Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.31 (beta-glucuronidase)
 7,680 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The present paper was designed to the study of cerebral edema induced by intracarotid infusion of dinitrophenol. The determinations included variations in three lysosomal enzymes (acid phosphatase, cathepsin C and beta-glucuronidase), Na+-K+-ATP-ase, changes in cerebral RNA and protein concentrations and the synthesis of these macromolecules in vitro. In experimental brain edema a drastic drop in the activity of lysosomal enzymes took place. The acid phosphatase decreased to less than 30% of controls. Cathepsin C and beta-glucuronidase were reduced about 30% and 50% of control levels respectively. Protein concentration in the cerebral tissue also decreased by more than 50%. The concentration of RNA, RNA synthesis, and the level of Na+-K+-ATP-ase remained unchanged. Protein synthesis was stimulated by 75% (against controls). All these phenomena were suppressed when the animals subjected to the action of dinitrophenol were concomitantly treated with the antiacidotic substance, tris (hydroxymethyl) aminomethane.
 ...
PMID:Biochemical changes in the rat brain associated with dinitrophenol-induced brain edema. 15 61

The activity of eight acid hydrolases and two energy metabolism enzymes were assayed from homogenates of predominantly red (proximal heads of m. vastus lateralis, m. vastus medialis, and m. vastus intermedius) and predominantly white (distal head of m. vastus lateralis) skeletal muscle of mice belonging to one of the following groups: 1) sedentary controls, never trained or exhausted; 2) exhausted controls, exhausted once by running on a treadmill 5, 10, or 20 days before killing; 3) trained mice, exercising until killed; 4) exhausted trained mice, exercising until exhausted 5, 10 or 20 days before killing, not exercising during that period; and 5) detrained mice, terminating training 5, 10, or 20 days before killing. In untrained but not in trained animals, exhaustive exercise caused, 5 days afterward, fiber necrosis and a marked increase in the activities of beta-glucuronidase, beta-N-acetylglucosaminidase, arylsulphatase, ribonuclease, deoxyribonuclease, cathepsin D, and cathepsin C, especially in red muscle fibers. Training increased the activities of citrate synthase, beta-glucuronidase, and cathepsin D in both muscle types and those of beta-N-acetylglucosaminidase, arylsulphatase, and cathepsin C in red muscle. Effects of detraining were minor. Exhaustive exercise causes lethal and evidently also sublethal fiber injuries manifesting themselves as an activation of the lysosomal system of muscle fibers 5 days later. Training affects cellular homeostasis by causing an apparent resistance to the damaging effects of exhaustive exercise. Moderately increased hydrolase activities may reflect increased turnover in endurance-trained muscles.
 ...
PMID:Exhaustive exercise, endurance training, and acid hydrolase activity in skeletal muscle. 22 20

Bone resorption plays an important role in bone modeling and remodeling. Osteoclasts are the cells responsible for the bone resorption. Osteoclasts are located on endosteal bone surfaces and on the periosteal surface beneath the periosteum. They are multinucleated giant cells highly polarized in their morphology and function. Among the proximal surface, the membrane and the area of the cytoplasm directly oppose to the bone surface, which are specialized into two regions. A central region consisting of many irregular cytoplasmic processes and infoldings, the ruffled border, is known to be the active site of bone resorption. Surrounding the ruffled border, a second region, the clear zone provides an area of close attachment to the mineralized bone surface. The osteoclasts secrete a large amount of protons by the action of H(+)-pump on the ruffled border into the sealed resorption cavity, resulting in the acidified microenvironment under which condition the bone matrix is dissolved. Protons are provided by the intracellular action of carbonic anhydrase. Following the secretion of the protons, several ion-transporting systems, i.e., carbonate-chloride exchanger, chloride-channel, Ca(2+)-transport systems, Na+/K(+)-ATPase, and voltage-dependent Ca(2+)-channel, are sequentially operated on both apical and basolateral cytoplasmic membranes. In addition, osteoclasts contain a large amount of lysosomal enzymes (cathepsin C, beta-glycerophosphatase, beta-glucuronidase, etc.), which contribute to degrade the bone organic matrices exposed in the resorption cavity. These enzymes bind to the mannose-6-phosphate receptor on Golgi apparatus, are transported to the ruffled border and are secreted into the extracellular compartment in an exocytotic manner. Osteoclasts also have a high tartrate-resistant acid phosphatase activity which is currently used as a marker enzyme osteoclastic differentiation. Osteoclasts are considered to develop from hematopoietic stem cells. So far, the following four different pathways of the differentiation of osteoclast are proposed: The precursors of osteoclast develop (1) from multilineage hematopoietic cells via a completely separate differentiation line, (2) from granulocyte macrophage-colony forming cells, (3) from committed but proliferative monocyte-macrophage, and (4) from mature and unproliferative monocyte-macrophage. However, the differentiation line of the osteoclasts has still to be elucidated. The formation of osteoclasts as well as that of other hematopoietic cells is strongly regulated by many cytokines [interleukin (IL)-1,IL-3,IL-6, M-colony stimulating factor (CSF), and GM-CSF]. 1,25-Dihydroxyvitamin D3 and parathyroid hormone also stimulate the differentiation of osteoclast precursors. However, the mature osteoclasts do not possess the receptors for these hormones.(ABSTRACT TRUNCATED AT 400 WORDS)
 ...
PMID:[Osteoclasts in bone metabolism]. 175 56

