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:3.2.1.31 (beta-glucuronidase)
7,680 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The application of zonal centrifugation to the analysis of homogenates of cardiac and skeletal muscle permits selection of fractions that are enriched in markers for lysosomes, sarcolemma, sarcoplasmic reticulum, and mitochondria. The method of disruption of normal and pathological tissue alters significantly the distribution of total protein and peaks of enzymatic activity on the gradient. Total activities of cathepsin, N-acetyl-beta-glucosaminidase, beta-glucuronidase, and para-nitrophenylphosphatase are distributed at different concentrations of sucrose on the gradient. Beta-Glucuronidase appears to "mark" the sarcoplasmic reticulum, as well as lysosomes, of skeletal muscle, para-Nitrophenylphosphatase, a common marker of acid phosphatase of lysosomes, is enriched in those fractions of cardiac muscle containing the highest specific activity of ouabain-inhibited Na-K-ATPase. Thus, these two enzymes appear to have a localization in at least two separate organelles. On the other hand, these results may indicate the isolation of several "populations" of lysosomes that are associated constantly with distribution peaks of other organelles. In any event, attempts to correlate changes in structure of organelles of normal and pathological specimens of tissue with functional impairment, e.g., Ca2+ uptake, activity of Na-K-ATPase, etc., must include consideration of dual localization of enzymatic markers or cross contamination by populations of other organelles.
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PMID:Lysosomes of cardiac and skeletal muscle: resolution by zonal centrifugation. 17 16

The activities of several lysosomal enzymes were assayed in control and in exercise-hypertrophied cardiac muscle of mice (Mus musculus). The repeated running program increased the activity of beta-glucuronidase (16.1%) in mouse cardiac muscle. Decreased activities of beta-N-acetylglucosaminidase (10.8%), acid ribonuclease (10.7%), and arylsulphatase (14.2%) were observed in the hypertrophied myocardium. The activities of acid deoxyribonuclease, cathepsin C, cathepsin D, and p-nitrophenylphosphatase as well as the activities of citrate synthase and cytochrome c oxidase, mitochondrial enzymes, were unaffected in cardiac muscle. We suggest that lysosomal enzyme responses are selective and highly different in physiologically and pathologically induced cardiac hypertrophies.
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PMID:Changes in lysosomal enzyme activities in exercise-induced cardiac hypertrophy of mice. 622 47

We studied the effects of running-training, heavy exercise and termination of training on the heart weight, the ratio heart to body weight and the cardiac muscle activities of actomyosin ATPase, citrate synthase, succinate dehydrogenase, cytochrome c oxidase, malate dehydrogenase, adenylate kinase and beta-glucuronidase with adult male NMRI-mice. Stable hypertrophy (6-7%), estimated by the ratio heart or ventricle weight to body weight, was achieved by 28 exercises and it was dependent on the running speed (20 vs. 25 m X min-1). The withdrawal of training for 5-61 days did not permanently decrease the heart weight or the heart to body weight ratio to the level of sedentary controls. The activity of enzymes of energy metabolism or actomyosin ATPase were not affected by training, heavy exercise or terminated training. beta-glucuronidase activity slightly (20-25%) increased in the trained animals and remained at a higher level during the period of terminated training. The results suggest that the capacity for aerobic metabolism of normal mice heart is sufficient to meet the enhanced demand for ATP imposed by running-training and that the heart enlargement occurs in equal proportions with the enzymatic potential of the cardiac tissue.
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PMID:Selected enzyme activities in mouse cardiac muscle during training and terminated training. 623 64

Study of the age-related changes in cardiac muscle of 5, 10, 15, 20, and 25 months old albino rats showed that the muscle mass decreased by 10% while the ratio of the weight of cardiac muscle to body weight decreased by 30% between 5 and 25 months. Autolytic and proteolytic activity of sarcoplasmic proteins increased remarkably (70% and 200%, respectively) between 5 and 25 months of age. Although the total protein content decreased, the amount of fibrous protein (collagen) increased by 50%. Levels of salt soluble and labile collagen (free hydroxyproline released at 65 degrees C in Ringer solution) decreased by 65% and 50%, respectively, while insoluble collagen increased by 180% with advance in age from 5 to 25 months. Increase in acid soluble collagen was seen only up to 20 months of age. The acid mucopolysaccharide content decreased, whereas the activity of beta-glucuronidase showed an increase from 110-148 units between 10 and 15 months of age. beta-N-acetylglucosaminidase increased by 25% as the age increased from 5 to 25 months.
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PMID:Age-related changes in cardiac muscle of rat. 644 63

