Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.23 (beta-galactosidase)
 14,648 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Unicameral bone cyst fluid possesses N-acetyl-beta-D-glucosaminidase, beta-glucuronidase, PZ-peptidase, cathepsin D, acid phosphatase, N-acetyl-beta-D galactosaminidase, and beta-galactosidase activities. The activities of lysosomal enzymes in the cyst fluid are, as a rule, higher than in the serum, whereas the total protein content is lower. The content of collagen degradation products in the cyst fluid is higher compared to the serum. In bone cavity wall tissues, the collagen content is decreased. Adenosine 3':5'-cyclic phosphate and cyclic guanosine 3,5'-monophosphate accumulate in the cyst cavity. However, in some cases, there is no correlation among the activities of lysosomal enzymes in the cyst fluid, blood serum, and cyst wall tissues. The ratios of lysosomal enzyme activities in the cyst fluid differ from those in the cyst wall tissues, cultured skin fibroblasts, and blood polymorphonuclear leucocytes. The lack of coincidence of enzymatic spectra of the cyst fluid, wall tissues, and serum is suggestive of the diversity of ways of lysosomal enzyme enter the cyst cavity, i.e., blood, cyst fluid cells, and cyst cavity walls. The cysts with different locations (i.e., active and latent cysts) have similar lysosomal lytic potentials. The presence in the cyst cavity of extracellular lysosomal enzymes and collagen degradation products testifies to the permanent corrosion of the cyst cavity walls from the inside as well as to the increase in the osmotic pressure of the cyst fluid. Lysosome destruction should be regarded as an important pathogenetic factor that requires surgical or pharmacologic correction or both in the course of bone cyst management.
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PMID:The role of lysosomes in the pathogenesis of unicameral bone cysts. 185 Mar 36

Experiments on rats were staged to investigate the activity of lysosomal cardiac enzymes (beta-galactosidase, beta-glucosidase, acid phosphatase) against a varied endogenous background of sex steroids (in male and female animals and in females at various stages of the estrual cycle) and a possibility of direct influence of steroids on lysosomes. The investigation has shown sex differences in the activity of lysosomal cardiac enzymes of rats: total activity of beta-galactosidase, beta-glucosidase and acid phosphatase in the heart of male rats was higher than that of female rats. Correlation between the activity of lysosomal cardiac enzymes of female rats and stages of the estrual cycle was noted. Sex hormones at high (nonphysiological) concentrations could produce a direct effect on rat cardiac lysosomes, estradiol as distinct from testosterone, causing stabilization of lysosomal membranes.
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PMID:[Effect of sex steroids on the activity of cardiac lysosomal enzymes]. 190 53

Cathepsin D, acid phosphatase, beta-galactosidase, N-acetyl hexosaminidase, leucine aminopeptidase (LAP), lactate dehydrogenase, glucose-6-phosphate dehydrogenase (g-6-PDH), and peroxidase activities were measured in the buccal mucosa of rats kept for 60 days on high-sucrose (68% of sucrose) caries-inducing diet. The findings evidence that this diet observed for 30 days results in a significant elevation of beta-galactosidase and LAP activities and in reduction of peroxidase level. After 60-day diet the examined parameters virtually did not differ from the reference characteristics (a control group kept on 68% starch diet), except elevated g-6-PDH and lowered peroxidase activities. Enzymic activity changes are adaptive and evidence changes in the metabolic processes in the buccal mucosa, that may eventuate in the development of periodontal diseases.
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PMID:[The effect of a high-saccharose diet on the enzymatic activity of the oral mucosa in rats]. 192 95

The PHO84 gene specifies Pi-transport in Saccharomyces cerevisiae. A DNA fragment bearing the PHO84 gene was cloned by its ability to complement constitutive synthesis of repressible acid phosphatase of pho84 mutant cells. Its nucleotide sequence predicted a protein of 596 amino acids with a sequence homologous to that of a superfamily of sugar transporters. Hydropathy analysis suggested that the secondary structure of the PHO84 protein consists of two blocks of six transmembrane domains separated by 74 amino acid residues. The cloned PH084 DNA restored the Pi transport activity of pho84 mutant cells. The PHO84 transcription was regulated by Pi like those of the PHO5, PHO8, and PHO81 genes. A PHO84-lacZ fusion gene produced beta-galactosidase activity under the regulation of Pi, and the activity was suggested to be bound to a membrane fraction. Gene disruption of PHO84 was not lethal. By comparison of nucleotide sequences and by tetrad analysis with GAL80 as a standard, the PHO84 locus was mapped at a site beside the TUB3 locus on the left arm of chromosome XIII.
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PMID:The PHO84 gene of Saccharomyces cerevisiae encodes an inorganic phosphate transporter. 203 28

The effect of cysteamine on the activity of lysosomal enzymes and the prolactin content of isolated hyperprolactinaemic cells has been investigated. In broken cell preparations, cysteamine markedly stimulated acid prolactin protease activity. In intact cells, however, cysteamine inhibited acid prolactin protease activity and beta-galactosidase. Moreover, the activities of alpha-mannosidase, acid phosphatase, beta-glucuronidase, total arylsulphatase and hexosaminidase were not changed by the addition of cysteamine. Cysteamine significantly depleted the cells of prolactin, and this action was not compromized by the inclusion of either leupeptin, chloroquine or NH4Cl in the incubation media. Taken together, these results indicate that cysteamine does not promote degradation of prolactin and hence depletion of prolactin from the pituitary through a mechanism involving lysosomal enzyme degradation.
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PMID:Effect of cysteamine on the lysosomal enzymes of the hyperprolactinaemic rat pituitary. 211 Sep 66

