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)

In the gastrocnemius muscle of cat and rat, staining for oxidative enzymes differentiated three fiber types (A,B,C) and staining for adenosine triphosphate at pH 9.4 differentiated two fiber types (I, II) with a reliability of 90% and 98%, respectively. In cat 96% and in rat 90% of the fibers were typed identically after staining for nicotinamide adenine dinucleotidelinked lactic dehydrogenase (LDH) and succinic dehydrogenase (SDH). When differentiated by staining for LDH, A and B fibers were of type I. IN RAT, 80-90% OF ALL FIBERS WERE OF TYPE 22, COMPPRISING A, B and C fibers. Type I fibers stained for LDH intensely as did C fibers of type II, but stained intermediately for SDH. The degree of staining was measured by photometry. When fibers were stained for LDH, histograms of density showed three peaks corresponding to A, B and C fibers in cat, but only two peaks corresponding to A and C fibers in rat, In cat and rat, the densities of A, B and C fibers belonged to different populations. In soleus muscle of cat and rat stained for LDH, menadione-linked alpha-glycerophosphate dehydrogenase and adenosine triphosphatase at pH 9.4, the degree of staining differed from thatin any type of fiber in gastrocnemius muscle
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PMID:Histochemical fiber typing and staining intensity in cat and rat muscles. 12 97

The response of rat gastrocnemius muscle fibers to chronic streptozotocindiabetes was studied. Transverse sections of this muscle from normal and diabetic rats were histochemically assayed for reduced diphosphopyridine nucleotide-diaphorase, myofibrillar adenosine triphosphatase, mitochondrial alpha-glycerophosphate dehydrogenase, beta-hydroxybutyrate dehydrogenase, and alkaline phosphatase activities. Cross-sectional areas of the fiber types were measured, and fiber capillarization and populations estimated. Chemically-induced diabetes appeared to have little effect on the metabolic or morphological properties of slow-twitch fibers. However, a general dedifferentiation occurred in the 2 fast-twitch fiber populations. There was a loss of oxidative potential in the fast-twitch-oxidative-glycolytic fibers, and a significant decrease in size in the fast-twitch-glycolytic fibers. No change in the proportions of slow- and fast-twitch fibers in the muscles of diabetic rats occurred. It is concluded that hypoinsulinism has differential effects on the 3 fiber types in heterogeneous rat skeletal muscle, and that slow-twitch fibers are least affected by the diabetic condition.
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PMID:Histochemical properties of skeletal muscle fibers in streptozotocin-diabetic rats. 12 6

Muscle samples were obtained from the gastrocnemius of 17 female and 23 male track athletes, 10 untrained women, and 11 untrained men. Portions of the specimen were analyzed for total phosphorylase, lactic dehydrogenase (LDH), and succinate dehydrogenase (SDH) activities. Sections of the muscle were stained for myosin adenosine triphosphatase, NADH2 tetrazolium reductase, and alpha-glycerophosphate dehydrogenase. Maximal oxygen uptake (VO2max) was measured on a treadmill for 23 of the volunteers (6 female athletes, 11 male athletes, 10 untrained women, and 6 untrained men). These measurements confirm earlier reports which suggest that the athlete's preference for strength, speed, and/or endurance events is in part a matter of genetic endowment. Aside from differences in fiber composition and enzymes among middle-distance runners, the only distinction between the sexes was the larger fiber areas of the male athletes. SDH activity was found to correlate 0.79 with VO2max, while muscle LDH appeared to be a function of muscle fiber composition. While sprint- and endurance-trained athletes are characterized by distinct fiber compositions and enzyme activities, participants in strength events (e.g., shot-put) have relatively low muscle enzyme activities and a variety of fiber compositions.
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PMID:Skeletal muscle enzymes and fiber composition in male and female track athletes. 12 49

The histochemical activities of succinic dehydrogenase (SDH), myofibrillar Adenosine triphosphatase (ATPase) and alpha glycerophosphate dehydrogenase were studied in serial sections of rat vastus lateralis (red) (RVL), gastrocnemius and diaphragm muscles. Three main fibre-types were distinguished. The "Type I" fibres of RVL and gastrocnemius muscles fell into two distinct groups: one category--"Type IA" showed very low ATPase activity. The second category of "Type IB" fibres displayed moderate ATPase reaction. The "Type IA" fibres were divisible into two sub-groups when tested for SDH reaction. "Type IA1" fibres possessed a homogenous distribution of diformazan granules throughout the fibre: "Type IA2" fibres displayed characteristic "moth-eaten" pattern of diformazan localization. The diaphragm muscle did not show either "Type IB" or "Type IA2" varieties. The great majority of TypeI fibres were sub-type IA1 in the three fast muscles studied. It is also demonstrated here that an inherent heterogeneity exists between Type I filores of diaphragm and leg muscles in regard to alpha-GPD localization. This histochemical data emphasizes the fact that subdivision of TypeI striated muscle fibres of mammalian animals into two sub-types is only approximate and that a further subcategorization is possible.
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PMID:Histoenzymatic characterization of sub-types of type I fibres in fast muscles of rats. 14 58

