Adenosine triphosphatases during maturation of cultured human skeletal muscle cells and in adult human muscle

Benders, A.A.G.M.; Kuppevelt, T. H. M. S. M. Van; Oosterhof, Arie; Wevers, Ron A.; Veerkamp, J.H.

doi:10.1016/0005-2736(92)90258-n

Cited by 20 publications

(23 citation statements)

References 46 publications

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“…Previous work had assumed 19.5 M 3-O-MFP to be optimal for human skeletal muscle (18). The fivefold higher activity reported for human muscle in the present study can largely be attributed to this modification.…”

Section: Assay Specificitymentioning

confidence: 42%

“…To our knowledge there are only two reports of K ϩ -stimulated 3-O-MFPase activity in human skeletal muscle (18,19) based on an earlier method for rat skeletal muscle (17). However, during preliminary investigations in our laboratory we were unable to reliably determine K ϩ -stimulated 3-O-MFPase activity in human skeletal muscle using this technique.…”

Section: ؉ -Atpase Activity In Small Samples Of Human Skeletal Musclementioning

confidence: 46%

“…1 , which was fivefold higher than the only other published results for human skeletal muscle (18,19). The current assay optimized enzymatic conditions for human skeletal muscle and was modified from previous work using rat (17) and human (18) skeletal muscle.…”

Section: Assay Specificitymentioning

confidence: 88%

“…However, during preliminary investigations in our laboratory we were unable to reliably determine K ϩ -stimulated 3-O-MFPase activity in human skeletal muscle using this technique. The present paper describes several substantial modifications to earlier K ϩ -stimulated 3-O-MFPase activity assays (17,18) to optimize enzymatic conditions for measurement of Na ϩ ,K ϩ -ATPase activity in human skeletal muscle.…”

Section: ؉ -Atpase Activity In Small Samples Of Human Skeletal Musclementioning

confidence: 99%

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Measurement of Na+,K+-ATPase Activity in Human Skeletal Muscle

McKenna

1998

Analytical Biochemistry

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Section: Assay Specificitymentioning

confidence: 42%

Section: ؉ -Atpase Activity In Small Samples Of Human Skeletal Musclementioning

confidence: 46%

Section: Assay Specificitymentioning

confidence: 88%

Section: ؉ -Atpase Activity In Small Samples Of Human Skeletal Musclementioning

confidence: 99%

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Measurement of Na+,K+-ATPase Activity in Human Skeletal Muscle

McKenna

1998

Analytical Biochemistry

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“…Brody's disease, was first reported by Brody in and/or lO'-de pendent 3-0-methyl fluoresce in phos-1969. The literature now cites 21 cases (Brody 1969, phatase (3-OMFPase;Benders et aL 1992). SR Ca2* Karpati et aL (1986), Dation et aL 1988, Taylor et aL ATPase was examined by Ca21 -dependent phosphoryl-1988, Benders et aL 1994a).…”

Section: Muscle Cell Cultures N a \ K* A Tp Ase And S R Cau A 1 T A Sementioning

confidence: 99%

Ion transport in human skeletal muscle cells: disturbances in myotonic dystrophy and Brody's disease

Benders

Wevers

Veerkamp

1996

Acta Physiologica Scandinavica

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After excitation of skeletal muscle, the disturbed ion homeostasis is restored by N « \ K1 ATPase of the sarcolemma and Ca2+ ATPase of the sarcoplasmic reticulum (SR). Contrary to Na+, K+ ATPase, the concentration and isoenzyme distribution of SR Ca2+ ATPase in human skeletal muscle depend on fibre type and age. In cultured human muscle cells the concentration and activity of N a \ K+ ATPase and SR Ca2* ATPase increase with maturation.In skeletal muscle and cultured muscle cells of patients suffering from myotonic dystrophy (MyD), the activity and the concentration of both N a \ K* ATPase and SR Ca2+ ATPase are decreased by about 40%, In addition, we measured in cultured MyD muscle cells at rest an

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Cellular Processes Integrating the Metabolic Response to Exercise

Meyer

Foley

1996

Comprehensive Physiology

101

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The sections in this article are: The Central Role of Adenine Nucleotides Components of the High‐Energy Phosphate System Phosphate Metabolites are a Linked Network Approaches to Understanding Metabolic Control Classic Enzyme Kinetics Nonequilibrium Thermodynamics Regulated Enzymes and the Role of Calcium Determinants of Muscle Cell ATPase Rate The Basal ATPase The Contractile ATPase Metabolite Changes During Muscle Stimulation Methodology The Low‐Rate, Nonfatiguing Domain The High‐Rate, Fatiguing Domain The Transitional Domain Control of Oxidative Phosphorylation in Muscle Kinetic Control by [ ADP ] Thermodynamic Control by Cytoplasmic Phosphates Experimental Tests of Control Models The Importance of Muscle Aerobic Capacity Control of Glycogenolysis/Glycolysis in Muscle The Conventional View Problems with the Conventional View Reaction Disequilibria and Metabolite Diffusion Enzyme Organization Control of Force Generation Summary and Future Directions

show abstract

Adenosine triphosphatases during maturation of cultured human skeletal muscle cells and in adult human muscle

Cited by 20 publications

References 46 publications

Measurement of Na+,K+-ATPase Activity in Human Skeletal Muscle

Measurement of Na+,K+-ATPase Activity in Human Skeletal Muscle

Ion transport in human skeletal muscle cells: disturbances in myotonic dystrophy and Brody's disease

Cellular Processes Integrating the Metabolic Response to Exercise

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