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)

The effects of botulinum toxin (type A) induced muscle paralysis on endocytosis and lysosomal enzyme activities in skeletal muscle were compared with the effects of surgical denervation. Muscle atrophy, measured as decrease in total muscle protein content, was as large or larger after botulinum toxin treatment as after denervation. Endocytic activity, measured as the in vitro uptake of horseradish peroxidase, and the specific activities of the lysosomal enzymes N-acetyl-beta-D-glucosaminidase and cathepsin D were all increased six days after denervation. Only the specific activity of cathepsin D was increased six days after botulinum toxin poisoning. The uptake of horseradish peroxidase and the specific activity of N-acetyl-beta-D-glucosaminidase were also increased eleven days after poisoning. Transverse sections of eleven days botulinum poisoned muscles from animals injected with horseradish peroxidase showed fibres with dense peroxidase staining similar to those seen in denervated muscle although they seemed to occur less frequently. The results show that increases in endocytic activity and lysosomal enzyme activities may occur in skeletal muscle without the presence of degenerating axons. The differences in effects of surgical denervation and botulinum toxin induced paralysis are discussed in terms of what is known about the mechanism of action of botulinum toxin and the possible functional roles of the two lysosomal enzymes studied.
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PMID:Effects of botulinum toxin induced muscle paralysis on endocytosis and lysosomal enzyme activities in mouse skeletal muscle. 376 72

Lysosomal enzyme activities in pancreatic islets of obese hyperglycemic ob/ob mice aged 3 to 6 months were investigated and compared with those of normal lean NMRI mice of the same age. It was observed that the glycogenolytic glucose-producing hydrolase acid amyloglucosidase displayed a fivefold higher activity in the islets of obese mice than in the islets of normal NMRI mice. However, other islet lysosomal enzyme activities measured, such as N-acetyl-beta-D-glucosaminidase and beta-glucuronidase, were of the same magnitude in both obese and lean mice. A starvation period of 24 hours induced a significant depression of islet acid amyloglucosidase activity in obese as well as lean mice, whereas the activities of N-acetyl-beta-D-glucosaminidase and beta-glucuronidase were unaffected. Further, the activities of other types of islet lysosomal enzymes, such as acid phosphatase and cathepsin D, were also measured in obese mice. These activities were not found to be affected by the actual fasting period. A good correlation (r = 0.815; P less than 0.01) was observed between islet acid amyloglucosidase activity and plasma insulin concentrations in obese mice, whereas no such relationship was apparent with regard to other islet lysosomal enzyme activities recorded. Acid amyloglucosidase activity in liver tissue of the obese mouse was about 30 times lower than that of islet tissue. Further, the activity of liver amyloglucosidase was of the same order of magnitude in obese and lean mice. Similarly, other lysosomal enzyme activities in the liver of obese and lean mice were not strikingly different.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Lysosomal enzyme activities in pancreatic islets from normal and obese hyperglycemic mice. 391 27

The effects of hormonal or cholinergic stimulation on survival and on activities of lysosomal enzymes and amylase in pancreatic tissue and ascites were studied in rats with induced pancreatitis. Pancreatitis per se caused an increase of the activities of cathepsin D, N-acetyl-beta-D-glucosaminidase and amylase, and a decrease of acid phosphatase in pancreatic tissue. Pancreatic protein concentration was not influenced. In pancreatitic rats administration of cerulein or carbachol markedly decreased survival rate. Cerulein increased the activities of cathepsin D and amylase in ascites and cathepsin D and acid phosphatase in pancreatic tissue. Carbachol increased the activities of cathepsin D and amylase in ascites and acid phosphatase in pancreatic tissue. Both cerulein and carbachol decreased the activity of amylase in pancreatic tissue. Administration of secretin or the anticholinergic drug Pro-Banthine did not influence survival rate or the activities of lysosomal enzymes and amylase in ascites. In pancreatic tissue the activity of acid phosphatase was slightly increased by secretin or Pro-Banthine. In conclusion, the results show a nonparallel alteration of lysosomal enzyme activities in pancreatic tissue in rats with pancreatitis. Cerulein and cholinergic stimulation decreased survival rate and brought about a marked increase of cathepsin D activity in ascites and, in the case of cerulein, also in pancreatic tissue. The implication of lysosomes and especially the catheptic proteases in the pathogenesis and outcome of acute pancreatitis deserves further attention.
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PMID:Hormonal and cholinergic effects on amylase and lysosomal enzyme activities in pancreatic tissue and ascites of rats with acute experimental pancreatitis. 619 36

