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 effect of 120- and 240-h starvation on rats hepatocytes ultrastructure and particularly the changes of the lysosomes were studied. Eelectronmicroscopically and cytochemically there have been observed diminution of the number of mitochondria and degranulation and vacuolzation of the ER. At the same time Golgi complex was hypertrophied and the number of lysosomes was much increased, mainly those of the autophagic type. Biochemically was shown, that the activity of some acid hydrolases (beta-glucosidase, alpha- and beta-galactosidases, beta-N-acetylglucosaminidase, beta-glucuronidase and arylsulphatases A and B) in the liver of starved rats was markedly expressed. The sedimentation properties of the lysosomes and the lysosomal membrane stability was damaged as well. The data received have been discussed in the light of the reconstructive role of lysosomes.
 ...
PMID:Effect of long-term starvation on the rat liver lysosomes. 0 4

The authors studied in rats the effect of starving from 24 to 96 hours after a regimen of single or all-day feeding. They determined in liver homogenate the total activities of beta-N-acetyl glucosaminidase, acid phosphatase and beta-glucuronidase as well as the free activities of the two first-mentioned enzymes. The activity of beta-N-acetyl glucosaminidase was also determined in the blood. It was found that the total activity of beta-N-acetyl glucosaminidase in the liver homogenate increased with the length of starvation. The free and serum activities of the enzymes under investigation showed similar changes. These increases were more marked in rats subjected to a single-feeding regimen before starving. These changes are explained as an expression of the active participation of the lysosomes and their enzymes in the transition to endogenous feeding. The lysosomal membrane was more sensitive in starving animals which had been subjected to a single-feeding regimen.
 ...
PMID:[Lysosomal enzymes in starvation after regimen of single or all-day feeding]. 95 37

The influence of starving on the activity of enzymes of the rat gastric mucosa was investigated by selected histochemical methods. Beside the conventional methods of enzymatic histochemistry the technique of semipermeable membranes was used in the proof of lysosomal enzymes. Dehydrogenases were proved in aqueous and also in gel media with PMS. During the starvation in the parietal cells a marked increase took place in the activity of acid phosphatase, E-600 resistant esterase, less in beta-glucuronidase. High activity of the lysosomal enzymes in macrophages did not change during starvation. Nor did any changes took place in the activity of alkaline phosphatase in the endothelium of the capillaries. The chief cells in the control and starving animals, in contrast to the human gastric mucosa, did not contain any non-specific esterase. Concerning dehydrogenases, parietal cells with a different activity of these enzymes were observed both in starved and control animals. In the rat gastric mucosa starving induced changes in the activity of the enzymes which mark important organelles of the cells. Thus it is possible to consider the observed histochemical changes as a functional manifestation of morphological damage of cellular structures which are affected during starvation.
 ...
PMID:Histochemical findings in the rat gastric mucosa during starvation. 99 73

Effect of different concentration of non-ionic detergents (Triton X-100, Triton X-305, BRIJ-35 and Triton WR-1339) on total and non-sedimentable activity of 8 rat liver lysosome enzymes (acid phosphatase, acid DNase, acid RNase, arylsulphatases A and B, beta-glucuronidase, beta-galactosidase, beta-glucosidase and beta-acetylglucosaminidase) was studied. Only Triton X-100 at the concentration of 0.1% (and higher) was found to release completely lysosome enzymes. Low concentrations of Triton X-100 (0.025-0.05%) were used to characterize the strength of enzyme binding: the level of releasing acid DNase, beta-galactosidase, beta-glucuronidase and acid phsophatase being considerably higher than that of other lysosome enzymes studied. On the basis of the data obtained a method is worked out, which is suitable for series studies of the stability of lysosome membranes under different physiological and pathological conditions. The essence of the method is the treatment of membrane particles with increasing concentrations of Triton X-100 (0.025; 0.05 AND 0.1%) AND THE SUCCESSIVE ESTIMATION OF NON-Sedimentable activity of marker enzymes. The method detected troubles in the stability of rat liver lysosome membranes under starvation, protein deficiency and aging.
 ...
PMID:[Determination of lysosome membrane stability]. 120 72

The total activity of four lysosome enzymes--acid phosphatase, beta-glucuronidase, alpha-glucosidase and beta-N-acetylglucosaminidase--is studied in liver homogenate at 2, 6, 24 and 48 hours after the last meal in rats, previously sustained on a single-daily-feeding regimen. In addition, the free activity (percentage of the total) of the latter enzyme and its activity in the serum as well are investigated. A rise of the total activity of the first three enzymes is recorded within 48 hours after the beginning of starvation. The free activity of beta-N-acetylglucosaminidase shows an increase at 48 hours, while its activity in the serum--as early as 24 hours. The changes described above are interpreted as an expression of lysosome membrane permeability enhancement under fasting conditions.
 ...
PMID:[Effect of short-term fasting on liver lysosomes in rats, biochemical studies (preliminary report)]. 123 93

The influence of fasting for 24-96 hours is studied in rats, subjected in advance to a regimen of all day long access to food, to a single feeding in 24 hours. Total activity of beta-N-acetylglucosaminidase (beta-N-AcG1), acid phosphatase (AP) and beta-glucuronidase, as well as the free activity of the first two enzymes are studied in liver homogenate. The activity of beta-N-AcG1 is determined in blood serum also. A rise of total beta-N-AcG1 activity is recorded in liver homogenate, increasing parallel to prolongation of the fasting period. The changes in free activity of AP and beta-N-AcG1, and in the plasma activity of the latter enzyme are similar. The above described changes are more strongly pronounced in the groups subjected in advance to a single feeding regimen. These changes are interpreted as an expression of the active participation of lysosomes and their enzymes in the transition to endogenic nutrition. The lysosome membrane proves to be more vulnerable to damage by starvation among the animals previously maintained on a single feeding regimen.
 ...
PMID:[Changes in lysosome enzymatic activity during fasting following a regimen of once-a-day or all-day feeding]. 123 94

