Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.4.23.5 (cathepsin D)
4,130 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Changes of cardiac, sceletal and hepatic lysosomes effected by three different variants of balanced isocaloric diets: 1--basic, 2--protein-lipid and 3--carbohydrate, with ratios of proteins, lipids and carbohydrates in mass 1.0:0.35:2.6; 1.0:0.48:0.67; and 1.0:1.3:10.9, respectively, were studied. Activities of enzymes participating in degradation of carbohydrates (beta-glucosidase, beta-N-acetyl-glucosaminidase) were more increased in the animals fed with the carbohydrate diet. Activation of proteolytic enzymes (cathepsin D) was observed in tissues of rats taking the protein-lipid food. As a rule physical exercise exerts lysosomal enzymes activation and their membrane labilization in rats maintained on the basic diet. Reversial reactions of lysosomes to physical exercise is observed in animals receiving the carbohydrate diet for along time that is expressed in increasing the total activity of lysosomal hydrolases and stabilizing the lysosomal membranes. On the contrary, maintaining the animals on the protein-lipid diet is followed by a more pronounced activation of the lysosomal apparatus of tissues as compared to the basic diet.
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PMID:[Effect of nutrition on lysosomal function during physical loading]. 373 10

Activity of lysosome enzymes (acidic phosphatase, beta-glucosidase, DNAase, RNAase and cathepsin D) is determined for its variation in different organs of rainbow trout during complete fasting. It is shown that the activity of most enzymes of concern almost in all organs except skeletal muscles is on the higher level in trouts fasted for 30 days than in the control ones. With an increase of the fasting term to 60 days the acid phosphatase, DNAase, RNAase activity decreases while the glucosidase and cathepsin D activity in some organs increases. Variations detected in the enzyme profile of the trout lysosomes under fasting are of adaptive character.
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PMID:[Changes in the activity of trout lysosomal enzymes during fasting]. 392 43

Liver tissue cirrhosis, developed in rats after long-term administration of CCl4, led to distinct increase in activities of acid phosphatase, acid DNAase, cathepsin D, beta-galactosidase and beta-glucosidase. When the treatment with the hepatotropic toxins was stopped activity of lysosomal enzymes decreased slightly but was maintained at the high level. Within a day after a single administration of choriogonine distinct decrease as compared with the controls in activity of all the acid hydrolases studied was found. Within subsequent periods the lysosomal enzymes activity continued to decrease and within 2 months after the choriogonine treatment it was distinctly lower as compared with control animals.
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PMID:[Effect of choriogonine on the enzymatic activity of lysosomes in the cirrhotic liver in the rat]. 681 64

The mechanism underlying exhaustive exercise-induced release of lysosomal enzymes was studied in the rat liver. Exhaustive exercise resulted in the release of beta-glucuronidase and cathepsin D, but not beta-glucosidase and acid phosphatase, into the blood and cytosol, suggesting that the release of lysosomal enzymes is not due to disruption of lysosomal membranes. The intralysosomal pH of the liver, which was approximately 5.5 at the resting level, rose significantly after exhaustive exercise to pH 6.3. In vitro, beta-glucuronidase and cathepsin D were released at an intralysosomal pH exceeding 6.2. In contrast, beta-glucosidase and acid phosphatase were not released. The elevation of intralysosomal pH reduced the aggregation of beta-glucuronidase and cathepsin D. The rate of ammonia accumulation increased markedly in the lysosome-enriched subcellular fraction after exercise. There was a positive relationship between the rate of ammonia accumulation and the elevation of intralysosomal pH in vitro. Lysosomes isolated after exhaustive exercise showed significantly increased osmotic fragility. Our findings suggest that, during exhaustive exercise, the accumulation of ammonia in lysosomes leads to the elevation of intralysosomal pH, resulting in the reduced aggregation of certain lysosomal enzymes. Thus, less aggregated lysosomal enzymes may be released into the cytosol through the lysosomal membrane, the permeability of which has been increased.
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PMID:Intralysosomal pH and release of lysosomal enzymes in the rat liver after exhaustive exercise. 851 76

