Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.6.1.3 (ATPase)
65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Exposure of fish to water of impaired quality has been shown to disrupt the function of the hypothalamo-pituitary-interrenal (HPI) axis and alter the interpretation of data from field studies due to the varying effects of handling and delayed sampling on exposed and reference animals. In the present study, juvenile whitefish, Coregonus lavaretus, were exposed for 6 weeks to diluted (4-8%) untreated and biologically treated bleached kraft mill effluent (BKME) and their response to acute handling was investigated. Liver microsomal EROD activity and glycogen phosphorylase (GPase) activity, in addition to gill Na+-K+-ATPase activity, and blood hemoglobin and hematocrit levels were increased in whitefish exposed for 6 weeks to untreated BKME, whereas those exposed to treated BKME exhibited increased blood hemoglobin and red blood cell K+ concentrations. Both handling procedures, exposure to a shallow water (10 cm, 5 min) and to an air challenge (10 s air/10 s water/30 s air/10 s water/10 s air), resulted in acute physiological stress, as recorded after 5-, 60-, and 120-min recovery periods. Following air exposure, the levels of plasma cortisol, blood glucose, hemoglobin, and hematocrit as well as the liver GPase activity were increased, and liver glycogen concentration decreased in control fish. These responses were attenuated in fish exposed to untreated or treated BKME. Plasma estradiol and testosterone levels were not affected by the BKME exposures or by the air challenge. Handling also resulted in attenuated EROD induction in fish exposed to untreated BKME. According to the present findings, the sensitivity of some widely used cellular and physiological variables may be improved by time-dependent standardization when interpreting data obtained following delayed sampling.
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PMID:Effects of acute handling stress on whitefish Coregonus lavaretus after prolonged exposure to biologically treated and untreated bleached kraft mill effluent. 1138 90

The aim of this study was to examine the nature of fibre-type redistribution in relation to fibre metabolic profile in the vastus lateralis in chronic obstructive pulmonary disease (COPD) and COPD subtypes. Fifteen COPD patients (eight with emphysema stratified by high-resolution computed tomography) and 15 healthy control subjects were studied. A combination of myofibrillar adenosine triphosphatase staining and immunohistochemistry was used to identify pure, as well as hybrid fibre types. For oxidative capacity, fibres were stained for cytochrome c oxidase and succinate dehydrogenase activities, and glycogen phosphorylase for glycolytic capacity. The proportion of type-I fibres in COPD patients was markedly lower (16% versus 42%), especially in emphysema, and the proportion of hybrid fibres was higher (29% versus 16%) compared to controls. The proportion of fibres staining positive for oxidative enzymes was lower in COPD patients, which correlated with the proportion of type-I fibres. In COPD oxidative capacity was lower within IIA fibres. The authors conclude that fibre-type transitions are involved in the fibre-type redistribution in chronic obstructive pulmonary disease. Low oxidative capacity is closely related to the proportion of type-I fibres, but an additional reduction of oxidative enzyme activity is present within IIA fibres. Fibre-type abnormalities may be aggravated in emphysema.
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PMID:Skeletal muscle fibre-type shifting and metabolic profile in patients with chronic obstructive pulmonary disease. 1199 89

A dynamic model of the glycogenolytic pathway to lactate in skeletal muscle was constructed with mammalian kinetic parameters obtained from the literature. Energetic buffers relevant to muscle were included. The model design features stoichiometric constraints, mass balance, and fully reversible thermodynamics as defined by the Haldane relation. We employed a novel method of validating the thermodynamics of the model by allowing the closed system to come to equilibrium; the combined mass action ratio of the pathway equaled the product of the individual enzymes' equilibrium constants. Adding features physiologically relevant to muscle-a fixed glycogen concentration, efflux of lactate, and coupling to an ATPase--alowed for a steady-state flux far from equilibrium. The main result of our analysis is that coupling of the glycogenolytic network to the ATPase transformed the entire complex into an ATPase driven system. This steady-state system was most sensitive to the external ATPase activity and not to internal pathway mechanisms. The control distribution among the internal pathway enzymes-although small compared to control by ATPase-depended on the flux level and fraction of glycogen phosphorylase a. This model of muscle glycogenolysis thus has unique features compared to models developed for other cell types.
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PMID:A computational model for glycogenolysis in skeletal muscle. 1222 81

A previously published mammalian kinetic model of skeletal muscle glycogenolysis, consisting of literature in vitro parameters, was modified by substituting mouse specific Vmax values. The model demonstrates that glycogen breakdown to lactate is under ATPase control. Our criteria to test whether in vitro parameters could reproduce in vivo dynamics was the ability of the model to fit phosphocreatine (PCr) and inorganic phosphate (Pi) dynamic NMR data from ischemic basal mouse hindlimbs and predict biochemically-assayed lactate concentrations. Fitting was accomplished by optimizing four parameters--the ATPase rate coefficient, fraction of activated glycogen phosphorylase, and the equilibrium constants of creatine kinase and adenylate kinase (due to the absence of pH in the model). The optimized parameter values were physiologically reasonable, the resultant model fit the [PCr] and [Pi] timecourses well, and the model predicted the final measured lactate concentration. This result demonstrates that additional features of in vivo enzyme binding are not necessary for quantitative description of glycogenolytic dynamics.
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PMID:Basal glycogenolysis in mouse skeletal muscle: in vitro model predicts in vivo fluxes. 1224 Oct 44