Normal arterial foci which take up Evans blue dye (EBD) in vivo are believed to represent atherosclerosis-prone, hemodynamically stressed foci compared to areas which exclude dye. We have used the rabbit EBD model to examine focal aortic hydrolases of blue areas versus white areas, and we report herein significant focal variations of hydrolase activities. Enzymes measured included neutral alpha-glucosidase, N-acetyl-beta-glucosaminidase, alpha-mannosidase, acid alpha-glucosidase, beta-galactosidase, beta-glucuronidase, cathepsin C, and acid cholesteryl esterase (ACE); specific activities were expressed on the basis of tissue DNA. In correlative areas of EBD uptake in normal rabbit aortic arch, ACE activity averaged 17% higher and cathepsin C activity averaged 37% lower than activities of areas free of EBD in the descending thoracic aorta (P less than 0.02). None of the glycosidases studied differed significantly between blue and white aortic areas. These findings indicate that discrete, intrinsic differences of hydrolytic enzyme activities exist in the normal rabbit aorta in areas delineated by in vivo EBD uptake, areas recognized as lesion-prone vs lesion-resistant.
 ...
PMID:Intrinsic focal variations of rabbit aortic hydrolase activities. 276 19

Lysosomal changes were recorded in the skeletal muscles of mice and rats during the repair of muscle fiber injuries caused by a single bout of prolonged running. One purpose of the study was to characterize cellular and compartmental distributions of lysosomal enzymes and to investigate ultrastructural changes in the lysosomal system associated with the appearance and repair of muscle fiber injuries. Furthermore, the level of muscle fiber injuries was correlated with the lysosomal enzyme response and the indices obtained were utilized in the evaluation of the pathogenesis of exercise myopathy. The main results were: Heavy physical exertion caused scattered necrotic injuries of muscle fibers and inflammation in several skeletal muscles. The most susceptible muscles to exercise injuries were the red deep parts of quadriceps femoris muscle and the soleus and tibialis anterior muscles. The total activities of several lysosomal acid hydrolases, in particular those of beta/-glucuronidase, cathepsin C and arylsulphatase, strongly increased during the repair of exercise injuries. The highest responses occurred 3-5 days after exertion and the degree of enzyme responses correlated significantly with the level of histological injuries. The histochemical staining intensities of beta-N-acetylglucosaminidase and beta-glucuronidase were highest 3 and 5 days after exertion. An increased staining intensity occurred in the inflammatory phagocytes and in the surviving muscle fibers, especially in the red muscle fibers close to necrotic foci. An autophagic response occurred in the muscle fibers close to necrotic foci 2-7 days after exertion. Autophagic vacuoles were frequently small and contained different cellular structures at various stages of degradation. The number of lysosome-like bodies, Golgi complexes and multilamellar bodies also increased. Macrophages removed the debris of necrotic muscle fibers by heterophagic uptake 2-5 days after exertion. The unsedimentable and releasable activities of acid hydrolases increased more prominently than those of the total activities in homogenates and reached their highest values 3 days after exertion. The proportional distribution of various acid hydrolases to unsedimentable, releasable and bound fractions varied strikingly but remained appreciably stable throughout the exercise myopathy. The content of lysosomal phosphomannosyl-enzyme receptors in the membrane fraction was unchanged 0-3 days after exertion but a small increase occurred later. The endogenous receptor-bound activity of beta-N-acetylglucosaminidase was considerably increased 1-5 days after exertion but decreased later to the control level.(ABSTRACT TRUNCATED AT 400 WORDS)
 ...
PMID:Lysosomal changes in skeletal muscles during the repair of exercise injuries in muscle fibers. 298 70