Effects of a short-term vitamin E deficiency on some lipid peroxidative properties were investigated in mouse cardiac and skeletal muscles. The concentration of vitamin E decreased 35.8% in 5 weeks and 61.2% in 12 weeks in skeletal muscle. The corresponding decrease in cardiac muscle was 65.7% in 12 weeks. Simultaneously the susceptibility of muscle homogenates to in vitro lipid peroxidation increased with 48.6% (5 weeks) and 44.5% (12 weeks) in skeletal muscle and with 101.8% (12 weeks) in cardiac muscle. Highly significant negative correlations were observed between the concentration of vitamin E and in vitro lipid peroxidation in cardiac and skeletal muscles. Also the sensitivity to Fe2+-induced peroxidation was increased in skeletal muscle after the deficiency of 5 weeks. The total contents of peroxidizable lipids (Fe2+-induction) were significantly (approx. 20%) decreased after 12 weeks in cardiac and skeletal muscles. The concentration of lipofuscin was unaffected in both muscles of vitamin E-deficient mice. Vitamin E deficiency (5 weeks) decreased the activity of selenium-dependent glutathione peroxidase in skeletal muscle but did not affect the activities of catalase and beta-glucuronidase and the concentrations of protein, reduced glutathione and total sulfhydryl groups. These results show that a short-term vitamin E deficiency affects the peroxidative properties of cardiac and skeletal muscles and may thus expose the muscles to peroxidation injuries.
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PMID:Vitamin E deficiency and the susceptibility to lipid peroxidation of mouse cardiac and skeletal muscles. 652 97

The activities of beta-glucuronidase and cathepsin D and the protein concentration were assayed from brain, kidney, liver, cardiac muscle and skeletal muscle (m. rectus femoris) samples from mice (Mus musculus) 1, 3, and 6 days after intermittent exhaustive (duration 100-145 min) and submaximal prolonged (duration 9 hr) running on treadmill. The activity of beta-glucuronidase in skeletal muscle strongly increased being the highest 3 days after both exertions. Cathepsin D activity also slightly increased. In cardiac muscle beta-glucuronidase activity was unaffected. Cathepsin D activity slightly increased 3 days after intermittent exhaustive exercise. The specific activities of beta-glucuronidase and cathepsin D in the liver increased 1 day after the both exertions. Simultaneously the protein concentration decreased. In the kidney beta-glucuronidase activity and protein concentration were unaffected but cathepsin D activity decreased 1 day after intermittent exhaustive exercise. In the brain protein concentration transiently decreased 3 days after the exertions. beta-Glucuronidase activity transiently decreased 1 day after intermittent exercise thereafter increasing 6 days afterwards above the control level. Cathepsin D activity decreased 1 day after intermittent exercise but was unaffected after prolonged submaximal exercise. Physical stress affected to varying extent the acid hydrolase activities in all organs studied.
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PMID:Acid hydrolase activity in tissues of mice after physical stress. 664 Nov 64

Male NMRI-mice, aged 3, 6, 9, and 12 months, were made to run for a period of 4 4 at a speed of 13.5 m/min on a motor-driven treadmill, 5 days after exertion, selected enzymatic estimates of acid and alkaline proteolytic as well as energy metabolic capacities were analyzed from the cardiac muscle and from the red and white parts of m. quadriceps femoris (MQF). The activities of alkaline and myofibrillar proteases increased most considerably in skeletal muscles with age. Cathepsin D and beta-glucuronidase activities were less affected in both muscles. Prolonged running increased the activities of cathepsin D, dipeptidyl aminopeptidase I and beta-glucuronidase in the white and, especially in the red part of MQF. This stimulation of acid hydrolytic capacity was more prominent at the ages of 3 and 6 months than in the older animals. The estimates of alkaline proteolytic or energy metabolic capacities were not affected by prolonged running. In cardiac muscle, no significant changes were recorded in acid hydrolytic or energy metabolic capacity. Histological observation showed no necrosis or other pathological phenomena in the proximal part of m. rectus femoris after excretion. We suggest that the increased acid proteolytic capacity is involved in subcellular regenerative processes of skeletal muscle fibres. The smaller lysosomal response of older mice may indicate a reduced potential capacity for cellular repair.
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PMID:Effects of age and prolonged running on proteolytic capacity in mouse cardiac and skeletal muscles. 702 79

