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)

The purpose of this study was to define variability of the oxidative capacity and glycogen content between different fiber types and regions of the hamster diaphragm. Using histochemical and microphotometric techniques, the oxidative capacity (identified by nicotinamide-adenine dinucleotide tetrazolium reductase reaction end product) and glycogen levels (identified by the periodic acid-Schiff stain test) were examined in three myofibrillar ATPase (M-ATPase) fiber types and four diaphragmatic regions: sternal, anterior costal, thoracic surface of the crural (thor/crur), and abdominal surface of the crural (abd/crur). Most regional differences were found between the crus and the rest of the diaphragm. There were no differences in the oxidative capacity between diaphragmatic regions in the types 1 and 2a fibers, but the type 2b fibers in the thor/crur region had the greatest oxidative capacity and the 2b fiber in the sternal region had the lowest oxidative capacity. There were differences in glycogen content between diaphragmatic regions for all of the three M-ATPase fiber types. Variability in oxidative capacity between fiber types was demonstrated in all regions except the thor/crur region. Variation in glycogen content between fiber types was only demonstrated in the two surfaces of the crus. The type 2b fiber demonstrated the most differences from types 1 and 2a fibers in oxidative capacity and glycogen content in the different diaphragmatic regions, whereas the types 1 and 2a fibers demonstrated few differences from each other in these features across the different diaphragmatic regions.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Fiber type and regional differences in oxidative capacity and glycogen content in the hamster diaphragm. 144 83

The main factors involved in the impairment of formation of the bile salt-independent bile flow (BSIF) in streptozotocin (SZ)-treated rats were examined. Twenty-four hours after SZ injection (50 mg/kg body wt, i.v.) bile flow, bile salt output and biliary excretion of the major inorganic electrolytes (sodium, chloride and bicarbonate) were significantly diminished. The relationship between bile flow and bile salt output obtained during the administration of sodium taurocholate at stepwise-increasing rates indicated that bile salt-independent bile flow (y-intercept) was diminished by 37% in SZ-treated rats. The relationship between electrolyte output and bile salt output showed that the fractions of sodium, chloride and bicarbonate excreted independently of bile salt (y-intercept) decreased to 59%, 47% and 67% of the control values respectively, while the amount of electrolyte secreted per unit of bile salt secreted was unaffected in SZ-treated rats. The hepatic activity of Na+,K(+)-adenosine triphosphatase (Na+,K(+)-ATPase) was decreased by 59% (P less than 0.05) in SZ-treated rats. Nicotinamide administered prior to SZ prevented the hyperglycemia indicative of SZ-induced diabetes, but had no effect on the decrease in Na+,K(+)-ATPase activity caused by the drug. These results suggest that SZ itself, and not its diabetogenic effect, decreases the BSIF by a mechanism that involves impairment of the biliary electrolyte excretion, which could be the result of the inhibition of the hepatic Na+,K(+)-ATPase activity.
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PMID:Studies on the mechanism of bile salt-independent bile flow impairment in streptozotocin-induced hepatotoxicity. 165 1

Aldose reductase (EC 1.1.1.21) is implicated in the pathophysiology of diabetic complications. In this paper we determined the activities of aldose reductase and ATPases of the erythrocytes in 17 patients with Type 2 (non-insulin-dependent) diabetes mellitus (NIDDM). In the aldose reductase assay we used fluorometric method to avoid the disturbance of hemoglobin. With dihydronicotinamide adenine dinucleotide (NADH), we verified it was aldose reductase but not aldehyde reductase II that was activated in the erythrocytes of the patients with NIDDM. The aldose reductase activity of the erythrocytes in the patients was significantly higher (P less than 0.01) than that in the controls. The activity of Na+/K(+)-ATPase of the patients was significantly lower (P less than 0.01) than that of the controls. The activities of Ca(2+)-ATPase and Mg(2+)-ATPase on the erythrocyte membranes of the patients were similar to those of the controls. At the same time we measured the seven nucleotide concentrations in the erythrocytes of the patients. In this experiment we used ultrafiltration method, instead of acid precipitation to make it possible to determine dihydronicotinamide adenine dinucleotide phosphate (NADPH) and NADH. The concentrations of ATP, ADP and AMP were similar to those of the controls. The concentrations of NADPH, NAD+ and NADH in the erythrocytes of the patients were significantly lower (P less than 0.01, 0.05 and 0.05 respectively) than those of controls. The concentration of nicotinamide adenine dinucleotide phosphate (NADP+) in the patients was significantly higher (P less than 0.01) than that of controls.
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PMID:Activities of aldose reductase, ATPases, and nucleotide concentrations of erythrocytes in patients with type 2 (non-insulin-dependent) diabetes mellitus. 166 Dec 22