Alterations in the activities of certain lysosomal enzymes such as beta-D-galactosidase, beta-D-glucosidase, beta-D-glucuronidase, alpha-L-fucosidase, N-acetyl-beta-D-glucosaminidase, cathepsins B and D were studied in serum and tissue homogenates of buccal mucosa of hamsters treated with 0.5%, 7,12-dimethylbenz[a]anthracene (DMBA) in liquid paraffin. Among the enzymes studied, the activities of beta-D-galactosidase and N-acetyl-beta-D-glucosaminidase showed significant elevation both in serum and tissue homogenates fro papilloma onwards and the elevations were progressive with the development of carcinomas. The elevations in the activities of alpha-D-fucosidase and cathepsin D were found to be significant from papillomatous tissue onwards whereas in serum they showed higher activities only in carcinoma stages. The activities of beta-D-glucosidase, beta-D-glucuronidase and cathepsin B in both serum and in tissue homogenate were elevated markedly only in carcinoma stages. It is suggested that beta-D-galactosidase and N-acetyl-beta-D-glucosaminidase may be used as diagnostic markers for premalignant and malignant lesions of oral mucosa.
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PMID:Studies of the activities of lysosomal enzymes in serum and buccal pouch tissue of hamsters during 7,12-dimethylbenz[a]anthracene-induced carcinogenesis. 862 88

1. The effect of taxol on selected lysosomal enzymes (cathepsin D, lysosomal lipase, beta-glucuronidase, beta-glucosidase, alanine aminopeptidase) in mouse hepatocytes after 24-hr treatment by increasing doses (0.75 mg/kg bw, 1.25 mg/kg bw and 2.5 mg/kg bw) was studied. 2. The segments were also taken from the mice for ultrastructural studies with the use of electron microscopy. The greatest changes in activity of enzymes at the taxol dose of 2.5 mg/kg bw were as follows: the activity of cathepsin D increased by 71%, that of alanine aminopeptidase increased by 103%, that of beta-glucuronidase decreased by 45% and that of beta-glucosidase decreased by 63%. 3. The significant changes observed in the hepatocyte ultrastructure were closely correlated with biochemical changes that were dependent on the taxol dosage.
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PMID:Activity of lysosomal system in mouse liver after taxol administration. 950 80

Phosphatases, C4 and C8 esterases, leucine and valine aminopeptidases, N-acetyl-beta-glucosaminidase, beta-glucosidase, beta-galactosidase and beta-glucuronidase were detected in extracts of the parasitic mite Psoroptes cuniculi. Lipase, trypsin-like and chymotrypsin-like activities were not present. Haemoglobin was hydrolysed by a detergent-soluble fraction of the mite extracts with a maximum hydrolysis between pH 3 and 5. Acid proteinase activity was greater against haemoglobin than bovine serum albumin. Inhibitors of cysteine, serine and metallo-proteinases failed to inhibit the hydrolysis of H-Pro-Thr-Glu-Phe-Phe(NO2)-Arg-Leu-OH while pepstatin A inhibited its hydrolysis in a dose-dependent manner (IC50 8.02 x 10(-11) M (+/- 0.30 x 10(-11). Thermal inactivation of the proteolytic activity followed an exponential decay pattern. Typical K(m) and Vmax values were 7.2 x 10(-5) (+/- 0.7 x 10(-5) M-1 and 1.13 x 10(-3) (+/- 0.05 x 10(-3) OD unit-1 min-1 respectively. Acid proteinase activity eluted from a size exclusion column in a single, major peak representing a molecular weight range of 21-24.5 kDa. The major endoproteinase of P. cuniculi therefore appears to be a cathepsin D-like aspartic proteinase.
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PMID:Hydrolytic enzymes of Psoroptes cuniculi (Delafond). 1007 Jul 42

