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)

Zinc deficiency (ZD) is teratogenic in rats, and fetal skeletal defects are prominent. To elucidate further the effects of maternal ZD in the fetal skeleton, we performed a morphological and histochemical study of tibial growth plate (GP) in ZD rat fetuses. The histochemical study included the identification of calcium, of hydrolytic enzymes associated with the process of calcification, and of oxidative enzymes related to energy production and to the synthesis of proteoglycans. Pregnant Sprague-Dawley rats were fed (1) a control diet (76.4 micrograms Zn/g diet) ad libitum (group C), (2) a zinc-deficient diet (0 micrograms/g) ad libitum (group ZD), or (3) the control diet pair-fed to the ZD rats (group PF). On day 21 of gestation, laparotomies were performed, the fetuses were removed, and fetal tibiae obtained. Specimens were stained with hematoxylin-eosin (H&E) and Masson Trichrome and were processed for identification of alkaline phosphatase, adenosine triphosphatase, succinic dehydrogenase, NADH dehydrogenase, and calcium. The morphologic patterns found in ZD fetal tibiae indicated defects in various cell types implicated in bone metabolism. Staining for hydrolytic enzymes revealed alterations in the size and distribution of matrix vesicles and a weaker staining for ATPase in ZD fetuses. Staining for oxidative enzymes was overall more intense in ZD fetal tibiae. ZD fetuses also presented irregular and defective calcification. These findings indicate that severe maternal ZD in the rat results in structural and functional alterations in the GP of fetal bone, leading to a defective endochondral ossification.
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PMID:Changes in the fetal tibial growth plate secondary to maternal zinc deficiency in the rat: a histological and histochemical study. 196 89

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 adaptation of a slow (soleus, Sol) and a fast (medial gastrocnemius, MG) skeletal muscle to spaceflight was studied in five young male rats. The flight period was 12.5 days and the rats were killed approximately 48 h after returning to 1 g. Five other rats that were housed in cages similar to those used by the flight rats were maintained at 1 g for the same period of time to serve as ground-based controls. Fibers were classified as dark or light staining for myosin adenosine triphosphatase (ATPase). On the average, the fibers in the Sol of the flight rats atrophied twice as much as those in the MG. Further, the fibers located in the deep (close to the bone and having the highest percentage of light ATPase and high oxidative fibers in the muscle cross section) region of the MG atrophied more than the fibers located in the superficial (away from the bone and having the lowest percentage of light ATPase and high oxidative fibers in the muscle cross-section) region of the muscle. Based on quantitative histochemical assays of single muscle fibers, succinate dehydrogenase (SDH) activity per unit volume was unchanged in fibers of the Sol and MG. However, in the Sol, but not the MG, the total amount of SDH activity in a 10-microns-thick section of a fiber decreased significantly in response to spaceflight. Based on population distributions, it appears that the alpha-glycerophosphate dehydrogenase (GPD) activities were elevated in the dark ATPase fibers in the Sol, whereas the light fibers in the Sol and both fiber types in the MG did not appear to change. The ratio of GPD to SDH activities increased in the dark (but not light) fibers of the Sol and was unaffected in the MG. Immunohistochemical analyses indicate that approximately 40% of the fibers in the Sol of flight rats expressed a fast myosin heavy chain compared with 22% in control rats. Further, 31% of the fibers in the Sol of flight rats expressed both fast and slow myosin heavy chains compared with 8% in control rats. Immunohistochemical changes in the MG were minimal. These data suggest that the magnitude and direction of enzymatic activity and cell volume changes are dependent on the muscle, the region of the muscle, and the type of myosin expressed in the fibers. Further, the ability of fibers to maintain normal or even elevated activities per unit volume of some metabolic enzymes is remarkable considering the marked and rapid decrease in fiber volume.
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PMID:Metabolic and morphologic properties of single muscle fibers in the rat after spaceflight, Cosmos 1887. 213 39

