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)

1. Both the post-partum involution of the rat uterus and the rapid breakdown of collagen that accompanies it are extensively inhibited by oestrogenic hormones. In the normal rat, 85% of the uterine collagen is degraded within 4 days after parturition; in rats treated with 100mug. of 17beta-oestradiol/day, only 35% of uterine collagen is broken down in the same period. 2. Similar effects are produced by diethylstilboestrol if the dose is increased tenfold. 3. Collagen breakdown is inhibited to a greater extent than is the loss of wet weight by oestradiol but not by diethylstilboestrol. 4. The oestrogens appear to act by blocking the breakdown of collagen. There is a greatly decreased concentration of free hydroxyproline in the uterus of treated animals. 5. Acid hydrolase concentrations (beta-glucuronidase, beta-galactosidase, cathepsin D and acid phosphatase) in the uterus are decreased by oestrogen treatment compared with controls, but the total amounts of these enzymes in the uterus are somewhat elevated. Oestrogens do not appear to inhibit collagen breakdown by altering the concentration and total amount of acid hydrolases.
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PMID:Inhibition by oestrogen of collagen breakdown in the involuting rat uterus. 582 64

BCG lesions were produced in the skin of rabbits, and biopsies were performed at 7, 21, and 42 days, when they were developing, maximal in size, and almost healed, respectively. Tissue sections were prepared and stained histochemically for several enzymes. The percentage of cells stained for a given enzyme and the distribution of such cells within lesions of various ages were determined. Seven-day BCG lesions contained few esterase- and beta-galactosidase-positive macrophages, but 21-day lesions contained many, especially in the viable and nonviable tuberculous granulation tissue at the edge of the now prominent caseous necrotic center. Both 7-day and 21-day lesions contained many acid phosphatase- and cathepsin-D-positive macrophages, which were numerous in the more peripheral parts of the lesion, where little or no necrosis was present. Enzyme patterns in 42-day lesions resembled those in 21-day lesions. The role of each of these enzymes in the development and regression of the BCG lesion is unknown. Nonetheless, these studies clearly demonstrate that this macrophage population is heterogeneous and that macrophages carry out different functions in different parts of the lesion at different times. Histochemical techniques were developed to stain two enzymes in the same tissue section. The first stain usually contained a naphthol substrate and produced a red color; the second stain contained an indoxyl substrate and produced a blue color. A cell staining with both was colored purple. The peroxidase-antiperoxidase immunocytochemical technique for cathepsin D (producing a red color) was also employed. 1) Red esterase (hydrolyzing naphthol AS-D acetate) and beta-galactosidase, and 2) red esterase and blue esterase (hydrolyzing 5-bromo-4-chloro-indoxyl acetate), probably the same enzyme, were usually present in the same macrophage. In contrast, each of the following enzyme pairs was usually present in a different macrophage: 3) cathepsin D and beta-galactosidase, 4) cathepsin D and blue esterase, 5) acid phosphatase and beta-galactosidase, and 6) acid phosphatase and blue esterase. Roughly 10% of the macrophages stained for one enzyme existed side by side with macrophages stained for a different enzyme. These results suggest that local macrophage activation is under two levels of control. The first, macrolocal control, would determine the overall enzyme distribution in the lesion; whereas the second, microlocal control, would determine enzyme distribution on a cell-by-cell basis, ie, how two neighboring macrophages can each be rich in a different enzyme.
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PMID:Macrophage functional heterogeneity in vivo. Macrolocal and microlocal macrophage activation, identified by double-staining tissue sections of BCG granulomas for pairs of enzymes. 615 72

The modification of lysosomal enzyme activities in animals irradiated with the same sublethal dose at 4 different times of the day is reported. The results confirmed the absence of circadian fluctuations in all the lysosomal enzymes and in protein content. A difference in behaviour between acid beta-galactosidase and beta-glucuronidase on the one hand and between acid phosphatase and cathepsin D on the other was evident in irradiated animals. The results showed that acid beta-galactosidase and beta-glucuronidase increase from the early intervals after irradiation and reach the highest activity between 36 and 48 h. At these intervals autolysis phenomena, heavy cellular alterations and numerous phlogosis cells are present in the epithelium. Only beta-glucuronidase and acid beta-galactosidase indicate the level of radiation injury.
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PMID:Modifications of small intestine lysosomal enzymes after irradiation at different times of the day. 628 98