A staining procedure used for simultaneously determining three different fiber types in single sections of bovine, porcine, or ovine skeletal muscle was modified for use with broiler skeletal muscle. The modification involved acid-preincubation of muscle sections at a pH of 4.15 followed by staining for reduced nicotinamide adenine dinucleotide (NADH) tetrazolium reductase enzyme and for acid-stable myosin-adenosine triphosphatase enzyme activity, respectively. Four broiler muscles were selected for fiber-type determination of fast (alpha), slow (beta), red, aerobic (R), or white, anaerobic (W) properties. The anterior latissimus dorsi muscle was composed almost entirely of beta-R fibers while the pectoralis superficialis muscle was composed almost entirely of alpha-W fibers. The sartorius and posterior latissimus dorsi muscles were much more heterogeneous in fiber-type distribution, exhibiting all three types of fibers (alpha-W, alpha-R, and beta-R).
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PMID:Research note: simultaneous histochemical determination of three fiber types in single sections of broiler skeletal muscles. 170 Apr 8

Various different combinations of histochemical stains at differing pH levels on single sections of bovine skeletal muscle were evaluated. The staining sequence that was the most consistent and reliable of those studied included an initial NADH-TR (reduced nicotinamide adenine dinucleotide-tetrazolium reductase) followed by an acid ATPase stain at pH 4.15. This staining combination resulted in easily discernable type I, II A, and II myofibers. Thus, a marked saving of expended time, labor and materials was realized.
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PMID:A rapid and reliable sequential staining method for bovine muscle. 170 Jun 44

The purpose of this study was to find a combination histochemical staining technique for the evaluation of equine skeletal muscle that is reliable and effective, while offering a substantial reduction in the labor and cost involved with currently used individual histochemical methods. Several combinations under varying conditions of pH were studied. The most uniform results were obtained using an acid preincubation step at an optimal pH of 4.2 followed by reduced nicotinamide adenine dinucleotide-tetrazolium reductase (NADH-TR) and the remainder of the acid-ATPase procedure.
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PMID:A combination histochemical stain for equine muscle. 171 35

The response of rat quadriceps muscle fibers to chronic streptozotocin (STZ) diabetes was studied. Transverse sections of rectus femoris muscle from diabetic and weight-matched control rats were assayed for myofibrilar adenosine triphosphatase (ATPase) and nicotinamide adenine dinucleotide-tetrazolium reductase (NADH-TR). A quantitative analysis was carried out by an automatic interactive analysis system focused on the fiber type size and distribution. STZ-induced diabetes caused important effects in this muscle, with changes in the distribution of oxidative enzyme reactions, type I fiber hypertrophy, and type II fiber atrophy, which was greater in type IIB than in type IIA. It is concluded that hypoinsulinism produces morphological alterations in proximal skeletal muscle fibers that are similar to those of neurogenic myopathy. Thus the pathological changes in these mammalian muscle fibers could explain the clinical syndrome seen in diabetic patients called "diabetic symmetrical proximal motor neuropathy," perhaps the least understood of the major neuropathic complications of diabetes.
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PMID:Proximal skeletal muscle alterations in streptozotocin-diabetic rats: a histochemical and morphometric analysis. 182 78

