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)

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

Pulmonary alveolar macrophages were isolated from adult, male New Zealand white rabbits by bronchial lavage and exposed to cadmium chloride in vitro. The observed cell sensitivity to this metal was highly dependent upon the incubation conditions used as well as the cytotoxic index selected. An LC50 value, as measured by dye exclusion (erythrosin B), was determined to be 390 microM when these cells were exposed to cadmium in Ham's F12 culture medium for 8 hr at 35 degrees C. The presence of fetal calf serum in the medium (10%; v/v) enhanced this toxicity slightly, LC50 = 235 microM, as did raising the incubation temperature to 37 degrees C, LC50 = 201 microM. No effect on cadmium toxicity was observed when the culture medium was made deficient in Cu, Zn, and Fe, nor was there any effect observed when Hepes buffer was substituted for the bicarbonate/carbon dioxide buffering system. Measurements of cadmium-109 uptake by pulmonary alveolar macrophages were consistent with and could explain, at least in part, the above observations of cytotoxicity. In the standard culture system (an 8-hr exposure period at 35 degrees C in Ham's F12 culture medium plus serum), the appearance in the culture medium of two lysosomal enzyme activities, acid phosphatase and cathepsin D, paralleled cell death. In addition, an EC50 value of 102 microM was found for cadmium when cell respiration (O2 uptake) was measured; an EC50 value of 31 microM was found for cadmium when cell function (engulfment of killed yeast particles) was followed; and scanning electron microscopic studies showed cell membrane changes (loss of fine structure and blebbing) at cadmium concentrations as low as 30 microM. These findings suggest that loss of cell function and/or changes in cell morphology are more sensitive measurements of macrophage exposure to cadmium than is either cell death, lysosomal enzyme release, or cell respiration.
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PMID:Toxicity of cadmium chloride in vitro: indices of cytotoxicity with the pulmonary alveolar macrophage. 394 38

This study was carried out to evaluate the influence of long-term treatment with doxorubicin (DXR) (4 mg/kg IV for 5 weeks) on heart and liver lysosomes of mice. We evaluated the variations in both total and "sedimentable" enzyme activity of cathepsin D, which is the major endopeptidase of myocites and probably involved in physiologic and pathologic degradation of actomyosin and mitochondria, and that of acid phosphatase, which is more prominent in interstitial cells. Our results show that marked changes occur in both total and sedimentable enzyme activity of cathepsin D in the heart of treated animals and to a lesser extent in the liver. In contrast, no modification of either total or sedimentable acid phosphatase was seen in either organ. The effects we observed are much more marked for cardiac cathepsin D; this is in good agreement with the cardiac specificity of DXR-induced cardiotoxicity with long-term administration and suggests that lysosomes could play a role in the pathogenesis of this phenomenon.
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PMID:Lysosomal alterations in heart and liver of mice treated with doxorubicin. 400 46

It has been shown in vitro that nonachlazine stabilizes rat myocardial lysosomal membranes and activates total acid phosphatase in homogenates of rat myocardium. Preliminary addition of nonachlazine to homogenates in two different final concentrations produces unequal changes in total and free activity of acid phosphatase and cathepsin D during 2.5-hour incubation of homogenates at 37 degrees C.
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PMID:[Effect of nonachlazine on the temperature sensitivity of the lysosomal membranes of the heart muscle in rats in vitro]. 402 78