The purpose of this investigation was to determine whether there is a link between sarcoplasmic reticulum (SR) glycogen status and SR Ca2+ handling. In this investigation, skeletal muscle SR was purified from female Sprague-Dawley rats (200-250 g). Glycogen was extracted from the SR purified from one hindlimb, whereas the SR purified from the contralateral limb served as control. Before removal of the tissue, the animals were anesthetized with an intraperitoneal injection of ketamine (80 mg/kg) and xylazine (10 mg/kg). Both alpha-amylase treatment (AM) and removal of EDTA from the homogenization and storage buffers reduced the amount of glycogen associated with the SR (P < 0.05). AM treatment reduced the glycogen phosphorylase content of SR (P < 0.05). In contrast, creatine kinase (CK) and pyruvate kinase (PK) contents were increased after both glycogen extraction protocols (P < 0.05). Under exogenous ATP conditions, both AM and EDTA-free (EF) treatments resulted in an increase in Ca2+-stimulated ATPase activity when normalized to sarco(endo)plasmic reticulum calcium-ATPase (SERCA) content (P < 0.05). CK and PK-supported SR Ca2+ uptake was decreased (P < 0.05) in the AM group when normalized to SERCA and CK or SERCA and PK content, respectively. AM was more effective than the EF for extracting glycogen associated with purified SR. Glycogen extraction alters the yield of purified SR proteins and must be taken into account when investigating SR calcium handling. Removal of glycogen from purified SR causes a change in Ca2+-handling properties as measured by ATPase and uptake activities.
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PMID:Skeletal muscle sarcoplasmic reticulum glycogen status influences Ca2+ uptake supported by endogenously synthesized ATP. 1296 14

Two-year-old whitefish (Coregonus lavaretus) were exposed for 30 days to episodic iron overload in iron-rich humic water (5%) supplemented with inorganic iron (5 mg FeL(-1)). Two parallel laboratory exposures were performed, one under conditions simulating winter and the other under conditions simulating spring. After exposure, some of the fish were subjected to acute handling stress in the form of a short air challenge to reveal possible modification of the primary and secondary stress responses. In whitefish sampled without additional handling, iron accumulated in the liver (under spring conditions) and gills (under winter and spring conditions); plasma catecholamine and beta-estradiol (both winter and spring groups) as well as blood hematocrit (winter group only) levels were depressed; blood glucose (winter group only) and red blood cell (RBC) Na+ levels (spring group only) were increased. In handled whitefish, liver glycogen phosphorylase (GPase), RBC, and blood glucose stress responses were impaired by the applied exposure conditions, which reflected natural iron-rich humic water. Exposure also removed some physiological effects of the applied ambient conditions: plasma catecholamines and beta-estradiol, gill Na+/K+ -ATPase, and RBC K+ concentration were not different in two iron-exposed fish groups, whereas there was a difference in reference fish. Thus, the physiological effects of this type of subchronic exposure, together with alterations in the acute stress response, can lead to incorrect conclusions being drawn from the results, if the effects of time-dependent stress response are ignored. In conclusion, waterborne iron overload may impair the optimal capacity of whitefish to carry out their normal physiological functions such as responding to external threats.
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PMID:Effects of waterborne iron overload and simulated winter conditions on acute physiological stress response of whitefish, Coregonus lavaretus. 1554 31

This manuscript discusses aspects of functional compartmentation in the regulation of metabolism. The functional consequences of enzymes coupling between creatine kinase, glycogen phosphorylase and sarcoplasmic reticular Ca2+ ATPase is examined. It is proposed that the coupling of creatine kinase and glycogen phosphorylase classifies as a novel class of diazyme complex with an important regulatory role in the inhibition of glycogenolysis at rest. In addition it is suggested that creatine kinase, glycogen phosphorylase and the sarcoplasmic reticular Ca2+ ATPase may couple to form a three-enzyme complex. From a consideration of the structure and chemical catalysis of the putative three-enzyme complex, a novel net reaction for glycogenolysis in the vicinity of the sarcoplasmic reticulum is suggested (Phosphocreatine+Glycogen+H(+)Creatine+Glycogen(n)(-1)+Glucose-1-Phosphate). The three-enzyme complex may also have an important role in inhibiting glycogenolysis at rest as well as improving the efficiency of high-energy phosphate transfer.
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PMID:Functional compartmentation of glycogen phosphorylase with creatine kinase and Ca2+ ATPase in skeletal muscle. 1600 21