We have shown that hybrid proteins composed of the yeast repressible acid phosphatase (PHO5) and bacterial beta-galactosidase (lacZ) interfere with secretion of native acid phosphatase (Wolfe, P. B. (1988) J. Biol. Chem. 263, 6908-6915). We now report that PHO5-LacZ hybrid proteins have a more general effect on secretion and prevent translocation of several secreted proteins. Translocation of both the mating pheromone alpha-factor and the vacuolar protease carboxypeptidase Y is partially blocked when PHO5-LacZ hybrids are expressed. Cell fractionation and protease sensitivity indicate that alpha-factor and carboxypeptidase Y accumulate in precursor form on the cytoplasmic surface of the endoplasmic reticulum. Indirect immunofluorescence with antibody directed against beta-galactosidase supports the localization of hybrid proteins to the endoplasmic reticulum. Analysis of the hybrid protein phenotype in vivo and in vitro suggests that the hybrid proteins deplete a soluble factor required for efficient translocation across the endoplasmic reticulum. First, a decrease in the expression of a hybrid protein in vivo decreases its effect on translocation. Second, an in vitro translation/translocation reaction, prepared from a hybrid-bearing strain, is deficient in its ability to translocate prepro-alpha-factor across yeast microsomal membranes. This deficiency is complemented by addition of cytosol prepared from wild type cells. Finally, the hybrid protein phenotype is shown to be independent of the requirement for SSA gene products.
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PMID:Expression of acid phosphatase-beta-galactosidase hybrid proteins prevents translocation by depleting a soluble factor. 212 90

The synthesis and secretion of pro-cathepsin D is increased by estrogens in MCF7 cells. We quantified the effect of estradiol on other lysosomal enzymes in order to investigate the mechanism of this hypersecretion. Precursors of beta-hexosaminidase, cathepsin B and beta-galactosidase, which are routed to lysosomes via the mannose-6-phosphate (Man-6-P) receptor, were secreted in much lower amounts than pro-cathepsin D, but their secretion was also increased by estradiol. The activity of acid phosphatase, which is routed to lysosomes via a different transmembrane mechanism, was not altered by estradiol. While estradiol stimulated gene expression of pro-cathepsin D, it had no effect on that of pro-cathepsin B. We conclude that estradiol stimulates the secretion of several lysosomal pro-enzymes in MCF7 cells, suggesting that a general mechanism is responsible for this derouting rather than a specific alteration of cathepsin D structure.
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PMID:Estradiol increases the secretion by MCF7 cells of several lysosomal pro-enzymes. 222 57

The specific activity of 4 lysosomal enzymes was studied in homogenate, hepatocytes, Kupffer and endothelial cells isolated from the livers of female Sprague-Dawley rats aged 3.5, 12 and 24 months. Cells were obtained by enzymatic digestion and centrifugal elutriation. Cell viability was not affected by age or diet. In hepatocytes, the activities of all enzymes (acid phosphatase, beta-galactosidase, arylsulfatase B and cathepsin D) increased with age in rats fed ad libitum (A) but were not altered significantly by dietary restriction. The activities of all enzymes except acid phosphatase were systematically higher at 3.5 months of age in Kupffer and endothelial cells than in hepatocytes. Acid phosphatase, arylsulfatase B and cathepsin D activities increased with age in both Kupffer and endothelial cells. Beta galactosidase was decreased significantly with age in Kupffer cells but was elevated in endothelial cells. Rats exposed to dietary restriction (R) showed higher activities of beta-galactosidase, arylsulfatase B and cathepsin D when compared to corresponding A animals with the exception of the younger age group. No clear cut pattern was observed in acid phosphatase activity. Thus, the activities of liver lysosomal enzymes increase with age but the pattern of change differs with respect to enzyme and cell populations. The heightened enzyme activity in Kupffer and endothelial cells from R rats may reflect a more efficient phagocytic capacity in these animals.
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PMID:Characterization of liver lysosomal enzyme activity in hepatocytes, Kupffer and endothelial cells during aging: effect of dietary restriction. 229 Mar 53

The catalytic and immunological properties of acid phosphatases (EC 3.1.3.2.) in different tissues were studied. It was demonstrated that high uptake forms of lysosomal enzymes like beta-galactosidase isolated from human platelets and bovine testis are mature enzymes, which have not lost their mannose-6phosphate marker. The results presented indicate that this phenomenon is related to a low activity or the complete absence of the lysosomal tartrate sensitive acid phosphatase activity in the tissues concerned.
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PMID:Lysosomal tartrate sensitive acid phosphatase deficiency in cells which contain lysosomal "high uptake forms". 232 40

Dextran blue decreases the activity of lysosomal acid cholesteryl esterase of rat liver at a concentration from 0.25 M to 10 M without altering acid phosphatase, acid beta-galactosidase and beta-glucosidase activities. The dextran blue filled lysosomes with a high degree of purity prepared by centrifugation over the linear sucrose density gradient contained insignificant impurities (up to 19%) of protein from other organelles. The specific activity of acid phosphatase, beta-galactosidase and beta-glucosidase was increased 35-40-fold in this fraction, whereas the activity of acid cholesteryl esterase rose but 14.7-fold. Chromatography on a Sepharose 2B column of the digitonin-digested native and dextran-containing lysosomes attests to the formation of large dextran aggregates with lysosomal matrix proteins. Since aggregation of dextran blue with acid phosphatase, beta-galactosidase and beta-glucosidase does not affect their activities, it is concluded that to bring about hydrolysis of lipoprotein cholesterol esters, it is necessary that cholesteryl esterase be associated with hydrophobic macromolecules. Moreover, dextran blue can be used for simulation cholesterol esters deposition in lysosomes.
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PMID:[Inhibition of liver lysosomal cholesterol esterase activity in rats by dextran blue in vivo and in vitro]. 240 93


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