Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.21 (beta-glucosidase)
 3,280 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The changes in the activities of certain lysosomal hydrolases, viz., beta-glucuronidase, beta-N-acetylglucosaminidase, beta-galactosidase, beta-glucosidase, alpha-glucosidase, alpha-galactosidase, alpha-mannosidase, cathepsin B, cathepsin D, and collagenolytic cathepsin, in serum and heart of rats subject to myocardial infarction with isoproterenol, were studied during the periods of peak infarction and recovery. The activities of all the enzymes assayed exhibited a significant increase both in serum and in heart at peak infarction stage and these levels returned to normal during the stage of recovery and repair. The infiltration of inflammatory cells at the infarct regions and the altered lysosomal fragility are probably responsible for the increased activity of the enzymes studied. This may also bring about the catabolism of connective tissue constituents as reported in literature.
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PMID:Influence of isoproterenol-induced myocardial infarction on certain glycohydrolases and cathepsins in rats. 201 10

Adler and Martin (1983, Curr. Eye Res. 2, 359-66) found cathepsin D to be present in crude preparations of bovine interphotoreceptor matrix (IPM). The purpose of the present study was to determine, by investigating several acid hydrolases in purer IPM samples, whether hydrolytic enzymes abundant in RPE lysosomes were present also as normal components of the IPM. IPM was prepared from bovine eyes by the introduction of a small bleb of buffer between the neural retina and the RPE. These IPM samples were free from significant contamination by surrounding tissues; they contained IRBP as their only major protein, and had negligible amounts of lactate dehydrogenase and ROS-specific proteins. Most acid hydrolases were assayed fluorometrically by measuring the 4-methylumbelliferone released upon hydrolysis of appropriate derivatives; the substrate for cathepsin was hemoglobin. The amounts of the enzymes found in the IPM were far from uniform and could not be correlated with enzyme activities in either RPE or retina homogenates. The hydrolases in the IPM varied in amount from beta-galactosidase (28% of the RPE level), through N-acetyl-beta-glucosaminidase (20%), alpha-fucosidase (15%), beta-glucuronidase (12%), alpha-glucosidase (8%), cathepsin D (7%), alpha-mannosidase (7%), down to beta-glucosidase, acid phosphatase, and acid lipase (trace amounts, less than 1%). These results agree with the relative amounts of enzymes found by Wilcox (1987) to be secreted into the medium by cultured human RPE cells. Furthermore, the rank order of hydrolases in the IPM is the same as that for hydrolases secreted (but not recaptured) by human fibroblasts in I-cell disease. The conclusion from these correlations is that lysosomal enzymes are probably secreted, as a normal process, by the RPE into the IPM, where they may have a role in digesting shed outer segments and in catabolizing IPM components.
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PMID:Selective presence of acid hydrolases in the interphotoreceptor matrix. 261 85

To study the role of lysosomal enzymes in glomeruli, we examined specific activities of lysosomal hydrolases in isolated glomeruli and, for comparison in isolated tubules, from rat kidney cortex of normal animals and animals with puromycin aminonucleoside nephrosis (PAN). Nephrotic syndrome was induced in rats by a single intraperitoneal injection of aminonucleoside and the rats were sacrificed at the time of peak proteinuria. Colloidal iron staining of renal cortex demonstrated decreased staining for the epithelial polyanion in animals with PAN. Lysosomal enzymes were determined by fluorogenic and colorimetric methods. In normal kidney, total specific activities of cathepsin beta 1, beta-2-fucosidase, acetyl-beta-glucosaminidase, and arylsulfatase were lower in glomeruli compared with tubules and with tissue slices of the same kidney. Total activity of acid phosphatase was higher in glomeruli than tubules. In glomeruli of PAN rats, there were lower activities of N-acetyl-beta-glucosaminidase, D-fucosidase, beta-glucosidase, beta-glucoronidase, and arylsulfatase compared with control rats. Activity of acid phosphatase, on the other hand, was higher in glomeruli of PAN than control rats. All differences were statistically significant. These studies demonstrate that (1) activities of lysosomal enzymes in normal glomeruli and in glomeruli of nephrotic rats have a property distinct from the rest of the kidney, and (2) the specific activities of lysosomal hydrolases are altered in glomeruli of rats with PAN. These studies suggest that changes in activities of lysosomal enzymes may be related to pathogenesis of this glomerulopathy.
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PMID:Activities of lysosomal enzymes in isolated glomeruli. Alterations in experimental nephrosis. 732 25

The impact of ovarian hormones and corticosterone acetate on uterine connective tissue degrading enzymes were studied in mature albino rats. Ovariectomy resulted in a significant increase in the activities of alpha- and beta-galactosidases and glucosidases in the uterus. Administration of estradiol to ovariectomized rats brought back the activities of alpha-galactosidase and alpha-glucosidase to normalcy. While beta-galactosidase and beta-glucosidase were significantly decreased. Administration of progesterone to ovariectomized rats resulted in the increase of alpha- and beta-galactosidases and glucosidases. Administration of corticosterone to ovariectomized rats produced a further increase in alpha- and beta-galactosidases and glucosidases in the uterus. Adrenalectomy in ovary intact rats produced a decrease in alpha-galactosidase however, beta-glucosidase was significantly increased. Administration of corticosterone to ovary intact rats significantly increased the activities of alpha- and beta-galactosidases, while alpha- and beta-glucosidases were found to be decreased. Ovariectomy resulted in a significant increase in the activities of cathepsin-D and cathepsin-E. Administration of estradiol to ovariectomized rats brought back the activity of cathepsin-D to normalcy, whereas cathepsin-E was significantly increased. Administration of progesterone as well as estradiol to ovariectomized rats significantly increased the levels of cathepsin-E, however, cathepsin-D was brought back to normalcy. Administration of corticosterone to ovariectomized rats as well as ovariectomy + adrenalectomy significantly increased the activity of cathepsin-D and cathepsin-E. Adrenalectomy significantly decreased the activity of cathepsin-D, while administration of corticosterone increased the cathepsin-D and cathepsin-E in the uterus. Therefore, these results suggest that estradiol is a potent ovarian steroid protecting the extra cellular matrix components. The effect of progesterone appears to modulate and act hand in hand with estradiol. Corticosterone appears to have an opposite effect to that of estradiol.
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PMID:Interaction of estradiol, progesterone and corticosterone on uterine connective tissue degrading enzymes. 955 57