The aim of this study was to examine the effects of reduced glycogen concentration on sarcoplasmic reticulum (SR) Ca(2+)-ATPase activity in rat fast-twitch muscles. In the first experiment, the gastrocnemius (GAS) muscle from one leg was removed, followed by starvation for 24-72 h, after which the remaining GAS was removed. Intra-animal comparisons revealed that starvation caused a 25% reduction (P<0.05) in the glycogen concentration but no change in SR Ca(2+)-ATPase activity in the GAS. In the second experiment, the SR was purified from a mixture of the GAS and vastus lateralis muscles. In half of the samples obtained from each animal, glycogen was extracted from the SR by treatment with glucoamylase. Treatment resulted in a 94.1 and 70.2% decrease (P<0.01) in glycogen and glycogen phosphorylase, respectively, and a 41.5% increase (P<0.05) in a fluorescein isothiocyanate (FITC) binding to SR Ca(2+)-ATPase. On the other hand, SR Ca(2+)-ATPase activity and the affinity of the enzyme for ATP were unaltered. These results do not implicate depletion of muscle glycogen as a contributor to impaired SR Ca(2+)-ATPase activity as measured in vitro. Therefore, it is concluded that muscle glycogen does not influence exercise tolerance and work productivity in working muscles by modulating the structure of protein involved in Ca(2+) sequestering. Furthermore, it is suggested that the FITC binding assay may be inappropriate as a method for examining the mechanisms for the altered activity of SR Ca(2+)-ATPase.
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PMID:Effects of reduced glycogen on structure and in vitro function of rat sarcoplasmic reticulum Ca2+-ATPase. 1636 70

The first biological action of amylin to be described was the inhibition of insulin-stimulated incorporation of radiolabeled glucose into glycogen in the isolated soleus muscle of the rat. This antagonism of insulin action in muscle was non-competitive, occurring with equal potency and efficacy at all insulin concentrations. Amylin inhibited activation of glycogen synthase, partially accounting for the inhibition of radiolabeled glucose incorporation. However, this did not account for a low rate of labeling at higher amylin concentrations, wherein the radioglycogen accumulation was even less than in incubations where insulin was absent. The principal action of amylin accounting for reduction of insulin-stimulated accumulation of glycogen was activation of glycogen phosphorylase via a cyclic AMP-, protein kinase C-dependent signaling pathway to cause glycogenolysis (glycogen breakdown). At physiological concentrations, amylin activated glycogen phosphorylase at its ED50, but because glycogen phosphorylase is present in such high activity, the resulting flux out of glycogen was estimated to be similar to insulin-mediated flux of glucosyl moieties into glycogen. Thus, in the rat, endogenous amylin secreted in response to meals appeared to mobilize carbon from skeletal muscle. Amylin-induced glycogenolysis resulted in intramuscular accumulation of glucose-6-phosphate and release of lactate from tissue beds that included muscle. When muscle glycogen was pre-labeled with tritium in the three position, amylin could be shown to evoke the release of free glucose. This is made possible by glucosyl moieties cleaved at the branch points in glycogen being released as free glucose, rather than being phosphorylated, as occurs with the bulk of the glycogen glucosyls. Free glucose is free to exit cells via facilitated transport, down a concentration gradient that might exist under such circumstances. When measured by a sensitive technique utilizing efflux of labeled glucose, amylin was reported to not affect muscle glucose transport. In most of the above respects, amylin behaved similarly to catecholamines in skeletal muscle. The pharmacology of amylin's effects on muscle glycogen metabolism was consistent with a classic amylin pharmacology in whole animals and in isolated soleus muscle. In one cell line, the pharmacology was CGRPergic. Amylin, like insulin, stimulated Na+/K+ ATPase activity and enhanced muscle contractility in vitro.
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PMID:Effects in skeletal muscle. 1649 48

The molecular and cellular mechanisms behind glycogen metabolism and the energy metabolite translocation between mammal neurons and astrocytes have been well studied. A similar mechanism is proposed for rapid mobilization of local energy stores to support energy-dependent transepithelial ion transport in gills of the Mozambique tilapia (Oreochromis mossambicus). A novel gill glycogen phosphorylase isoform (tGPGG), which catalyzes the initial degradation of glycogen, was identified in branchial epithelial cells of O. mossambicus. Double in situ hybridization and immunocytochemistry demonstrated that tGPGG mRNA and glycogen were colocalized in glycogen-rich cells (GRCs), which surround ionocytes (labeled with a Na(+)-K(+)-ATPase antiserum) in gill epithelia. Concanavalin-A (a marker for the apical membrane) labeling indicated that GRCs and mitochondria-rich cells share the same apical opening. Quantitative real-time PCR analyses showed that tGPGG mRNA expression levels specifically responded to environmental salinity changes. Indeed, the glycogen content, glycogen phosphorylase (GP) protein level and total activity, and the density of tGPGG-expressing cells (i.e., GRCs) in fish acclimated to seawater (SW) were significantly higher than those in freshwater controls. Short-term acclimation to SW caused an evident depletion in the glycogen content of GRCs. Taken altogether, tGPGG expression in GRCs is stimulated by hyperosmotic challenge, and this may catalyze initial glycogen degradation to provide the adjacent ionocytes with energy to carry out iono- and osmoregulatory functions.
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PMID:Glycogen phosphorylase in glycogen-rich cells is involved in the energy supply for ion regulation in fish gill epithelia. 1736 79


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