The differentiation of fibre types in developing human skeletal muscle was studied. The material consisted of muscle samples from different muscles of 86 foetuses (abortions) between 12 weeks gestation and delivery and 50 children 1 day to 7 years old. The latter samples were obtained at surgery. Histochemical stains for myofibrillar ATPase were made after preincubations at pH 4.3, 4.6 and 10.3 in order to identify the subgroups A and B of type II fibres and undifferentiated fibres (type II C). Stains for glycogen and lipids were also performed as well as for NADH-diaphorase and alpha-glycerophosphate dehydrogenase. After 20 weeks gestation a few large size type I fibers could be found in some muscles, but not until after the 30th week were some type II A fibres seen. During the last 3 months of gestation a very rapid further differentiation occurred, but at delivery the differentiation process was still not completed. At birth 15-20% of the fibres were classified as undifferentiated. This picture only gradually changed with a slow increase in the number of type I, II A and II B fibres. The stains for metabolic enzymes and substrates were pale until late in foetal life when some distinction between fibre types became discernible.
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PMID:Enzyme histochemistry on skeletal muscle of the human foetus. 15 51

The histochemical activities of myofibrillar adenosine triphosphatase (ATPase), succinic dehydrogenase (SDH) and alpha glycerophosphate dehydrogenase (alpha-GPD) were studied in intrafusal muscle fibres of rat fast and slow muscles. The ATPase reaction was carried out after the three standard acid preincubations. The cold K2-EDTA preincubated ATPase reaction product was similar to that seen following the regular or alkali-preincubated ATPase reaction, except that the intermediate bag fibres exhibited much higher activity after cold K2-EDTA preincubation. Following either acetic acid solution or cold and room temperature K2-EDTA-preincubation, followed by the ATPase reaction, chain fibres of the fast muscles vastus lateralis and extensor digitorum longus exhibited a very low amount of reaction product as compared with those of the slow soleus. Veronal acetate and K2-EDTA preincubations (and equally preincubation in acetic acid solution) resulted in acid stable ATPase activity along the entire length of the typical bag fibres but only in the polar regions of the intermediate bag fibres. On the basis of differing alpha-GPD reaction, two sub populations of nuclear chain fibres were discovered in one spindle. It is a matter of conjecture, to what extent the histochemical differences of intrafusal fibres from fast and slow muscles reflects functional distinctions in the response to stretch of muscle spindles from fast and slow muscles.
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PMID:A histoenzymatic study of rat intrafusal muscle fibres. 15 74

(1) The histochemical staining pattern of succinic dehydrogenase (SDH) does not show unequivocal differentiation between the type I red and type II red fibres in mammalian striated muscles. (2) Since high biochemical activity of beta-hydroxybutyric dehydrogenase (beta-HOBDH) occurs in mitochondria of the type I red fibres, the histochemical localization of this enzyme may show a pattern of staining reciprocal to that seen for myofibrillar ATPase. (3) It remains to be confirmed that the type I red fibres, which are possibly slow-twitch physiologically, possess the highest concentration of myoglobin. The histochemical correlation of myoglobin and myofibrillar ATPase in serial sections should be studied. (4) In order to achieve a more realistic picture, various glycolytic and glycogenolytic enzymes should be incubated according to the gelatin film technique, or semipermeable membrane technique or collagen polypeptide technique. A histochemical correlation of phosphorylase, LDH, PFK, alpha-glycerophosphate dehydrogenase, and myofibrillar ATPase in adjacent muscle sections may throw light on the histochemical characteristics of the different fibre-types. (5) The specific histochemical demonstration of AMPase is achieved following preincubation of tissue sections. (6) ADPase has been demonstrated by the calcium precipitation technique only (GUTH and YELLIN, 1971). A number of studies claim, however, that ADPase is not demonstrable histochemically in muscle fibres. (7) The presence of magnesium ions is a prerequisite for the adequate histochemical demonstration of mitochondrial ATPase. The latter is inhibited almost completely by 40 mM Ca++ (when Mg++ is not added) at both neutral and alkaline pH values. (8) The histochemical activity of SR-AT-Pase seen as continuous reticula but without punctuate and sub-sarcolemmal staining possibly represents the extra ATPase of SR. (9) On the basis of myofibrillar ATPase reaction, an inherent heterogeneity, between the type II red and type II white may be recognized. In addition, the above fibre-types possess their respective sub-populations. (10) Following diK+ EDTA preincubation, some type II red fibres show selective lability. These are the mitochondria-rich fibres. Thus in the total absence of both punctuate and subsarcolemmal staining, the presence of mitochondrial ATPase activity under the histochemical conditions for myofibrillar ATPase is unlikely. (11) The reaction pattern of CK/ATPase (coupled reaction) at pH 6.9 is distinctly intermyofibrillar and unlike SDH-pattern. This reticular reaction is associated mainly with the SR and hence the importance of transphosphorylation in this organelle for the Ca++ uptake and muscle relaxation. (12) The CK/ATPase reaction at pH8.0 has shown important histoenzymatic characteristics. At this pH value the type I red fibres and slow-twitch soleus show myofibrillar reaction pattern. This identical histochemical behaviour suggests that type I red fibres are possibly slow-contracting...
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PMID:Histochemical characteristics of vertebrate striated muscle: a review. 18 61