The localization of cathepsin D-like acid proteinase in the rat stomach and other tissues was studied, and its biochemical properties were compared with those of rat gastric cathepsin D (EC 3.4.23.5). Cathepsin D-like acid proteinase existed overwhelmingly in the mucosal layer and was hardly detected in the gastric juice. Its subcellular distribution profile was very similar to that of acid phosphatase, but not to that of pepsinogen. This proteinase-like enzyme activity was also found in rat splenic extract. These results strongly suggest that the proteinase is a lysosomal enzyme. In addition, cathepsin D-like acid proteinase demonstrated an in vitro transition of molecular species during storage at -30 degrees C. Although this molecular change was distinctive in ion-exchange column chromatography and susceptibility to some enzyme inhibitors, it was not accompanied by a significant decrease in molecular weight. To compare cathepsin D-like acid proteinase with ordinary cathepsin D, gastric cathepsin D was newly purified to apparent homogeneity in polyacrylamide gel electrophoresis. Its biochemical properties demonstrate that this is a true cathepsin D in rat gastric mucosa. Moreover, this cathepsin D activity was not abolished by treatment with antiserum specific to cathepsin D-like acid proteinase or pepsinogen. From these results, we can conclude that the proteinase is a lysosomal acid proteinase different from newly purified gastric cathepsin D.
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PMID:A comparative study of two kinds of cathepsin D-type proteinases from rat gastric mucosa. 406 86

The effect of human growth hormone on arterial basement membrane-like (BM) material was studied. BM-like material was obtained from the cell layer of cultured aortic myomedial cells using a sonication-differential centrifugation technique. After the addition of small amounts of growth hormone (1 ng/ml) to the cultures, we observed a 26% increased incorporation of amino acids into BM-like material (2p less than 0.005). However, further increase in the incorporation was not observed using either 3 ng or 10 ng growth hormone per ml. Growth hormone inhibited removal/degradation of BM-like material by 16% (2p less than 0.01). However, pinocytosis rate and activity of major lysosomal enzymes: cathepsin D, acid phosphatase and beta-N-acetyl-glucosaminidase were unchanged. Incorporation of glycosaminoglycans as evaluated by [35SO4]-labelling was reduced by 8% when cells were exposed to growth hormone (2p less than 0.01). The present study demonstrates an effect of growth hormone on the turnover and composition of BM-like material in cultured arterial myomedial cells.
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PMID:Growth hormone effect on accumulation of arterial basement membrane-like material studied on rabbit aortic myomedial cell cultures. 409 60

The response of rat liver lysosomes to an intraperitoneal injection of glucagon has been evaluated from studies on the mechanical fragility, osmotic sensitivity, and sedimentation properties of these subcellular particles. It has been found that about (1/2) hr after the injection of glucagon the hepatic lysosomes exhibit a fairly sudden increase in their sensitivity to mechanical stresses and to exposure to a decreased osmotic pressure. At the same time, their sedimentation properties undergo complex changes characterized mainly by a significant increase in the sedimentation coefficient of a considerable proportion of the total particles. In addition, glucagon causes an increase in the proportion of slowly sedimenting particles, with the result that the distribution of sedimentation coefficients within the total population tends to become bimodal. The latter change is more pronounced for acid phosphatase, less so for cathepsin D, and barely detectable for acid deoxyribonuclease. All these modifications are maximal between 45 and 90 min after injection and regress to normal within approximately 4 hr. With the exception of the increase in the slow component, for which no explanation can be advanced at the present time, they are consistent with the hypothesis that glucagon causes an increase in lysosomal size, and may be related to the autophagic-vacuole formation known to occur after glucagon administration.
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PMID:Influence of glucagon, an inducer of cellular autophagy, on some physical properties of rat liver lysosomes. 429 15

Postnuclear supernates from homogenates of skeletal muscle from rats subjected to starvation, injections of Triton WR-1339, dextran-500, and dextran + corticosterone were fractionated by means of rate and isopycnic zonal centrifugation in sucrose-0.02 M KCl gradients. Zonal fractions were analyzed for protein, RNA, cytochrome oxidase, and up to six acid hydrolases. The results indicate the presence of two groups of lysosome-like particles. One group contributes approximately 95% of the cathepsin D and acid phosphatase activity and 75% of the acid ribonuclease, beta-glucuronidase, and arylsulfatase activity in muscle. It is characterized by a modal equilibrium density of 1.18 that is decreased by starvation, but is not shifted by dextran-500 or Triton WR-1339. The second group has a higher proportion of acid ribonuclease, beta-glucuronidase, and arylsulftase; the equilibrium density can be shifted by dextran-500 and Triton WR-1339. It is suggested that this group of lysosomes is derived from macrophages and other connective tissue cells, whereas the former group represents lysosome-like particles from muscle cells.
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PMID:Lysosomes in skeletal muscle tissue. Zonal centrifugation evidence for multiple cellular sources. 432 73