Factors controlling variability in enzyme transient expression assays have been investigated in electroporated protoplasts isolated from wheat embryogenic and nonembryogenic calli. The level of variation was reduced to a minimum through the optimization of the beta-glucuronidase measurements in the pellet and the supernatant of the homogenized protoplasts, by expressing the data on the basis of the number of protoplasts found to be viable immediately before the assay and on the amount of protein in the pellet and supernatant. Protoplast separation on the basis of size was also useful in eliminating some of the variation resulting from the heterogeneity of the callus used. Efforts to partially synchronize the callus tissue by auxin starvation have not resulted in a significant decrease of this variation. Our results indicate that the level of variation in enzyme transient activity in protoplasts resulting from calli can be reduced by implementation of the experimental techniques presented here.
 ...
PMID:Factors controlling variability in measurements of the transient gene expression in electroporated protoplasts of wheat callus. 144 20

To depolymerize plant pectin, the phytopathogenic enterobacterium Erwinia chrysanthemi produces a series of enzymes which include a pectin-methyl-esterase encoded by the pem gene and five isoenzymes of pectate lyases encoded by the five genes pelA, pelB, pelC, pelD, and pelE. We have constructed transcriptional fusions between the pectinase gene promoters and the uidA gene, encoding beta-glucuronidase, to study the regulation of these E. chrysanthemi pectinase genes individually. The transcription of the pectinase genes is dependent on many environmental conditions. All the fusions were induced by pectic catabolic products and responded, to different degrees, to growth phase, catabolite repression, temperature, and nitrogen starvation. Transcription of pelA, pelD, and pelE was also increased in anaerobic growth conditions. High osmolarity of the culture medium increased expression of pelE but decreased that of pelD; the other pectinase genes were not affected. The level of expression of each gene was different. Transcription of pelA was very low under all growth conditions. The expression of the pelB, pelC, and pem genes was intermediate. The pelE gene had a high basal level of expression. Expression of pelD was generally the most affected by changes in culture conditions and showed a low basal level but very high induced levels. These differences in the expression of the pectinase genes of E. chrysanthemi 3937 presumably reflect their role during infection of plants, because the degradation of pectic polymers of the plant cell walls is the main determinant of tissue maceration caused by soft rot erwiniae.
 ...
PMID:Environmental conditions affect transcription of the pectinase genes of Erwinia chrysanthemi 3937. 144 47

Whereas the phosphorolytic breakdown of liver glycogen is known to be of great physiological importance, the functional role of the hydrolytic glycogenolysis in the lysosomal system is less well understood. In the present study the effects of fasting, alpha- and beta-adrenoceptor antagonism and insulin-induced hypoglycaemia on liver lysosomal glycogen-hydrolysing enzyme activity were investigated in mice. In freely fed mice the glycogen-hydrolysing activity (acid amyloglucosidase) was only 50% of the maltose-hydrolysing activity (acid maltase). Starvation for 24 h reduced the acid amyloglucosidase activity by approximately 30% (P less than 0.001), whereas the activities of acid maltase, acid phosphatase and beta-glucuronidase appeared unaffected. N-acetyl-beta-D-glucosaminidase activity was moderately (20%; P less than 0.01) enhanced by fasting. Thus, liver lysosomal enzyme activities may change independently of each other during fasting. Further, during short-term hypoglycaemic conditions (45 min) induced by endogenous or exogenous insulin, the activity of liver acid amyloglucosidase was found to be moderately reduced (15-20%). Blockade of alpha- and beta-adrenoceptors by phentolamine and propranolol did not result in any apparent influence on acid amyloglucosidase activity except for the indirect effect exerted by the phentolamine-induced hypoglycaemia. A moderate negative correlation (r = -0.51; P less than 0.001) between total liver glycogen concentration and acid amyloglucosidase activity was observed in a series of 43 freely fed NMRI mice. Our data show that in mouse liver the acid maltase activity predominates over the acid amyloglucosidase activity.(ABSTRACT TRUNCATED AT 250 WORDS)
 ...
PMID:Glycogen and glycogen-hydrolysing lysosomal enzyme activity in mouse liver: effects of fasting, adrenoceptor antagonism and insulin-induced hypoglycaemia. 289 Feb 62

Strenuous prolonged running causes muscle fibre necrosis in skeletal muscles. The muscle injury is associated with inflammation and a strong increase in the total activities of certain acid hydrolases a few days after exertion. The activity changes of acid hydrolases quantitatively well reflect the severity of histopathological changes during the myopathy (for review see Salminen, Acta Physiol Scand [Suppl 539] 1985). In this study male NMRI-mice were exposed to a protocol of fasting and refeeding together with or without a 6 h run on a treadmill at 13.5 m.min-1. The animals were killed 4 days after the exercise and samples from the red part of quadriceps femoris were analyzed for arylsulfatase (ASase) and beta-glucuronidase (GUase) activities. Starvation protocols did not affect ASase or GUase. Running caused a 3.2-fold increase in ASase and a 5.1-fold increase in GUase. If mice were exercised in the fasted condition a normal exercise response occurred in both activities, but when mice were exercised 2 days after the finish of fasting the exercise response was greatly diminished. Thus food deprivation followed by 2 days refeeding induces a protection against exercise myopathy in mice. The protection greatly resembles that induced by regular endurance training preceding strenuous prolonged exertion.
 ...
PMID:Food deprivation decreases the exertion-induced acid hydrolase response in mouse skeletal muscle. 334 83


1 2 3 4 Next >>