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 activity of certain enzymes of energy metabolism (cytochrome c oxidase, citrate synthase, malate dehydrogenase, and lactate dehydrogenase) and of lysosomes (beta-glucuronidase, beta-N-acetylglucosamindase, arylsuphatase, ribonuclease, deoxyribonuclease, acid phosphatase, and cathepsin D) was assayed from m. rectus femoris of mice trained 5 days per week, 1 hr per day for 4 weeks according to 4 different programmes: I. running speed 20 m/min, horizontal track, II. 25 m/min, horizontal track, III. 20 m/min 8 degrees uphill inclination, and IV. 25 m/min 8 degrees uphill inclination. Oxidative capacity increased and anaerobic capacity decreased without distinction between the different traning programmes. Of acid hydrolases assayed the activities of beta-glucuronidase and cathepsin D were increased independently of training intensity. Simultaneous histochemical observations on beta-glucuronidase and arylsulphatase activities in the contralateral m. rectus femoris showed more intense staining in red as compared to white muscle fibres. It is suggested that training affected the red fibres and that the applied level of loading was probably too low to cause major involvement of white fibres.
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PMID:Oxidative and lysosomal capacity in skeletal muscle of mice after endurance training of different intensities. 21 99

The activities of beta-glucuronidase, beta-N-acetylglucosaminidase, arylsulphatase, ribonuclease, p-nitrophenylphosphatase, and malate dehydrogenase together with protein content were assayed from representative mixed (m. rectus femoris), predominantly red (proximal heads of m. vastus lateralis, m.v. medius and m. v. intermedius), and predominantly white (distal head of m. vastus lateralis) muscle homogenates of mice during a two-week period following one single exposure to exhausting intermittent running on a treadmill. The activities of cathepsin D and beta-glycerophosphatase were assayed from mixed muscle only. In all three muscle types, particularly in red muscle, the activities of beta-glucuronidase, beta-N-acetylglucosaminidase, arylsulphatase, and ribonuclease progressively increased between one to five days after the exercise; thereafter the activities began to decrease, being near the conrol values 15 days after the exercise. In mixed muscle, cathepsin D activity increased. No corresponding changes were observed in the activities of acid phosphatases. The time course of the activity changes closely resembled that earlier found to be caused by ischaemia in rabbit muscles. It is tentatively concluded that the two treatments, exhaustive exercise and temporary ischaemia, cause similar cell injuries, and that the lysosomal system involved seems to function similarly in the post-stress recovery of the fibres from these injuries.
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PMID:Acid hydrolase activity in red and white skeletal muscle of mice during a two-week period following exhausting exercise. 21 65

The activity of eight acid hydrolases and two energy metabolism enzymes were assayed from homogenates of predominantly red (proximal heads of m. vastus lateralis, m. vastus medialis, and m. vastus intermedius) and predominantly white (distal head of m. vastus lateralis) skeletal muscle of mice belonging to one of the following groups: 1) sedentary controls, never trained or exhausted; 2) exhausted controls, exhausted once by running on a treadmill 5, 10, or 20 days before killing; 3) trained mice, exercising until killed; 4) exhausted trained mice, exercising until exhausted 5, 10 or 20 days before killing, not exercising during that period; and 5) detrained mice, terminating training 5, 10, or 20 days before killing. In untrained but not in trained animals, exhaustive exercise caused, 5 days afterward, fiber necrosis and a marked increase in the activities of beta-glucuronidase, beta-N-acetylglucosaminidase, arylsulphatase, ribonuclease, deoxyribonuclease, cathepsin D, and cathepsin C, especially in red muscle fibers. Training increased the activities of citrate synthase, beta-glucuronidase, and cathepsin D in both muscle types and those of beta-N-acetylglucosaminidase, arylsulphatase, and cathepsin C in red muscle. Effects of detraining were minor. Exhaustive exercise causes lethal and evidently also sublethal fiber injuries manifesting themselves as an activation of the lysosomal system of muscle fibers 5 days later. Training affects cellular homeostasis by causing an apparent resistance to the damaging effects of exhaustive exercise. Moderately increased hydrolase activities may reflect increased turnover in endurance-trained muscles.
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PMID:Exhaustive exercise, endurance training, and acid hydrolase activity in skeletal muscle. 22 20