We have screened the bloodstream form of Trypanosoma brucei for the presence of enzymes that could serve as markers for the microbodies and the highly repressed mitochondrion of this organism. None of seven known microbody enzymes were detected at all, but glycerol-3-phosphate oxidase, ATPase, isocitrate dehydrogenase, acid phosphatase and part of the hyperoxide dismutase and malate dehydrogenase activities were found to be particle-bound after fractionation of homogenates by differential centrifugation. Part of the ATPase activity was sensitive to oligomycin, an inhibitor of oxidative phosphorylation. This oligomycin-sensitive activity can serve as a specific marker for the mitochondria. More than 80% of the NAD+-linked glycerol-3-phosphate dehydrogenase in T. brucei was found to be particulate and latent. The enzyme could be activated by Triton X-100, by the combined action of sonication and salt, but not by salt alone, and partially by freezing and thawing. We conclude that the NAD+-linked glycerol-3-phosphate dehydrogenase is located inside an organelle.
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PMID:Particle-bound enzymes in the bloodstream form of Trypanosoma brucei. 19 9

We have studied the effect of 3,5,3'-triiodothyronine (T3) on the respiration of adult rat hepatocytes in primary monolayer culture prepared from hypothyroid rat liver. After addition of T3 to the culture medium at a concentration of 2 x 10(-7) M, oxygen consumption of the cultured cells increased detectably at 24 h and was maximal at 72--96 h, relative to control cultures (38.0 +/- 1.8 vs. 25.0 +/- 1.5 microliter/h.mg protein). The thyroid-responsive enzymes, Na+ + K+-activated adenosine triphosphatase (NaK-ATPase) and alpha-glycerophosphate dehydrogenase (GPD), each exhibited increased activity in response to T3, in parallel with the change in oxygen consumption, whereas the activity of Mg-dependent ATPase was unaffected. These responses to T3 were dose dependent over similar concentration ranges, the half-maximal response for each occurring at ca 8 x 10(-10) M. In thyroid-treated cells, the observed increase in respiration was almost completely (90%) inhibited after addition of ouabain (10(-3) M) to the culture medium. It was found also that a 4-h exposure of the cultured hepatocytes to T3 was sufficient to elicit a significant thermogenic response, measured at a time (48 h later) when T3 was no longer present in the medium. The response to T3 occurred in fully defined culture medium and was independent of the presence or absence of hypothyroid rat serum, corticosterone, or insulin, and cellular ATP was unaffected by T3 in concentrations up to 2 x 10(-7) M. The findings document that adult rat hepatocytes in primary monolayer culture respond directly to thyroid hormone; the increases in respiration and NaK-ATPase activity elicited by T3 were cotemporal and apparently coordinate.
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PMID:Thyroid thermogenesis in adult rat hepatocytes in primary monolayer culture: direct action of thyroid hormone in vitro. 22 Mar 77

1. Seven fractions sedimenting at between 3000 and 120000g-min were prepared from a rat liver homogenate by differential centrifugation in buffered iso-osmotic sucrose. The following measurements were carried out on each of these fractions: Ruthenium Red-sensitive Ca(2+) transport in the absence and in the presence of P(i) as well as in the presence of N-ethylmaleimide to prevent P(i) cycling, succinate-supported respiration in the absence and in the presence of ADP, the DeltaE and -59 DeltapH components of the protonmotive force, cytochrome oxidase, uncoupler-stimulated adenosine triphosphatase, alpha-glycerophosphate dehydrogenase, P(i) content and the effect on the ;resting' rate of respiration of repeated additions of a fixed Ca(2+) concentration. 2. Ca(2+) transport either in the presence or in the absence of added P(i) and in the presence of N-ethylmaleimide exhibits significantly higher rates in the fraction sedimenting at 8000g-min. By contrast, respiration in the presence or in the absence of added ADP and the values for DeltaE and -59 DeltapH were similar in those fractions sedimenting between 4000 and 20000g-min, indicating that the driving force for Ca(2+) transport was similar in each of these fractions. 3. Experiments designed to determine the capacity of the individual fractions for Ca(2+), as measured by the effect of repeated additions of Ca(2+) on the resting rate of respiration, showed that fraction 2, i.e. that sedimenting at 8000g-min, also exhibited the greatest tolerance towards the uncoupling action of the ion. 4. Of the three enzyme activity profiles, only that of alpha-glycerophosphate dehydrogenase was similar to that of Ca(2+) transport. Because previous workers have assigned this enzyme to loci in the inner peripheral membrane [Werner & Neupert (1972) Eur. J. Biochem.25, 379-396], it is concluded that the Ruthenium Red-sensitive Ca(2+)- transport system also is located in this domain of the inner membrane. The relation of these findings to the mechanisms of mitochondrial Ca(2+) transport and the biogenesis of mitochondria is discussed.
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PMID:Submitochondrial location of ruthenium red-sensitive calcium-ion transport and evidence for its enrichment in a specific population of rat liver mitochondria. 72 72


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