Acid proteolytic capacity in mouse cardiac muscle and in predominantly white (distal head of m. vastus lateralis) or predominantly red (proximal red heads of m. vastus lateralis, m. v. medialis, and m. v. intermedius) skeletal muscle was estimated 5 days after 3 h, 6 h or 9 h prolonged running at a speed of 13.5 m/min. The activities of acid protease and beta-glucuronidase together with the rate of acid autolysis considerably increased in both skeletal muscle types, especially in red muscle, but did not increase in cardiac muscle. Acid proteolytic capacity and beta-glucuronidase activity increased in relation to the duration of running. Protein content and oxidative capacity (the activities of citrate synthase and malate dehydrogenase) decreased in red skeletal muscle after 6 h and 9 h running. In white muscle only protein content slightly decreased after 9 h running. No corresponding changes were observed in cardiac muscle. Histopathological changes were traced in mixed skeletal muscle (m. rectus femoris). Necrotic lesions were observed in the red superficial area of m. rectus femoris after 6 h and, in particular, after 9 h running. The results show that prolonged submaximal running also produces lethal and sublethal skeletal muscle fibre injuries, as well as exhaustive exercise or temporary ischaemia as reported earlier. It is suggested that sublethal injuries precede lethal ones and that acid proteolytic capacity increases especially in the sublethally injured muscle fibres.
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PMID:Acid proteolytic capacity in mouse cardiac and skeletal muscles after prolonged submaximal exercise. 719 62

Acid hydrolase activities in skeletal and cardiac muscle were studied 5, 10 and 20 days after exhaustive intermittent running by untrained and endurance-trained mice. Exhaustion increased the activities of cathepsin D, beta-glucuronidase and ribonuclease, but not that of p-nitrophenylphosphatase in skeletal muscle of untrained mice. Activities were highest on the fifth day after exhaustion and decreased during the following two weeks. More intensive loading produced no changes in acid hydrolytic capacity in skeletal muscle of endurance-trained mice. Acid hydrolase activities in cardiac muscle of both untrained and trained mice were unaffected by exhaustive running. It is suggested that exhaustive running causes both lethal and sublethal hypoxic fiber injuries in the skeletal muscle of untrained mice but not in that of endurance-trained mice or in the cardiac muscle of animals of either group. These injuries manifest themselves as fiber necrosis (lethal) and as increased acid hydrolytic capacity in surviving fibers (sublethal).
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PMID:Acid hydrolase activities in mouse cardiac and skeletal muscle following exhaustive exercise. 719 24

THE COMPOSITION OF ISOLATED NUCLEI AND CELL PREPARATIONS FROM TISSUES OF CALF, BEEF, HORSE, AND FOWL WAS STUDIED WITH RESPECT TO THE FOLLOWING COMPONENTS: 1. Liver and kidney arginase, catalase, and uricase; pancreatic lipase and amylase; cardiac muscle myoglobin; erythrocyte hemoglobin; intestinal alkaline phospharase. These are referred to as "special" components in view of their characteristically restricted distribution reflecting the differentiated nature of the tissues in question. 2. Esterase, beta-glucuronidase, alkaline and nucleotide phosphatases, adenosine deaminase, guanase, and nucleoside phosphorylase. These are enzymes of general distribution. The differences in nuclear composition noted with respect to the "special" components, together with the broad variability in nuclear activity found for enzymes of general distribution, led to the conclusion that nuclei are differentiated structures. The following distribution was observed: 1. "Special" components: Hemoglobin was found to be present in fowl and goose erythrocyte nuclei, but myoglobin was entirely absent from heart muscle nuclei; of the special enzymes listed, only catalase and arginase appeared to be concentrated in some of the nuclei. There was no significant nuclear concentration of lipase, amylase, uricase, or alkaline phosphatase. No simple relationship was found between the concentration of a special enzyme in a tissue and its activity in the corresponding nuclei. For example, arginase activity, which is high in mammalian liver and in fowl kidney, was found in liver, not kidney, nuclei. Similarly, catalase activity was demonstrated only in mammalian liver nuclei, although, in mammals, both liver and kidney are rich sources of this enzyme. 2. Enzymes of general distribution fell into three classes: (a) Those present in low concentrations, if at all, in the nuclei-alkaline phosphatase, the nucleotide phosphatases) and beta-glucuronidase. (b) Those present in nuclei in varying concentrations-esterase. (c) Those present in high proportions in most nuclei-adenosine deaminase, nucleoside phosphorylase, and guanase. The exceptionally low nuclear activity of intestinal mucosa with respect to these enzymes was discussed in relation to physiological considerations. The response of nuclei to changes in physiological state was demonstrated by experiments on starvation. The outstanding aspect of this response was a change in nuclear enzymatic activity opposing that observed in the cytoplasm. A comparison of fetal and adult mucosa cells led to the following tentative interpretation of the observed intracellular enzyme distribution: In cells tending to moribundity, as in those subjected to starvation, relative nuclear enzymatic activity falls. The occurrence of special enzymes in nuclei was considered in terms of differentiation, and the high nuclear concentration of the nucleoside-specific enzymes was interpreted in terms of general nuclear metabolic activity.
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PMID:Some enzymes of isolated nuclei. 1489 35


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