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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)
We studied the effects of prolonged running exercise (5 days a week, 1.5 h per day at a speed of 17.6 m/min) on the activity of some acid hydrolases (
beta-glucuronidase
, beta-N-acetylglucosaminidase, acid phosphatase and cathepsin D) and three enzymes of energy metabolism (cytochrome c oxidase,
lactate dehydrogenase
and creatine kinase) in the distal and in the proximal, the predominantly white and red parts, respectively, of the vastus lateralis-muscle from mice. The acid hydrolase activity levels were 1.24--1.69 higher in untrained red muscle compared to untrained white muscle. The light training applied increased the activity of
beta-glucuronidase
in both red and white muscle. No other significant training effects were observed in the enzyme activities measured.
...
PMID:beta-Glucuronidase activity in trained red and white skeletal muscle of mice. 21 65
Infection of HeLa-cell monolayer cultures with rabbit poxvirus induces a marked decrease in cell-associated protein and in the activities of
lactate dehydrogenase
, acid phosphatase, and
beta-glucuronidase
. This effect begins to occur around 10 hours post-infection (p.i.) and is accompanied by a concomitant rise of these enzyme activities in the culture medium. Only few cells detach from infected monolayers and these cannot account for protein release. Virion release can be inhibited at 4 degrees C, whereas protein release cannot and it seems therefore that these events do not happen by a common mechanism. Moreover, penetration studies with [14C]-sucrose indicate that protein release reflects a true increase in plasma membrane permeability. Using the Gomori stain for acid phosphatase, a release of the enzyme into the cytoplasm around 8 hours p.i. can be confirmed rendering a causative role of lysosomal hydrolases in the pathogenesis of the observed plasma membrane permeability changes possible but not proving it.
...
PMID:Permeability changes of plasma and lysosomal membranes in HeLa cells infected with rabbit poxvirus. 21 5
The effect of N6,O2'-dibutyryl adenosine 3',5'-cyclic-monophosphate (dbcAMP) on the mobilization of calcium (Ca2+), inorganic phosphate (Pi) and lysosomal enzymes was studied in a bone culture system for 24 h using half calvaria from 6--7 day-old mice. DbcAMP inhibited spontaneous as well as parathyroid hormone-stimulated mineral mobilization. DbcAMP in a concentration of 5 x 10(-4)M also reduced the activities of
beta-glucuronidase
, beta-galactosidase and acid phosphatase found in the media while the activities of
lactate dehydrogenase
, aspartate aminotransferase and alanine aminotransferase were not affected. It is concluded that cAMP is not a stimulator but an inhibitor of bone resorption within the culture period studied (24 h) and that the cyclic nucleotide might interfere with release processes involved in bone resorption.
...
PMID:Inhibitory effect of dibutyryl cyclic AMP on the release of calcium, inorganic phosphate and lysosomal enzymes from calvarial bones cultured for 24 hours. 22 6
56 human liver biopsy specimens with insignificant or no histological changes, but with abnormally strong canalicular alkaline phosphatase activity, were studied histochemically for other enzyme changes. In comparison with normal specimens, more extensive and increased canalicular activity of gamma-glutamyl transferase, and increase of canalicular leucine aminopeptidase, was found, while the sinusoidal activity of the latter enzyme was decreased. Staining for adenosine triphosphatase regularly desclosed the normal pattern of sinusoidal and canalicular activity. The lysosomal enzymes, acid phosphatase and
beta-glucuronidase
, stained more intensely than ordinarily, while the reactions for enzymes present in the cytosol (
lactic dehydrogenase
), in the mitochondria (succinic dehydrogenase, imonoamine oxidase) and in the endoplasmic reticulum (glucose-6-phosphatase) were normal.
...
PMID:On histochemical enzyme changes in association with canalicular activity of alkaline phosphatase in human liver. 24 Dec 3
The role of calcium in triggering prostaglandin and thromboxane synthesis was studied in several systems with ionophores of different ion specificities. Divalent cationophore A23187 stimulates prostaglandin and thromboxane production by washed human platelets in a concentration-dependent manner (0.3-9 muM). A23187 also induces an antimycin A-insensitive burst in oxygen utilization which is partially blocked by 5 mM aspirin or 10 muM indomethacin. Under our conditions, A23187 (up to 10 muM) does not appear to damage platelet membranes since it does not cause appreciable loss of
lactate dehydrogenase
or
beta-glucuronidase
. Mono- and divalent cationophore X537A also stimulates platelet thromboxane B(2) production and oxygen utilization, but monovalent cationophores nigericin, monensin A, A204, and valinomycin have no effect. The synthesis of prostaglandins E(2), D(2), and F(2alpha) by rat renal medulla mince is stimulated by 1 and 5 muM A23187 without changes in tissue ATP content, lactate output, or K(+) efflux. X537A, monensin A, and nigericin (all 5 muM) stimulate both prostaglandin output and K(+) efflux from renal medulla, while 5 muM valinomycin or A204 has no effect on either. None of the ionophores stimulates renomedullary prostaglandin production if calcium is omitted from the incubation medium. A23187 also stimulates prostaglandin production by human lymphoma cells, rat stomach and trachea preparations, and guinea pig polymorphonuclear leukocytes. These observations suggest a major role for Ca(2+) in stimulating prostaglandin and thromboxane biosynthesis, and also indicate that prostaglandin and/or thromboxane release may partially mediate some of the previously described effects of ionophores on cells and tissues.