Homogenates of cultured rat embryo fibroblasts have been assayed for acid phosphatase, N-acetyl-beta-glucosaminidase, cathepsin D, acid deoxyribonuclease, cytochrome oxidase, NADH cytochrome c reductase, 5'-nucleotidase, inosine diphosphatase, acid pyrophosphatase, neutral pyrophosphatase, esterase, catalase, cholesterol, and RNA. The validity of the assay conditions was checked. Neutral pyrophosphatase is a readily soluble enzyme. Acid hydrolases, except acid pyrophosphatase, are particle-bound enzymes, which exhibit a high degree of structural latency. They are activated and solubilized in a parallel fashion by mechanical treatments and tensio-active agents. Catalase is also particle-bound and latent; activating conditions stronger than those for hydrolases are required to activate the enzyme. Acid pyrophosphatase, 5'-nucleotidase and inosine diphosphatase are firmly particle-bound, but not latent; they are not easily solubilized. In differential and isopycnic centrifugation, the latent hydrolases, cytochrome oxidase and catalase dissociate largely from each other; this suggests the occurrence of lysosomes and peroxisome-like structures besides mitochondria. The distribution patterns of 5'-nucleotidase and cholesterol are largely similar; digitonin influences their equilibrium density to the same extent; these two constituents are thought to be related to the plasma membrane. Inosine diphosphatase and acid pyrophosphatase are also partially associated with the plasma membrane, although some part of these enzymic activities probably belongs to other structures. NADH cytochrome c reductase is associated partly with the endoplasmic reticulum, partly with mitochondria.
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PMID:Analytical fractionation of homogenates from cultured rat embryo fibroblasts. 437 90

1. The density-gradient distribution patterns of acid phosphatase, Trypan Blue and denatured (125)I-labelled albumin were studied by discontinuous sucrose- and isopycnic sucrose-density-gradient centrifugation on combined heavy and light mitochondrial (M+L) fractions of liver isolated from normal rats and from rats injected with Triton WR-1339. 2. The results obtained from the subfractionation of the M+L pellet of normal animals indicate that the equilibrium density of Trypan Blue and acid-insoluble radioactivity is the same as that for acid phosphatase, which suggests they are bound by a common membrane to form a distinct subcellular population of lysosomal nature. 3. In contrast, the analysis of the isopycnic gradients obtained on subfractionation of M+L pellets of liver isolated from rats treated with Triton WR-1339 show that the acid-insoluble radioactivity has an equilibrium density around 1.21, whereas the acid hydrolases, including cathepsin D, show the characteristic shift to an equilibrium density of around 1.12. Trypan Blue is distributed along the gradient with distinct peaks at densities 1.22 and 1.12. 4. Similar equilibrium-density distribution patterns were obtained with M+L pellets isolated from rats pretreated with Triton WR-1339 but not injected with Trypan Blue. 5. Treatment of the rats with Triton WR-1339 does not affect albumin digestion of isolated intact lysosomes despite the fact that most of the cathepsin D and the albumin ingested by phagocytosis are located in different vacuoles. 6. It is concluded from these experiments that in the liver of animals treated with Triton WR-1339 (125)I-labelled albumin is located within heterophagosomes which do not fuse with heterolysosomes containing the non-ionic detergent Triton WR-1339. The inability of these two lysosomal populations to fuse is not due to Trypan Blue.
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PMID:The effect of triton WR-1339 on the subcellular distribution of trypan blue and 125 I-labelled albumin in rat liver. 477 28


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