Hormonal and cholinergic influences on lysosomal and digestive enzyme activities in pancreatic tissue were studied in normal adult rats. Hormonal stimulation by the cholecystokinin analogue, caerulein, induced a marked enhancement of the activities of cathepsin D and N-acetyl-beta-D-glucosaminidase in pancreatic tissue, whereas the activities of amylase and lipase tended to decrease. Acid phosphatase activity was not affected. Further, caerulein was found to induce a significant increase of cathepsin D output in bile-pancreatic juice. This output largely parallelled that of amylase. Cholinergic stimulation by the muscarinic agonist carbachol, at a dose level giving the same output of amylase as caerulein, did not affect pancreatic activities of cathepsin D and N-acetyl-beta-D-glucosaminidase. Further, cholinergic stimulation induced an increase of amylase activity and a slight decrease of acid phosphatase activity in pancreatic tissue. Lipase activity was not affected. No apparent effect on cathepsin D output in bile-pancreatic juice was encountered after cholinergic stimulation. The activities of neither the digestive nor the lysosomal enzymes were influenced by the administration of secretin. The results suggest a possible lysosomal involvement in caerulein-induced secretion and/or inactivation of pancreatic digestive enzymes, whereas cholinergic stimulation seems to act through different mechanisms.
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PMID:Hormonal and cholinergic influences on pancreatic lysosomal and digestive enzymes in rats. 619 43

Guinea pigs were exposed to silica dust (SiO2) aerosols at 6, 13, 28, and 46 mg/m3 for 3 weeks and examined 4, 8, 16, and 23 weeks later. Twenty-four milligrams of TiO2 per cubic meter served as the control dust. Lung weights were increased at 8 weeks and later. Free lung cells showed a tendency to decrease in phagocytosis capacity at 8 weeks after cessation of exposure and later. Alveolar macrophage production of N-acetyl-beta-D-glucosaminidase, cathepsin D, and acid phosphatase was decreased at 8 weeks after exposure and later. The relationship between the depressant effect on macrophages and the absence of an exposure-related polymorphonuclear neutrophil response for the development of fibrosis could be part of the mechanism behind fibrosis.
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PMID:Pulmonary macrophage phagocytosis and enzyme production after in vivo exposure to silica dust. 630 49

Lactate dehydrogenase (LDH) and lysosomal enzyme activity were measured in lung lavage fluid of guinea pigs exposed for 3 weeks to different concentrations of silica dust. Eight weeks and later after cessation of exposure, the amounts of N-acetyl-beta-D-glucosaminidase, cathepsin D, acid phosphatase, and LDH were increased. It is suggested that this increase indicates cell damage to alveolar macrophages, and that the enzyme changes are of relevance to determine the risk for pulmonary fibrosis caused by airborne substances.
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PMID:Enzymes in lung lavage fluid after inhalation exposure to silica dust. 632 42

The spatial distribution of horseradish peroxidase (HRP) uptake has been studied by light- and electron microscopy in the denervated hemidiaphragm of the mouse. Segments with high HRP uptake were observed in a band centrally located in the denervated muscle. This distribution is similar to the well-known innervation pattern of the diaphragm. Ultrastructural studies demonstrated a high incidence of postsynaptic folds in close proximity of fibre areas with high intracellular content of HRP. 8-12 days after denervation a large number of fibres showed segments of high HRP uptake. 2-4 days after denervation very few such segments were observed. Biochemical studies also demonstrated an increase in HRP uptake after denervation occurring primarily in the endplate region. The activities of the lysosomal enzymes N-acetyl-beta-D-glucosaminidase, acid phosphatase and cathepsin D all increased after denervation, most prominently in the endplate region. It is suggested that the observed segmental uptake of HRP and lysosomal activation reflects a process for rapid membrane turnover in denervated muscle.
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PMID:Uptake of horseradish peroxidase in denervated skeletal muscle occurs primarily at the endplate region. 653 Jun 15