Intact and viable parenchymal and non-parenchymal liver cell preparations were isolated by enzyme perfusion techniques from young and old rats. The distribution of the lysosomal enzymes acid phosphatase, beta-galactosidase, cathepsin D, acid DNAse, and arylsulphatase B over parenchymal and non-parenchymal cells was determined. In addition, morphological and morphometric changes which occur in parenchymal cells with age were investigated. All lysosomal enzymes studied are present in both cell classes, but non-parenchymal cells possess much ligher activities per mg protein than do parenchymal cells. This phenomenon is most pronounced for cathepsin D with a 13-times higher specific activity in non-parenchymal cells. Electron microscopic observations demonstrated that the lysosomal activities in non-parenchymal cells can be attributed mainly to the large and numerous lysosomal structures in Kupffer cells. Parenchymal cells from old rats have higher lysosomal enzyme activities per mg protein than do hepatocytes from young rats. This observation is in agreement with the general increase with age in the cytoplasmic volume fraction occupied by lysosomal structures in parenchymal cells. In general, non-parenchymal cells show no increase in specific enzyme activities with age. The results obtained suggest an increase in the heterogeneity--in both appearance and enzyme content--of the lysosomal structures in parenchymal cells with age.
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PMID:Changes in lysosomes during ageing of parenchymal and nonparenchymal liver cells. 23 90

Activity of arylsulphatase, beta-glucuronidase, cathepsin D, and acid phosphatase in the homogenates of melanotic and amelanotic melanoma was determined. The activity of these enzymes is higher in melanotic than in amelanotic melanoma. Respective values for melanotic and amelanotic tumours are: arylsulphatase 10,78 +/- 3,20, and 1,45 +/- 0,66 micron 4-nitrocatechole/mg protein/hr; beta-glucuronidase 11,10 +/- 1,40, and 9,98 +/- 1,35 micron phenolphthalein/mg protein/hr; cathepsin D 4,24 +/- 1,37, and 3,26 +/- 0,73 micron tyrosine/mg protein/hr; acid phosphatase 230 +/- 22, and 180 +/- 25 micron p-nitrophenol/mg protein/hr. These differences are statistically significant. The increased activity of the lysosomal enzymes in melantoic melanoma probably depends on the occurrence of an higher number of lysosomes in tissues containing melanins.
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PMID:Activity of some lysosomal hydrolases in the homogenates of transplantable melanotic and amelanotic melanoma in golden hamster (Mesocricetus auratus, Waterhouse). 68 81

The effect of insulin on the concentration of different glycosaminoglycan (CG) fractions was different in different segments of aorta. Chondroitin sulphate A and heparin were increased in the aortic arch, thoracic and abdominal aorta, while chondroitin sulphate B and C were increased only in the aortic arch and abdominal aorta. Heparin sulphate and hyalutonic acid were increased only in the abdominal aorta. In the liver, significant increases occurred in all GG fractions. All enzymes studied which are involved in the biosynthesis of GG precursors, i.e. glucosaminphosphate isomerase, UDP glucose dehydrogenase and glucose-1-phosphate uridylyltransferase, were increased in the animals of the insulin group, while all enzymes involved in the degradation of GG, i.e. hyalurono glucosidase, beta-glucosaminidase, arylsulphatase, and cathepsin D, were decreased. Concentration of hepatic PAPS, activity of the sulphate-activiting system and sulphotransferase increased on administration of insulin.
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PMID:Insulin and metabolism of glycosaminoglycans in rabbits. 71 66

Parenchymal and nonparenchymal cells were isolated from the livers of female BN/BiRij rats, aged 3, 12, 24 and 30-35 months, by means of enzymatic techniques. About 70% of the cells in the nonparenchymal cell suspensions were endothelial cells and 25% were Kupffer cells. More than 90% of the isolated parenchymal, Kupffer and endothelial cells were viable as judged by trypan blue exclusion and ultrastructural appearance. The age-related changes in the specific activities of the lysosomal enzymes acid phosphatase, beta-galactosidase, cathepsin D and arylsulphatase B in parenchymal and nonparenchymal cells showed no correlated behavior. The most prominent change was observed for the cathepsin D activity in parenchymal cells, which nearly triples during the lifespan of the rat. A comparison of the activities obtained with homogenates of the whole liver and with parenchymal and nonparenchymal cells revealed that aging changes in lysosomal enzyme activities in homogenates should be carefully interpreted, since opposite patterns of change were often observed in the activities in parenchymal cells and in nonparenchymal cells.
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PMID:Lysosomal enzyme activities in parenchymal and nonparenchymal liver cells isolated from young, adult and old rats. 99 58