As a series of studies on postmortem changes in the fine structure of porcine muscle, activity of two mitochondrial marker enzymes, succinate dehydrogenase (SDH) and magnesium dependent adenosine triphosphatase (Mg-ATPase), was measured and localized in cardiac, red and white muscles stored at 4 degrees C, -18 degrees C or -80 degrees C. The postmortem loss of SDH activity was most remarkable in cardiac muscle. The variation of SDH activity was proportional to the amount of absolute activity. The postmortem change of Mg-ATPase was more variable than SFH, though the activity was well preserved up to 15 weeks in all three types of porcine muscle stored at -80 degrees C. The loss of Mg-ATPase was most remarkable in red muscle stored at -18 degrees C or -80 degrees C. Cytochemical localization of SDH was between the outer and the inner mitochondrial membranes while that of Mg-ATPase was on the inner surface or matrix side of the inner membrane. Those localization was not altered by the difference in temperature and the duration of storage.
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PMID:Post-mortem changes in cytochemical localization and enzymological measurement of marker enzymes of the mitochondria, SDH and Mg-ATPase, of porcine muscle stored at 4 degrees C, -18 degrees C, or -80 degrees C. 213 22

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

Chronic infection of woodchucks with woodchuck hepatitis virus (WHV) was associated with the development of hepatitis, foci of altered hepatocytes and hepatocellular adenomas and carcinomas. The cytomorphological and cytochemical analysis permitted the identification of three different types of focal lesions; namely, glycogen-storage foci, mixed-cell foci and intermediate-cell foci, each showing a characteristic pattern. The cells of the glycogen-storage foci had clear to acidophilic cytoplasm, and were overloaded with glycogen. They showed a marked elevation in the activity of glucose-6-phosphate dehydrogenase (G6PDH) and malate dehydrogenase (MDH), increased activity of succinate dehydrogenase (SDH), glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and glycerol-3-phosphate dehydrogenase (G3PDH), reduction in the activity of glycogen phosphorylase (PHO), glucose-6-phosphatase (G6Pase), adenosine triphosphatase (ATPase) and adenyl cyclase (ADC), and unchanged activity of glycogen synthase (SYN) and gamma-glutamyl transferase (GGT). The mixed-cell foci mainly consisted of basophilic cells poor in glycogen, but were intermingled with cells containing glycogen. These foci were characterized by a marked decrease in activity of PHO, SYN, G6Pase, G6PDH, ATPase and ADC, and increased activity of GGT, SDH, MDH and GAPDH. The intermediate-cell foci consisted of cells with both basophilic and glycogenotic cytoplasmic compartments, and showed a similar enzyme histochemical profile to the mixed-cell foci, with slight differences in the degree of elevation or reduction of some enzymes. The phenotypic similarities and the close spatial relationship between the foci of altered hepatocytes, and the hepatocellular adenomas and carcinomas in WHV-infected woodchucks, suggest that these lesions are preneoplastic. The focal morphological and metabolic aberrations emerging during hepatocarcinogenesis in WHV-infected woodchuck, are in principle similar to those identified in the course of chemical hepatocarcinogenesis in various species. The focal metabolic aberrations apparently represent a general biological response of the liver parenchyma to oncogenic agents and are closely linked to neoplastic transformation of the hepatocytes.
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PMID:Phenotypic patterns of preneoplastic and neoplastic hepatic lesions in woodchucks infected with woodchuck hepatitis virus. 215 41

Primary cell culture system from middle-ear epithelium of the guinea pig was established in defined condition. Mucosal cells were dispersed with enzymatic procedure and over 90% of the cell viability was obtained. Collagen gel and fibronectin coated Thermanox plate were used as culture substrates, and cultured cells on both materials formed confluent epithelial linings. Histochemical localization of succinate dehydrogenase, cytochrome oxidase and adenosine triphosphatase in mitochondria were examined. Cultured ciliated cells and some non-ciliated cells with numerous microvilli showed strong activities of succinate dehydrogenase and cytochrome oxidase. Also in vivo, normal ciliated epithelium near the eustachian tube in the middle-ear cavity of the guinea pig revealed strong mitochondrial metabolic activities. We concluded that this system would be useful for the study of cellular multiplication and differentiation systems of the middle-ear epithelium.
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PMID:[Cell culture of middle-ear epithelium of the guinea pig--histochemical localization of mitochondrial enzymatic activities in cultured cells]. 215 82