The properties of skeletal muscle lysosomes from normal and dystrophic chickens were studied to assess their involvement in the dystrophic process. A method is described for isolation of a three-to-sevenfold purified lysosome fraction with 29-33% yield. Lysosomal enzymes in crude homogenates and isolated lysosome-enriched fractions from dystrophic muscle exhibit decreased latency for N-acetyl beta-D-glucosaminidase, acid phosphatase, and cathepsin D. However, no differences in the fragility of lysosomes in isolated lysosome-enriched fractions from normal and dystrophic muscle were observed using shear, sonication and detergent stress. Lower percent recovery, enrichment factor and percent latency of acid phosphatase compared to N-acetyl-beta-D-glucosaminidase and cathepsin D were observed from both normal and dystrophic muscle. These results are consistent with the presence of a significant amount of nonlysosomal acid phosphatase activity in skeletal muscle.
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PMID:Skeletal muscle lysosomes: comparison of lysosomes from normal and dystrophic avian pectoralis muscle as a function of age. 685 5

The catalytic activities of 4 glycosidases (hyaluronate-4-glycanohydrolase (EC 3.2.1.35), beta-N-acetyl-D-glucosaminidase (EC 3.2.1.30), beta-glucuronidase (EC 3.2.1.31), alpha-L-iduronidase (EC 3.2.1.76)), of the arylsulphatases A and B (EC 3.1.6.1) and of the protease cathepsin D (EC 3.4.23.5) were measured in extracts from hepatocytes and non-parenchymal cells and in serum during the development of thioacetamide-induced rat liver fibrosis (22 weeks). In non-parenchymal liver cells the catalytic activities of beta-N-acetyl-D-glucosaminidase, beta-glucuronidase, alpha-L-iduronidase and cathepsin D were increased significantly during chronic liver damage, but that of hyaluronate-4-glycanohydrolase was reduced by 40 to 65% during the period of application of thioacetamide. The catalytic activities of the arylsulphatases were lowered by 65% compared to control values in the 12th week but with advancing liver damage the catalytic activities returned to nearly normal values. Parenchymal cells of rats, which had been liver-damaged for 6 months, contained strongly elevated activities of beta-glucuronidase, beta-N-acetyl-D-glucosaminidase, arylsulphatases A and B, and cathepsin D but only slightly increased activities of hyaluronate-4-glycanohydrolase and alpha-L-iduronidase, respectively. In the serum of liver-damaged rats the activity of alpha-L-iduronidase was strongly elevated, while that of N-acetyl-beta-D-glucosaminidase was only slightly increased. The activities of beta-glucuronidase and of arylsulphatases A and B were decreased during the whole period of treatment. The catalytic functions of hyaluronate-4-glycanohydrolase and of cathepsin D, respectively, were decreased initially, but both enzyme activities were elevated during the more advanced stages of long term thioacetamide treatment.
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PMID:Changes in the catalytic activities of proteoglycan-degrading lysosomal enzymes in parenchymal and non-parenchymal liver cells and in serum during the development of experimental liver fibrosis. 687 76

Activities of lysosomal enzymes (acid phosphatase, N-acetyl-beta-D-glucosaminidase, acid lipase and cathepsin D) have been examined in a synchronized culture of mouse L-fibroblasts. Cell synchronization was achieved by the double thymidine block with a subsequent mitotic selection after colcemid treatment. Specific activities of the enzymes studied were found to be higher in S-G2 that in G1. There is a linear increase (approximate doubling) in enzyme activities per cell from G1 to M. Activity of galactosyltransferase, a marker of the Golgi apparatus, declined in mitotic cells in comparison with the interphase cells. Ultrastructural examination of L-cells revealed a reduction of the intracellular membrane system including the Golgi apparatus during mitosis. Changes in the Golgi apparatus activity have been considered as a possible regulatory point of lysosome formation. The data presented are compared with the results of morphological studies of lysosomal system in L-cells.
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PMID:[Changes in lysosomal enzyme activity in the mitotic cycle of L cells]. 687 15


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