1. Rat kidney lysosomal glycoproteins, prelabelled in the N-acetylneuraminic acid and polypeptide portions with N-acetyl[(3)H]mannosamine and [(14)C]lysine, or with N-acetyl-[(14)C]glucosamine, were incubated under various conditions. Autolytic cleavage of labelled N-acetylneuraminic acid and peptide was maximum at pH5.0. 2. N-Acetylneuraminic acid was released more rapidly than peptide during incubation at 37 degrees or 4 degrees C at pH5. p-Nitrophenyloxamic acid, an inhibitor of bacterial neuraminidase (Edmond et al., 1966), inhibited the cleavage of N-acetylneuraminic acid and peptide, and also inhibited cathepsin D activity. 3. Galactono-, mannono-, and glucono-lactone, inhibitors of the corresponding glycosidases, blocked the autolytic cleavage of N-acetyl[(14)C]glucosamine and protein without inhibiting beta-N-acetylhexosaminidase or cathepsin D activity. These findings suggest that the carbohydrate side chains protect the polypeptide portion of the lysosomal glycoproteins against proteolytic attack by lysosomal cathepsins. 4. In electrofocusing experiments, autolysis was minimized by adding 0.1% p-nitrophenyloxamic acid to the media used for extraction and electrofocusing, and by maintaining an alkaline pH (pH8.8-9) during extraction and dialysis. Arylsulphatase occurred in two forms with pI values of 4.4 and 6.4-6.7, and beta-glucuronidase in two forms with pI values of 4.4 and 6.1. When [(14)C]lysine and N-acetyl[(3)H]mannosamine were given to rats 1.5 and 1 h before killing, (14)C and (3)H were largely restricted to highly acidic glycoprotein species with pI values of 2.1-5.1. 5. When a lysosomal extract was adjusted to pH5 and incubated at 20 degrees C for 16h and then at 37 degrees C for 1 h before electrofocusing, 32 and 58% of the labelled peptide and N-acetylneuraminic acid was cleaved and the pI values of the labelled glycoproteins were markedly increased. About 80% of the acidic form of arylsulphatase and beta-glucuronidase was recovered with the basic form, and the pI of the basic form of both enzymes rose to 7.0. Similar, though less marked changes, were observed when a lysosomal extract was kept at pH5 for 2h at 4 degrees C before electrofocusing. 6. When an acidic lysosomal fraction (pI4.2-4.6) was incubated at pH5 for 2.5h and refocused, 80% of the arylsulphatase now occurred in two forms with pI values of 5 and 6.4. When a basic lysosomal fraction (pI5.8-6.4) was similarly incubated, the pI of arylsulphatase increased from 6.4 to 7.2. The relative increase in pI of arylsulphatases was accompanied by a proportional loss of N-acetylneuraminic acid from the glycoprotein associated with these forms. 7. These experiments show that lysosomal glycoproteins and two representative hydrolases, when exposed to a mildly acidic pH, readily undergo autolytic degradation and their pI values increase. These observations may have a bearing on the origin of the molecular heterogeneity of the lysosomal enzymes.
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PMID:Autolysis of glycoproteins in rat kidney lysosomes in vitro. Effects on the isoelectric focusing behaviour of glycoproteins, arylsulphatase and beta-glucuronidase. 445 20

The activities of several lysosomal enzymes were assayed in control and in exercise-hypertrophied cardiac muscle of mice (Mus musculus). The repeated running program increased the activity of beta-glucuronidase (16.1%) in mouse cardiac muscle. Decreased activities of beta-N-acetylglucosaminidase (10.8%), acid ribonuclease (10.7%), and arylsulphatase (14.2%) were observed in the hypertrophied myocardium. The activities of acid deoxyribonuclease, cathepsin C, cathepsin D, and p-nitrophenylphosphatase as well as the activities of citrate synthase and cytochrome c oxidase, mitochondrial enzymes, were unaffected in cardiac muscle. We suggest that lysosomal enzyme responses are selective and highly different in physiologically and pathologically induced cardiac hypertrophies.
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PMID:Changes in lysosomal enzyme activities in exercise-induced cardiac hypertrophy of mice. 622 47

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


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