The present study was designed to evaluate the possible beneficial effect of lipoic acid in preventing the renal damage induced by cyclosporine A in rats. Male albino rats of Wistar strain were divided into four groups and treated as follows. Two groups received cyclosporine A by oral gavage (25 mg/kg/body weight) for 21 days to induce nephrotoxicity, one of which simultaneously received lipoic acid treatment (20 mg/kg body weight) for 21 days. A vehicle (olive oil) and a lipoic acid drug control were also included. Cyclosporine A induced renal damage was evident from the decreased activities of tissue marker enzymes (alkaline phosphatase, acid phosphatase, lactate dehydrogenase, aspartate transaminase and alanine transaminase) and decreased activities of ATPases (Na+, K+-ATPase, Ca2+-ATPase and Mg2+ ATPase). An apparent increase in the levels of serum constituents (urea, uric acid and creatinine) and urinary marker enzymes (N-acetyl-beta-D-glucosaminidase, beta-glucosidase, beta-galactosidase, cathepsin-D and gamma-glutamyl transpeptidase) along with significant decline in creatinine clearance were seen in the cyclosporine treated rats, which was reversed upon treatment with lipoic acid. Ultrastructural observations were also in agreement with the above abnormal changes. Lipoic acid effectively reverted these abnormal biochemical changes and minimized the morphological lesions in renal tissue. Hence, this study clearly exemplifies that lipoic acid might be an ideal choice against cyclosporine A induced cellular abnormalities.
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PMID:Therapeutic efficacy of DL-alpha-lipoic acid on cyclosporine A induced renal alterations. 1761 14

In this study, S-allyl cysteine sulfoxide (SACS) was used to evaluate its preventive effect in isoproterenol (ISO)-induced myocardial ischemia in male Wistar rats. Rats were pretreated with SACS (40 and 80 mg kg(-1)) orally for 5 weeks. After the treatment period, ISO (150 mg kg(-1)) was administered subcutaneously to rats at an interval of 24 h for 2 days. The activities of beta-D-N-acetyl-glucosaminidase, beta-galactosidase, beta-glucosidase, and acid phosphatase increased in serum and heart in ISO-induced rats. In addition, these rats showed a significant (p < 0.05) increase in the activities of beta-glucuronidase and cathepsin-D in serum and heart and a significant (p < 0.05) decrease in their activities in lysosomal fraction of the heart. The activity of Na(+)K(+)-ATPase declined, while those of Ca(2+)- and Mg(2+)-ATPases significantly (p < 0.05) elevated in the heart of ISO-induced rats. Pretreatment with SACS (40 and 80 mg kg(-1)) showed a significant (p < 0.05) effect in all the biochemical parameters studied. The effect at a dose of 80 mg kg(-1) body weight was more effective than that at 40 mg kg(-1) body weight and brought back all the biochemical parameters to near normal levels. Hereby, our study shows the membrane-stabilizing as well as antioxidant effects of SACS in ISO-induced rats.
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PMID:Preventive effect of S-allyl cysteine sulfoxide (alliin) on lysosomal hydrolases and membrane-bound ATPases in isoproterenol-induced myocardial infarction in Wistar rats. 1762 87

The objective of the present study was to investigate whether lysosome is a target in benzo(a)pyrene-induced, oxidative stress-mediated lung cancer in Swiss albino mice and the plausible role of the phytochemical substance capsaicin in mitigating lysosomal damage. Oxidative stress was assessed based on the level of carbonyl content. The activities of lysosomal proteases like cathepsin-D, cathepsin-B, beta-D-glucosidase, beta-D-galactosidase, beta-D-glucuronidase, beta-D-N-acetylglucosaminidase and acid phosphatase were assessed to evaluate lysosomal function. Administration of benzo(a)pyrene (50 mg/kg body weight) to mice induced a increase in the activities of lysosomal enzymes and oxidative stress was evident by the increase in carbonyl content. Treatment with capsaicin (10 mg/kg body weight) decreased carbonyl content and restored the activities of lysosomal enzymes to near normalcy. Transmission electron microscopic study of lysosomes further showed the defensive action of capsaicin against the lysosomal damage caused in benzo(a)pyrene-induced lung cancer. From the present study, it can be concluded that lysosomal damage is an indispensable event in benzo(a)pyrene-induced lung cancer, and capsaicin was able to effectively prevent it, which proves the chemoprotective effect of capsaicin against benzo(a)pyrene-induced experimental lung carcinogenesis.
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PMID:Lysosomal abnormalities during benzo(a)pyrene-induced experimental lung carcinogenesis--defensive role of capsaicin. 1920 42