...
PMID:Ionophores stimulate prostaglandin and thromboxane biosynthesis. 27 Jun 68
1 Rabbit isolated peritoneal neutrophil polymorphonuclear leucocytes were depleted of calcium by exposure for 1 h to calcium-free bathing fluid at 4 degrees C. 2 Addition of calcium ions to the previously calcium-depleted calls during incubation at 37 degrees C stimulated the release of
beta-glucuronidase
and of lysozyme but not of
lactate dehydrogenase
. 3 Low concentrations of indomethacin, flufenamate or salicylate, such as those which occur in the blood plasma after therapeutic doses of these drugs, selectively inhibited the calcium-induced release of
beta-glucuronidase
. The slight release of this enzyme which occurred in the absence of added calcium ions was not altered by these drugs, neither was the release of
lactate dehydrogenase
. 4 Release of lysozyme was inhibited by low concentrations of salicylate, amidopyrine or oxyphenbutazone, independent of the presence or absence of calcium ions. 5 Chloroquine, hydrocortisone or colchicine did not alter the release of leucocyte enzymes.
...
PMID:Effect of indomethacin and related drugs on the calcium ion-dependent secretion of lysosomal and other enzymes by neutrophil polymorphonuclear leucocytes in vitro. 40 67
The activities of several enzymes in urine are masked by the presence of interfering substances in native urine. From several methods proposed for the removal of low molecular mass interferences dilution, dialysis, gel filtration, and ultrafiltration have been successfully applied. Gel filtration seems to be of these most suitable. I is effective, accurate, precise and economical. Scale-down procedures provide for acceptable speed. By this method the complete separation of
lactate dehydrogenase
, gamma-glutamyltransferase, alkaline phosphatase, arylsulphatase A, alpha-glucosidase, beta-galactosidase, trehalase, N-acetyl-beta-glucosaminidase,
beta-glucuronidase
and leucine arylamidase from low molecular mass substances, e.g. a heat-stable, competitive inhibitor of N-acetyl-beta-glucosaminidase was possible. The preparation and determination of urinary enzymes should be thoroughly standardized and controlled. Acceptable precision (coefficient of variation less than 10% between-day) can be achieved with manual spectrophotometric methods.
...
PMID:Preparation of urine for enzyme determinations by gel filtration. 44 74
This study analyzed the neutrophils and sera of patients with rheumatoid arthritis and of normal controls. No significant differences were found in the activities of the granular enzymes
beta-glucuronidase
and lysozyme or the cytoplasmic enzyme
lactic dehydrogenase
(
LDH
). Normal neutrophils were found to release significant (P less than 0.05) amounts of the granular enzymes, but not of
LDH
in response to immunoglobulin G aggregates. There was no difference in the percent release exhibited by rheumatoid versus control neutrophils. Studies delineating the effects of rheumatoid factor sera and normal sera on aggregate-induced enzyme release revealed a significant negative correlation between the amount of rheumatoid factor in the sera and the percent release of
beta-glucuronidase
and lysozyme but not of
LDH
. These studies thus demonstrate no abnormalities in rheumatoid neutrophil or rheumatoid serum enzyme activities or in neutrophil response to immunoglobulin G aggregates. They suggest, however, that rheumatoid factor may partially inhibit the release of lysosomal enzymes, thus suppressing this important component of the rheumatoid inflammatory process.
...
PMID:Neutrophil enzyme activities in rheumatoid inflammation. 47
The effect of diphenylhydantoin (DPH) on degradation of collagen was studied during 10 days in organ culture of cat palatal mucosa by measuring the release of hydroxyproline to the culture medium. In parallel, the activities of beta-glucuronidaase and
lactate dehydrogenase
(
LDH
) as markers for lysosomal and cytosokic enzymes, respectively, were registered in the tissues and in the culture medium and the glucose consumption was also measured. DPH caused a 36% inhibition of the cumulative release of hydroxyproline to the medium. The activities in the media of
beta-glucuronidase
and
LDH
showed a 23% and 30% reduction, respectively. The glucose consumption was unaltered by the drug. The results show that one way by which DPH may interfere with collagen degradation is by blocking enzyme release from the cells.
...
PMID:The effect of diphenylhydantoin upon enzyme release in relation to collagen degradation in cat palatal mucosa during organ culture. 50 11
Rabbit polymorphonuclear leukocytes were incubated with a sonically treated suspension of pooled dental plaque to determine if the plaque would induce release of lysosomal enzymes from the polymorphonuclear leukocytes. Cells incubated with plaque at 37 degrees C released significantly greater amounts of the lysosomal enzymes,
beta-glucuronidase
and lysozyme, than did cells incubated with plaque at 0 degrees C or without plaque at 37 degrees C. This response was both dose and time dependent. Release of the cytoplasmic enzyme
lactate dehydrogenase
was minimal, and there were no significant differences in
lactate dehydrogenase
release between cells at 0 and 37 degrees C, or without plaque. These results indicate that dental plaque can induce the selective release of lysosomal enzymes, which could be involved in the periodontal injury produced by dental plaque.
...
PMID:Exocytosis of polymorphonuclear leukocyte lysosomal contents induced by dental plaque. 56 Oct 32
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