The specific activities of the lysosomal enzymes acid phosphatase, beta-galactosidase, arylsulphatase B and cathepsin D were determined in homogenates of livers of rats fed ad libitum and of rats subjected to long-term dietary restriction (10%, 30% and 50% of diet consumed by the ad libitum group). Dietary restriction began soon after weaning and animals were sacrificed 3, 9, 15 and 24 weeks later. Dietary restriction influenced all four enzymes but the changes depended on the enzyme as well as on the degree and duration of the dietary restriction. Total activity of acid phosphatase increased significantly at 3 weeks of restriction but only in the 50% group. The activity returned to normal values at 9 weeks. Arylsulphatase B increased in all experimental groups with a more pronounced change observed at 3 weeks and in the more severely restricted rats. No notable change in the activities of beta-galactosidase and cathepsin D activities was observed. Changes in the liver ultrastructure paralleled the biochemical changes seen at 3 weeks. Numerous autophagic vacuoles and dense bodies resembling age pigments were formed in the hepatocytic cytoplasm. Mitochondrial enlargement, increased matrical density and rough endoplasmic reticulum fragmentation were also noted. Few of these changes were observed at 9 weeks, and the hepatocyte's morphology was virtually normal at 15 and 24 weeks. The marked changes seen at 3 weeks may be a manifestation of the body's adaptive processes to the nutritional stress.
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PMID:Liver lysosomal enzymes in rats during long-term dietary restriction. 1. Changes during the developmental period of life. 642 Jun 22

Lysosomal enzymes acid phosphatase, acid DNAase, acid RNAase cathepsin D,beta-galactosidase beta-glucuronidase were studied in mice and rat liver tissue within 3 days beginning from 4 o'clock a.m. at 4 hrs intervals. Activities of acid phosphatase, acid RNA ase in mice liver tissue and of cathepsin D in rat and mice liver tissues was higher at morning and day time than at evening and night. Alterations in enzymatic activity of non-sedimenting fraction of mice liver tissue correlated with that of total activity. In non-sedimenting fraction of rat liver tissue the enzymatic activity was altered only slightly. Within the second half of a day the enzymatic activity redistributed in the cells with an increase of the activity in non-sedimenting fraction, caused by labilization of lysosomal membranes.
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PMID:[Diurnal changes in the lysosomal enzyme activity of the liver of mice and rats]. 642 29

The acid hydrolases alpha-glucosidase, beta-galactosidase, N-acetyl-beta-D-hexosaminidase, beta-glucocerebrosidase and cathepsin D were studied immunocytochemically in normal and mutant human cells using monoclonal and affinity-purified polyclonal antibodies. For light microscopy, Rhodamine or Fluorescein-labelled conjugates were used, and for electron microscopy protein A-gold conjugates were employed. With the double labelling procedure, it was found that in normal fibroblasts every lysosome contained all the enzymes studied. The method described also enabled us to demonstrate the presence or absence of mutant enzyme protein in fibroblasts derived from patients with a genetic lysosomal enzyme deficiency. Immunoreactive acid hydrolases or their precursor forms were found in the rough endoplasmic reticulum, the cisternae of the Golgi complex, Golgi associated vesicles and lysosomes. This is in agreement with the present concept that the Golgi complex plays an essential role in the processing and targeting of lysosomal enzymes.
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PMID:Immunocytochemistry of lysosomal hydrolases and their precursor forms in normal and mutant human cells. 648 Mar 99

Changes in activities of a new proteinase cathepsin T as well as some other lysosomal acid proteinases and hydrolases were examined in liver homogenate from rats treated with a single hepatotoxic dose of carbon tetrachloride. The most striking changes were several-fold increases of liver cathepsin T and D activities over their levels in untreated rats 3 days after administration of the agent to rats. Increase of cathepsin T was greater than that of cathepsin D at all doses of the hepatotoxin examined. The activities of N alpha-benzoyl-DL-arginine 2-naphthylamide hydrolase, acid phosphatase, beta-galactosidase and beta-glucuronidase in poisoned rat liver were unchanged or only slightly increased. Cathepsin T and D activities were less enhanced in mitochondrial lysosomal fractions than in the homogenate, and were greatly elevated in the supernatant fractions of liver from the treated rats. As judged from the molecular weights, the elevated activities of cathepsins T and D in the treated rat liver could be attributable to the two cathepsins themselves and not to other proteinases. Administration to rats of other hepatotoxic agents, thioacetamide and dimethylnitrosamine, also induced the elevation of the two cathepsin activities in liver, but on partial hepatectomy the activities of liver cathepsins T and D did not show such marked increases. Nonparenchymal liver cell fractions were responsible for almost all the increased activities of liver cathepsins T and D. It is possible that cathepsins T and D play a role in the heterolytic breakdown of hepatocyte molecules following CCl4 poisoning.
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PMID:Increased activities of liver cathepsins T and D in carbon tetrachloride-treated rats. 649 24