This paper deals with the study of infrasound phonophoresis-induced changes in biochemical factors, which affect the permeability of eyeball tissues. During 10 days, the rabbit right eye was exposed to an infrasound in the changing pressure mode at 4 Hz and 173 dB for 10 minutes every day. The left eye remained control. After finishing a series of studies, the animals were slaughtered, the eyes were enucleated and prepared into individual tissues. Changes in sodium-potassium composition were investigated in the first series. By causing a reduction in the cellular content of K+, infrasound exposure was found to cause a decrease in membranous potential and activation Na-channel, as confirmed by the elevated intracellular levels of Na+. This in turn enhances ocular tissue permeability for drugs without damaging the structure of a cell membrane. Changes in the activity of the following enzymes: beta-glucosidase, cathepsin D, and hy- aluronidase. Infrasound was ascertained to enhance the activity of beta-glucosidase, which accounts for the lower levels of glucose in ocular tissues and points to the activation and acceleration of biochemical processes in the tissues. At the same time the increased concentrations of cathepsin D and hyaluronidase found in ocular tissues were responsible for a temporary reduction in the viscosity of hyaluronic acid, which promotes resolution of opacities, adhesions or scars and increased tissue permeability.
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PMID:[Study of changes in the enzyme-salt composition affecting the permeability of ocular tissues under infrasound phonophoresis]. 1607 26

Acid beta-glucosidase (GCase) is a 497-amino acid, membrane-associated lysosomal exo-beta-glucosidase whose defective activity leads to the Gaucher disease phenotypes. To move toward a structure/function map for disease mutations, 52 selected single amino acid substitutions were introduced into GCase, expressed in an insect cell system, purified, and characterized for basic kinetic, stability, and activator response properties. The variant GCases from Gaucher disease patients and selected variant GCases from the mouse had decreased relative k(cat) and differential effects on active site binding and/or attachment of mechanism-based covalent (conduritol B epoxide) or reversible (deoxynojirimycin derivatives) inhibitors. A defect in negatively charged phospholipid activation was present in the majority of variant GCases but was increased in two, N370S and V394L. Deficits in saposin C enhancement of k(cat) were present in variant GCases involving residues 48-122, whereas approximately 2-fold increases were obtained with the L264I GCase. About 50% of variant GCases each had wild-type or increased sensitivity to in vitro cathepsin D digestion. Mapping of these properties onto the crystal structures of GCase indicated wide dispersion of functional properties that can affect catalytic function and stability. Site-directed mutagenesis of cysteine residues showed that the disulfide bonds, Cys(4)-Cys(16) and Cys(18)-Cys(23), and a free Cys(342) were essential for activity; the free Cys(126) and Cys(248) were not. Relative k(cat) was highly sensitive to a His substitution at Arg(496) but not at Arg(495). These studies and high phylogenetic conservation indicate localized and general structural effects of Gaucher disease mutations that were not obvious from the nature of the amino acid substitution, including those predicted to be nondisruptive (e.g. Val --> Leu). These results provide initial studies for the engineering of variant GCases and, potentially, molecular chaperones for therapeutic use.
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PMID:Analyses of variant acid beta-glucosidases: effects of Gaucher disease mutations. 1629 21

The effects of a new synthetic gestagen 17alpha-acetoxy-3beta-butanoyloxy-6-methyl-pregna-4,6-dien-20-on (ABMP) and reference drug progesterone on rat skin fibroblasts were evaluated by variations in lysosomal enzyme activity (cathepsin D and beta-glucosidase). Our results suggest that ABMP exhibits lysosomotropic properties, which depended on its concentration and time of treatment. The direct effect of progesterone on lysosomal enzyme activity in skin fibroblasts was compared to the influence of systemic treatment with gestagens on skin lysosomes. The data indicate that local application of gestagen preparations holds much promise for the therapy of skin diseases accompanied by increased proliferation (e.g. psoriasis).
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PMID:Activity lysosomal enzymes in rat skin fibroblasts after treatment with progesterone and new gestagen ABMP. 1902 99


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