have established a similar fibre distribution of carnosine and taurine in muscle fibres from horses (Dunnett and Harris 1995) and camels (Dunnett et al 1997). Similarly, higher activities of CS in type I fibres and higher activities of Phos in type II fibres have previously been reported (Harris et al 1976). …”

Section: Discussionmentioning

confidence: 77%

Carnosine, taurine and enzyme activities of human skeletal muscle fibres from elderly subjects with osteoarthritis and young moderately active subjects

et al. 2006

View full text Add to dashboard Cite

show abstract

“…This is one of the few studies to have examined the activity of the glycogen catabolizing enzyme phosphorylase. The values for phosphorylase activity before training are similar to those obtained by Harris et al (9) on untrained men, after adjustments have been made for differences in methodology. Phosphorylase exhibits a lower level of activity than PFK and, therefore, may impose a limitation on the rate of glycolysis during short duration, high-intensity exercise.…”

Section: Enzyme Activity Levelssupporting

confidence: 59%

Anaerobic Muscle Enzyme Changes After Interval Training

Roberts¹,

Billeter²,

Howald³

1982

Int J Sports Med

View full text Add to dashboard Cite

In contrast to endurance training, little evidence is available concerning the effects of sprint-type training programs on the anaerobic metabolism of skeletal muscle. Four male subjects completed a mean of 16 training sessions consisting of eight 200-m runs at 90% of maximal speed, which were separated by 2-min rest periods. Before and after the 5-week training period, muscle biopsies were taken out of the lateral head of m. gastrocnemius and analyzed for the activities of phosphorylase, phosphofructokinase (PFK), glyceraldehyde phosphate dehydrogenase (GAPDH), lactate dehydrogenase (LDH), succinate dehydrogenase (SDH), and malate dehydrogenase (MDH). Following training there was a significant increase in the subjects' performance time in a treadmill test at a speed of 16 km/h speed and 15% grade. Significant increases were observed in the activities of phosphorylase, PFK, GAPDH, LDH, and MDH, whereas the 17.5% increase in SDH was not statistically significant. It is concluded that interval training with high intensity and a 1:4 work-rest ratio leads to increased activities of key enzymes involved in glycogenolysis and anaerobic glycolysis of skeletal muscle.

show abstract

“…α‐Enolase is a highly conserved cytoplasmic glycolytic enzyme that catalyzes the formation of phosphoenolpyruvate from 2‐phosphoglycerate. This high‐energy intermediate propels the generation of ATP in glycolysis (Harris et al, 1976). This study is consistent with the decrease in glucose metabolism in AD pathology with α‐enolase oxidation and activity decline.…”

Section: Discussionmentioning

confidence: 99%

An increase in S‐glutathionylated proteins in the Alzheimer's disease inferior parietal lobule, a proteomics approach

Newman

Sultana

Perluigi

et al. 2007

J of Neuroscience Research

159

110

View full text Add to dashboard Cite

Alzheimer's disease (AD) is a neurodegenerative disorder characterized by neurofibrillary tangles, senile plaques, and loss of synapses. Many studies support the notion that oxidative stress plays an important role in AD pathogenesis. Previous studies from our laboratory employed redox proteomics to identify oxidatively modified proteins in the AD inferior parietal lobule (IPL) and hippocampus. The proteins were consistent with biochemical or pathological alterations in AD and have been central to further investigations of the disease. The present study focused on the identification of specific targets of protein S-glutathionylation in AD and control IPL by using a redox proteomics approach. For AD IPL, we identified deoxyhemoglobin, alpha-crystallin B, glyceraldehyde phosphate dehydrogenase (GAPDH), and alpha-enolase as significantly S-glutathionylated relative to these brain proteins in control IPL. GAPDH and alpha-enolase were also shown to have reduced activity in the AD IPL. This study demonstrates that specific proteins are sensitive to S-glutathionylation, which most likely is due to their sensitivity to cysteine oxidation initiated by the increase in oxidative stress in the AD brain.

show abstract

Glycogen Phosphorylase Activity in Biopsy Samples and Single Muscle Fibres of Musculus Quadriceps Femoris of Man at Rest

Cited by 27 publications

References 18 publications

Carnosine, taurine and enzyme activities of human skeletal muscle fibres from elderly subjects with osteoarthritis and young moderately active subjects

Carnosine, taurine and enzyme activities of human skeletal muscle fibres from elderly subjects with osteoarthritis and young moderately active subjects

Anaerobic Muscle Enzyme Changes After Interval Training

An increase in S‐glutathionylated proteins in the Alzheimer's disease inferior parietal lobule, a proteomics approach

Contact Info

Product

Resources

About