We examined specific activities (based on DNA) of six glycosidases and cathepsin C in aorta, kidney, and liver from male rats of 2, 6, 10, and 14 months of age. The premise was that assessing cellular catabolism of arterial and nonvascular tissues over age might more fully clarify the impact of age (and growth) alone upon vascular wall metabolism. All aortic glycosidases increased significantly (P less than 0.05) over the holding period as follows: neutral alpha-glucosidase, up 93%; beta-galactosidase, up 102%; N-acetyl-beta-glucosaminidase, up 119%; alpha-mannosidase, up 77%; beta-glucuronidase, up 65%; acid alpha-glucosidase, up 95%. Cathepsin C specific activity was unchanged as was aortic DNA content; total protein content increased 136%. In the kidney, all glycosidase specific activities declined over age with decreases ranging 39-55%; cathepsin C was unchanged. In the liver, neutral alpha-glucosidase increased 12%, acid alpha-glucosidase was unchanged, and the four remaining glycosidases decreased an average of 5-35% by 14 months of age. Liver cathepsin C decreased 44% over this period. Thus, enhancement of hydrolase baseline activities prevails during growth and aging in rat aortic tissue whereas hydrolases of kidney and liver tissues generally decline.
 ...
PMID:Hydrolase activities increase in the rat aorta with growth and aging but not in liver and kidney. 309 18

The activities of acid proteolytic enzymes were assayed in the liver and muscular tissues of mice (Mus musculus) 1, 6 and 24 hr after the administration of a protease inhibitor leupeptin (i.p., 15.5 mg/kg body wt). Leupeptin administration induced a strong inhibition of cathepsin B and a moderate inhibition of cathepsin C and acid autolytic rate in mouse liver 1 hr after injection. Thereafter the inhibition reduced and disappeared during 24 hr. The activity of cathepsin D was increased in liver 6 and 24 hr after injection. The activity of beta-glucuronidase was not affected by the leupeptin treatment. The administration of leupeptin did not affect the rate of acid autolysis and the activities of cathepsin C and D in cardiac and skeletal muscles. A slight increase in cathepsin B activity was observed 1 hr after leupeptin treatment in calf muscles. The cause of both tissue and enzyme specific changes after leupeptin treatment is discussed.
 ...
PMID:Acid proteolytic activities in mouse liver and muscle tissues after treatment with protease inhibitor leupeptin. 614 85

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.
 ...
PMID:Changes in lysosomal enzyme activities in exercise-induced cardiac hypertrophy of mice. 622 47

In dystrophic hamsters, increases in the levels of cathepsin B plus L and thiol proteinase inhibitor were marked in skeletal muscle, but only slight in heart muscle. The lysosomal hydrolases did not increase in parallel in dystrophic muscle: cathepsin B plus L and beta-glucuronidase increased, but cathepsin C and acid phosphatase did not. In immunohistochemical studies with antibodies against rat liver cathepsin B and thiol proteinase inhibitor, the proteinase and inhibitor were both stained in phagocytes, chiefly macrophages, but not in muscle cells, indicating that the increases in cathepsin B plus L and thiol proteinase inhibitor in dystrophic muscle are due to their presence in invading phagocytes. The levels of cathepsin B plus L, beta-glucuronidase and thiol proteinase inhibitor in isolated peritoneal macrophages were 50 to 180 times higher than those in skeletal muscle, but the levels of acid phosphatase and cathepsin C were only about 10 to 30 times those in skeletal muscle. Plots of the cathepsin B plus L activities versus the level of thiol proteinase inhibitor in homogenates of tissues of various animals showed an exponential rather than a linear relation between the two activities, suggesting that the syntheses of the proteinases are higher than that of the inhibitor in phagocytes invading dystrophic muscle.
 ...
PMID:Increases in cathepsins B and L and thiol proteinase inhibitor in muscle of dystrophic hamsters. Their localization in invading phagocytes. 653 Apr

Three experiments were designed to study the lysosomal changes associated with the development and maintenance of the endurance training induced resistance against exercise injuries in mouse skeletal muscles. The activities of arylsulphatase, cathepsin C, cathepsin D, and beta-glucuronidase were assayed from the red part of mouse quadriceps femoris muscle 4 days after prolonged strenuous running of 4-9 h duration. Exercise injuries were characterized by necrotic fibers and focal inflammation. Strenuous running of untrained mice induced necrotic lesions and a 4-5 fold increase in the activities of lysosomal enzymes. This lysosomal response was considerably reduced already by daily training bouts on the 3 days preceding the strenuous exertion. Simultaneously exercise injuries were markedly reduced. Extending the endurance training program increased the running ability of mice and further reduced the necrotic lesions and lysosomal changes induced by the strenuous exercise. The detraining of 1 week after the termination of regular endurance training considerably increased the degree of exercise induced lysosomal response. The detraining of longer durations further increased the lysosomal response and no effect of prior endurance training existed after 1 month detraining. Our observations suggest that the severity of exercise injuries is related to the strength of the exercise stimulus and the level of preceding physical activity and can be characterized by the lysosomal changes.
 ...
PMID:Lysosomal changes related to exercise injuries and training-induced protection in mouse skeletal muscle. 672 Mar 24


1 2 Next >>