Enzymatic activity was investigated in metal-binding proteins from rat epidermal cells. Tris-HCl buffer soluble and KSCN solubilized proteins were extracted stepwise from granular and cornified cells of 2-day old rat epidermis. Each extract was separately applied to a Cu2+ or Zn2+ chelate Sepharose 6B column and the proteins were eluted with buffers of different pHs and finally with EDTA solution. Metal chelate-binding proteins were found in both soluble and solubilized proteins but there was a larger amount in the latter. Affinity of the proteins to bind with Cu2+ chelate was greater than that with Zn2+ chelate. In Tris-HCl buffer extract, histidase activity was detected in Cu2+ chelate-binding proteins, but not in Zn2+ chelate-binding proteins. Acid phosphatase, cysteine proteinase, dipeptidase, cathepsin D, beta-galactosidase, gelatin hydrolase, and superoxide dismutase did not bind to metal chelates although these enzymes, except acid phosphatase, were inhibited by Cu2+, but not by Zn2+. In contrast, KSCN solubilized metal chelate-binding proteins showed plasminogen activator, acid phosphatase, and gelatin and casein hydrolases while histone hydrolase did not bind to either chelate column. Since metal-binding proteins in rat epidermal cells have been shown previously to be histidine- and cysteine-rich proteins concentrated in keratohyalin granules, interaction of metals and the structural proteins with certain enzymes may be involved in the regulation of epidermal cell functions.
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PMID:Enzymatic activity of metal-binding proteins in epidermal cells. 653 44

It has been shown that low concentrations of E. coli lipopolysaccharides (LPS) greatly and selectively stimulate phagocytosis and related functions in mouse bone marrow-derived macrophages. Culture in the presence of 50 ng/ml LPS induced on average a 10-fold enhancement of phagocytosis of IgG-coated sheep erythrocytes. Activation was in two stages--a small increase observed during the first 8 to 12 hr, and the major increase noted between 16 and 24 hr. Phagocytic activity remained at the maximal level for 24 hr and then declined progressively. Stimulation by LPS was dose-dependent; significant effects could be observed at 0.8 ng/ml and the maximum was reached at 10 ng/ml. LPS-treated cells also showed a markedly increased tendency to form colonies. All these effects could be prevented by the addition of 100 ng/ml polymyxin B together with LPS, indicating that the active principle is lipid A. The LPS-dependent increase in phagocytic activity is probably mediated by increased Fc receptor capacity because both parameters were influenced in parallel by the stimulus. Phagocytosis-related events, such as enhanced hexose monophosphate shunt activity, H2O2 formation, and nitroblue tetrazolium reduction were also stimulated by LPS. By contrast, pinocytosis was unaffected. Measurements of cell-associated enzyme activities showed that lactate dehydrogenase, acid phosphatase, and cathepsin D were significantly increased. Beta-glucuronidase, beta-galactosidase, alkaline phosphodiesterase, and aminopeptidase were unchanged and NAD nucleosidase was markedly decreased after LPS treatment. 5'-Nucleotidase and glucosamine uptake were undetectable both in control and LPS-stimulated cells. LPS treatment induced a significant increase in cell-associated protein, but did not result in cell proliferation or increased cell loss as shown by the DNA content that remained constant. LPS-induced changes were dependent on de novo protein synthesis; cycloheximide prevented enhancement of phagocytosis, Fc receptor capacity, and colony formation.
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PMID:Stimulation of phagocytosis in bone marrow-derived mouse macrophages by bacterial lipopolysaccharide: correlation with biochemical and functional parameters. 673 51

The specific activity of three lysosomal proteinases (cathepsins B1, D, and L) as well as acid phosphatase and beta-galactosidase has been determined in the liver of both 7-10 day-old and young adult rats. Cathepsin B1 in suckling rats is markedly lower than in adults, while cathepsin D is only moderately lower and cathepsin L does not significantly differ. The activity of acid phosphatase is similar in the two groups of animals whereas that of beta-galactosidase in suckling rats is approx. twice as high as in adults. The activity of lysosomal hydrolases thus appears to be regulated individually during the development. Moreover it is suggested that the low activity of cathepsin B1 may be related to the low rate of cell protein catabolism characteristic of the developing liver (Conde and Scornik, 1977).
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PMID:Lysosomal hydrolase activities in the developing rat liver. 677 67


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