Administration of different doses of L-thyroxine (T4) and triiodo-L-thyronine (T3) in vivo in G. carnosus stimulated the activities of cytochrome oxidase, alpha-glycerophosphate dehydrogenase (alpha-GPDH), succinate dehydrogenase (SDH), and Mg2+ adenosine triphosphatase (Mg2+ ATPase) and inhibited the activity of malate dehydrogenase (MDH). While a low dose of thiouracil administration produced a stimulatory effect on cytochrome oxidase and alpha-GPDH activities, a higher dose of thiouracil significantly inhibited the activities of cytochrome oxidase, alpha-GPDH, SDH, Mg2+ ATPase, and MDH. Injection of T4 or T3 into thiouracil-treated animals significantly restored the stimulatory effect of thyroid hormones on oxidative enzyme activities. It is suggested that thyroid hormones in vivo increase and that thiouracil decreases the oxidative capacity of hepatic mitochondria of G. carnosus.
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PMID:Stimulation of oxidative metabolism by thyroid hormones in an apodan amphibian, Gegenophis carnosus (Beddome). 216 65

The influences of iron deficiency on the cochlear iron enzymes and adenosine triphosphatase were studied in 68 iron-deficient rats and 68 control rats (normal and with chronic anemia). A disorderly or topographic distribution and reduction or disappearance of the cochlear succinic dehydrogenase and peroxidase reaction products were found in 37.8% of the rats fed on a basic iron-deficient diet for 14 to 100 days. The activity of cochlear sodium-potassium-dependent adenosine triphosphatase in iron-deficient rats was slightly increased, compared to that in normal controls. These results suggest that iron deficiency would produce significant abnormalities of succinic dehydrogenase and peroxidase activity, which in turn would disturb cell respiration and initiate peroxidative damage to the inner ear cells, result in sensorineural hearing loss, or provide a pathologic basis for cochlear deafness.
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PMID:Changes in the cochlear iron enzymes and adenosine triphosphatase in experimental iron deficiency. 217 94

Ten healthy sedentary Thoroughbreds with previous race training experience were trained conventionally for 9 weeks. Muscle biopsy samples were obtained before and after training and after 6 weeks of detraining pasture rest. Biopsy samples were obtained from the right deltoid, triceps, vastus lateralis, middle gluteal, biceps femoris, and semitendinosus muscles. The deep-frozen biopsy samples were analyzed for activities of succinate dehydrogenase (SDH), 3-hydroxy-acylcoenzyme A dehydrogenase (HAD), and phosphorylase (PHOS) and for glycogen concentration. The triceps and gluteal muscle samples were also serially sectioned and stained for myofibrillar actomyosin adenosine triphosphatase (ATPase) activity after alkaline (pH 10.3) and sequential acidic (pH 4.34) ATPase inactivation. Fiber types I (alkaline preincubation), IIA1, IIA2, and IIA3 (sequential acidic preincubation over 5 minutes) were identified and were evaluated for fiber-type distribution and fiber areas. Increases in response to training were observed in deltoid and vastus muscle SDH and gluteal muscle HAD activities, and deltoid muscle glycogen concentration (P less than 0.05 to P less than 0.01). Changes in PHOS activity were not observed. Type-IIA1, -IIA2, and -IIA3 fiber areas in triceps muscle were increased in response to training (P less than 0.05 to P less than 0.01). Changes in fiber-type distribution did not occur in response to training. Changes in muscle enzyme activities, glycogen concentration, fiber types, and fiber areas were not seen from posttraining to detraining. Further increases were observed when detraining values were compared with pretraining values in deltoid, triceps, vastus, gluteal, and biceps femoris muscle SDH activities and in gluteal muscle glycogen concentration (P less than 0.05 to P less than 0.01).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Muscle responses of thoroughbreds to conventional race training and detraining. 236 47


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