Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P20020 (adenosine triphosphatase)
 3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

This study was designed to determine the effects of reduced neuromuscular activity on the expression of proteins associated with contractile and metabolic functions and the size of single muscle fibers in the cat soleus. Adult cats were spinalized (Sp) at T12-T13 and maintained in a healthy condition for 6 months. Some of the cats were trained to weight-support (Sp-WS) for 30 minutes per day beginning one month posttransection. Cross-sectional area (CSA), succinate dehydrogenase (SDH), alpha-glycerophosphate dehydrogenase (GPD), and myofibrillar adenosine triphosphatase (ATPase) activities were determined in a population of single fibers identified in frozen serial cross-sections. Each fiber was categorized as either light or dark based on its staining density for qualitative myosin ATPase, alkaline preincubation (pH 8.75). The Sp (45%) and Sp-WS (31%) groups had significantly higher percentages of dark ATPase fibers than control (less than 1%). All dark ATPase fibers were shown to react positively for a fast myosin heavy chain monoclonal antibody, while some of these fibers showed a reaction to both fast and slow myosin heavy chain antibodies. Overall mean fiber CSA were significantly smaller (approximately 25%) than control in both Sp groups. In the Sp-WS, but not the Sp cats, the dark fibers were larger than the light fibers (P less than 0.05), suggesting a preferential effect of postural training on the ATPase converted fibers. There were no significant differences among the three groups in any of the mean enzyme activities for either ATPase type fiber. However, there was a general tendency for the Sp cats to have elevated GPD and ATP activities per muscle; this appeared to be directly related to the percentage of fibers staining darkly for myosin ATPase. These data indicate that 6 months after spinalization some of the fibers of the slow muscle developed fast myosin staining patterns and oxidative and glycolytic enzyme profiles that are normally exhibited in fast fatigue-resistant motor units. Periods of daily weight-support appear to ameliorate some of these adaptations to spinalization. Further, the observation that SDH activities are maintained at control values in spinalized adult cats as well as in spinalized kittens (unpublished observations) suggest that, at least in the soleus, skeletal muscle fibers can maintain their oxidative potential even though there is a marked reduction in neuromuscular activity for 6 months.
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PMID:Expression of a fast fiber enzyme profile in the cat soleus after spinalization. 214 97

The reconstituted glycolytic system described previously (Scopes, 1973) was used to simulate post-mortem glycolytic metabolism in muscle. The effects of the following factors have been investigated: ATPase (adenosine triphosphatase) amount, AMP deaminase amount, percentage of the phosphorylase in the a form and the effect of diluting the glycolytic enzyme complex as a whole. It was confirmed that the rate of metabolism was solely dependent on the amount of ATPase present and that various concentrations of the glycolytic enzymes had no effect over a wide range encompassing the variation found in anatomically different muscles. The extent of metabolism, represented by the value of the ;ultimate' pH, depended markedly on the amount of phosphorylase in the a form; as little as 1% of the a form resulted in a considerably lower pH than in its absence. To a lesser extent the amount of AMP deaminase also affected the ultimate pH, but this was probably only significant for comparisons of genetically distinct muscles with widely differing amounts of AMP deaminase. The reconstituted system behaved almost identically with regard to post-mortem glycolytic metabolism compared with intact muscle tissue. It is concluded that the controlling effectors found with the reconstituted system apply to intact muscle also.
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PMID:Studies with a reconstituted muscle glycolytic system. The rate and extent of glycolysis in simulated post-mortem conditions. 428 Mar 4

The vacuolar H+-adenosine triphosphatase (ATPase) subunit V0C (ATP6V0C), a proton-conducting, pore-forming subunit of vacuolar ATPase, maintains pH homeostasis and induces organelle acidification. The intracellular and extracellular pH of cancer cells affects their growth; however, the role of ATP6V0C in highly invasive esophageal cancer cells (ECCs) remains unclear. In this study, we examined the role of ATP6V0C in glucose metabolism in ECCs. The ATP6V0C depletion attenuated ECC proliferation, invasion, and suppressed glucose metabolism, as indicated by reduced glucose uptake and decreased lactate and adenosine triphosphate (ATP) production in cells. Consistent with this, expression of glycolytic enzyme and the extracellular acidification rate (ECAR) were also decreased by ATP6V0C knockdown. Mechanistically, ATP6V0C interacted with pyruvate kinase isoform M2 (PKM2), a key regulator of glycolysis in ECCs. The ATP6V0C depletion reduced PKM2 phosphorylation at tyrosine residue 105 (Tyr105), leading to inhibition of nuclear translocation of PKM2. In addition, ATP6V0C was recruited at hypoxia response element (HRE) sites in the lactate dehydrogenase A (LDHA) gene for glycolysis. Thus, our data suggest that ATP6V0C enhances aerobic glycolysis and motility in ECCs.
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PMID:Vacuolar H+-ATPase Subunit V0C Regulates Aerobic Glycolysis of Esophageal Cancer Cells via PKM2 Signaling. 3155 33