The effects of three tetrachlorobiphenylols [2',3',4',5'-tetrachloro-2-biphenylol (1); 2',3',4',5'-tetrachloro-4- biphenylol (2); and 2',3',4',5'-tetrachloro-3-biphenylol (3)]; three monochlorobiphenylols [5-chloro-2-biphenylol (5), 3-chloro-2-biphenylol (6); and 2-chloro-4-biphenylol (7)] and a tetrachlorobiphenyldiol [3,3',5,5'-tetrachloro-4,4'-biphenyldiol (4) on respiration, adenosine triphosphatase (ATPase) activity, and swelling in isolated mouse liver mitochondria have been investigated. Tetrachlorobiphenylols (1-3) and the tetrachlorobiphenyldiol (4) inhibited state-3 respiration in a concentration-dependent manner with succinate as substrate (flavin adenine dinucleotide [FAD]-linked) and the tetrachlorobiphenyldiol (4) caused a more pronounced inhibitory effect on state-3 respiration than the other congeners. The monochlorobiphenylols 5-7 were less active as inhibitors of state-3 mitochondrial respiration and significant effects were observed only at higher concentration (greater than or equal to 0.4 microM). However, in the presence of the nicotinamide adenine dinucleotide (NAD)-linked substrates (glutamate plus malate), hydroxylated PCBs (1-7) significantly inhibited mitochondrial state-3 respiration in a concentration-dependent manner. Compounds 5, 6, and 7 uncoupled mitochondrial oxidative phosphorylation only in the presence of FAD-linked substrate as evidenced by increased oxygen consumption during state-4 respiratory transition, stimulating ATPase activity, releasing oligomycin-inhibited respiration, and inducing mitochondrial swelling (5, 6, and 7). Tetrachlorobiphenylols 1, 2, and 3 had no effect on mitochondrial ATPase activity while the tetrachlorobiphenyldiol, 4, decreased the enzyme activity. The possible inhibitory site of electron transport by these compounds and their toxicologic significance is discussed.
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PMID:Effects of hydroxylated polychlorinated biphenyls on mouse liver mitochondrial oxidative phosphorylation. 183 67

Haemonchus contortus, incubated in 10 micrograms/ml and 50 micrograms/ml concentrations of Nilzan and albendazole in Tyrode solution were stained for histoenzymatic demonstration of various phosphatases, oxido-reductases and esterases. The intestine showed major alterations after drug treatments. The alkaline phosphatases (AkPase), adenosine triphosphatase (ATPase), glucose-6-phosphatase, succinic dehydrogenase (SDH), glutamate dehydrogenase (GDH), reduced nicotinamide adenine dinucleotide phosphate diaphorase and reduced nicotinamide adenine dinucleotide diaphorase showed a decreased activity in intestine after Nilzan treatment, whereas lactic dehydrogenase (LDH), glucose-6-phosphate dehydrogenase (G-6-PD) and monoamine oxidase resisted increased reaction. The albendazole treatment resulted in altered distribution pattern of the AkPase, ATPase, SDH, and GDH; while LDH, G-6-PD, and non-specific esterases exhibited slightly enhanced activity in the epithelium. The functional significance of these changes has been fully discussed.
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PMID:Effect of Nilzan and albendazole on the absorptive surfaces of Haemonchus contortus (Nematoda)--a histoenzymic study. 196 79

The technique of fluorescence quenching by the non-ionic quenchers acrylamide and nicotinamide has been used to probe the accessibility of the environmentally sensitive N-(bromoacetyl)-N'-(1-sulpho-5-naphthyl) ethylenediamine (1,5-Br-AEDANS) fluorophore attached to either Cys-177 of the A1-light chain or the SH1 thiol (Cys-707) of the myosin subfragment (S1) heavy chain. Neither quencher caused any detrimental effects to the ATPase activities of S1 under the conditions of the experiments. It was found that the fluorophore on the isolated light chain was highly exposed to solvent and although this exposure was reduced on hybridization into S1(A1-AEDANS), the probe was still accessible to solvent. This exposure was unaltered by formation of binary complexes with either Mg.ATP or actin or by the formation of a weakly associated acto-S1 complex (in which the Cys-697 and Cys-707 residues of S1 were crosslinked with p-phenylenedimaleimide). The lack of corresponding change in lambda max of emission and quantum yield supported the quenching date and indicated that actin neither binds directly to this region nor induces any significant conformational changes in this locality despite the observation that the A1-Cys-707 moves some 3 nm closer to a point on actin in the weak-binding state (Trayer, H.R. and Trayer, I.P. (1988) Biochemistry, 27, 5718-5727). Parallel experiments with the fluorophore attached to the Cys-707 of the S1 indicated that this region was less accessible to solvent than the light chain thiol despite its ease of labelling. This exposure was not significantly altered by binary complex formation with actin and Mg.ATP, although spectral changes in the absence of quencher support the notion that some conformational change is occurring in this region.
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PMID:Dynamic quenching studies of fluorophore-labelled myosin subfragment 1 and its alkali light chain subunits. 202 38


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