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 activities of acid proteolytic enzymes were assayed in the liver and muscular tissues of mice (Mus musculus) 1, 6 and 24 hr after the administration of a protease inhibitor leupeptin (i.p., 15.5 mg/kg body wt). Leupeptin administration induced a strong inhibition of cathepsin B and a moderate inhibition of cathepsin C and acid autolytic rate in mouse liver 1 hr after injection. Thereafter the inhibition reduced and disappeared during 24 hr. The activity of cathepsin D was increased in liver 6 and 24 hr after injection. The activity of beta-glucuronidase was not affected by the leupeptin treatment. The administration of leupeptin did not affect the rate of acid autolysis and the activities of cathepsin C and D in cardiac and skeletal muscles. A slight increase in cathepsin B activity was observed 1 hr after leupeptin treatment in calf muscles. The cause of both tissue and enzyme specific changes after leupeptin treatment is discussed.
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PMID:Acid proteolytic activities in mouse liver and muscle tissues after treatment with protease inhibitor leupeptin. 614 85

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

To elucidate the metabolic abnormality of musclar dystrophy, 27 kinds of enzyme activity in various organs of control and dystrophic mice were examined. The organs examined included muscle, bone, heart, testis, uterus, spleen, thymus, submaxillary gland, stomach, pancreas, liver, kidney, brain, and lung. The activities of 14 different aminopeptidases, 5 endopeptidases, 4 glycosidases, phosphatase, esterase, and ribonuclease were measured. Most of the enzyme activities were significantly elevated in muscles and bones of dystrophic mice. These organs were similar in their patterns of enzyme abnormality. Among the 14 kinds of aminopeptidase activity studied, the degree of increased activity was greater for the aminopeptidases (AP):Ala-AP, Leu-AP, Met-AP, Phe-AP, Trp-AP, Gly-Pro-Leu-AP. In addition to aminopeptidases, there were significant increases in activities of chymotrypsinlike enzyme, cathepsin C, cathepsin D, several glycosidases and neutral ribonuclease in the muscles of dystrophic mice. Similarly increased enzyme activity was also observed in organs other than muscle and bone. Furthermore, protein content in most organs was higher in dystrophic mice than in those of control mice. These abnormalities were seen in both males and females. The present results suggest that there are extensive abnormalities in the protein metabolism in dystrophic mice. It seems therefore that the therapeutic approach to muscular dystrophy should be studies not only from the well-known abnormality of intramuscular endopeptidases, but from other aspects as well.
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PMID:Various enzyme activities in muscle and other organs of dystrophic mice. 625 14

The activities of four lysosomal and two nonlysosomal hydrolases were studied in skeletal muscle biopsy samples from patients with neuromuscular diseases and from controls. beta-Glucosaminidase activity was increased in polymyositis. beta-Glucuronidase and alkaline protease activities were elevated in muscular dystrophy in adults, whereas cathepsin D activity was increased in amyotrophic lateral sclerosis. There were significant correlations between the activities of lysosomal and nonlysosomal hydrolases. The activity of beta-glucuronidase, beta-glucosaminidase, alkaline protease, and dipeptidyl aminopeptidase IV showed a positive correlation with the severity of muscular atrophy. The activities of these hydrolases and the activity of dipeptidyl aminopeptidase I correlated positively with the activities of muscular galactosylhydroxylysyl glucosyltransferase and with the serum concentration of type III procollagen aminoterminal propeptide. The results suggest that in neuromuscular diseases the lysosomal and nonlysosomal pathways for muscle degradation are affected concomitantly with collagen biosynthesis.
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PMID:Lysosomal and nonlysosomal hydrolases of skeletal muscle in neuromuscular diseases. 635 16

Hypertrophy was induced in the patagialis (PAT) muscle of 6-week-old normal and dystrophic chicks by passive stretch for 1 week. Stretch was then removed and muscle weights and activities of the proteolytic enzymes cathepsin C, cathepsin D, and leucine aminopeptidase (LAPase) were measured after 3, 5, 7, 10, and 14 days. In both genotypes, weights of stretch-released muscles dropped progressively for 7 days relative to control muscles, after which they were not significantly different. At the time of stretch release, proteolytic enzyme activities were approximately twice as high in stretched normal muscles as in normal control muscles. In dystrophic chicks there was no difference in activities between stretched and control muscles. However, the activities of the enzymes in dystrophic muscles were already about 4 times higher than in normal control muscles. After stretch release, the enzyme activities in normal muscle progressively fell for 10 days, after which they were not different from normal control muscles. In dystrophic muscles the enzyme activities remained elevated and were not different from dystrophic control muscle activities at any time. We conclude that degradative enzyme activities in normal muscle closely parallel changes in muscle weight, whereas in dystrophic muscle proteolytic enzymes remain elevated and constant whether the muscle is gaining or losing weight.
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PMID:The effect of stretch removal on muscle weight and proteolytic enzyme activity in normal and dystrophic chicken muscles. 654 1

Changes of protease activities that follow passive stretch, denervation, and denervation plus stretch were followed in the patagialis muscle of normal and dystrophic chicks between 6 and 7 weeks of age. The baseline activities of cathepsin C, cathepsin D, and leucine aminopeptidase in dystrophic muscle were 2 to 3.5 times higher than in normal muscle. Passive stretch and denervation induced increases in protease activities by 40 to 120% in normal muscle, whereas the same treatments did not significantly affect the activities of the enzymes in dystrophic muscle. We conclude that the level of protease activity in dystrophic chicken muscle at 6 weeks of age had already attained a maximum limit and could not be increased even by denervation. In spite of protease activities, which were not different from control dystrophic muscle, denervated dystrophic muscles lost muscle weight rapidly whether they were stretched or not. They weighed 60% less than the innervated control muscle after 7 days. Inherently high protease activities in dystrophic muscle do not vary at this age regardless of whether or not the muscle is gaining or losing weight.
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PMID:Effects of stretch and denervation on protease activities of normal and dystrophic chicken muscle. 671 51

Three experiments were designed to study the lysosomal changes associated with the development and maintenance of the endurance training induced resistance against exercise injuries in mouse skeletal muscles. The activities of arylsulphatase, cathepsin C, cathepsin D, and beta-glucuronidase were assayed from the red part of mouse quadriceps femoris muscle 4 days after prolonged strenuous running of 4-9 h duration. Exercise injuries were characterized by necrotic fibers and focal inflammation. Strenuous running of untrained mice induced necrotic lesions and a 4-5 fold increase in the activities of lysosomal enzymes. This lysosomal response was considerably reduced already by daily training bouts on the 3 days preceding the strenuous exertion. Simultaneously exercise injuries were markedly reduced. Extending the endurance training program increased the running ability of mice and further reduced the necrotic lesions and lysosomal changes induced by the strenuous exercise. The detraining of 1 week after the termination of regular endurance training considerably increased the degree of exercise induced lysosomal response. The detraining of longer durations further increased the lysosomal response and no effect of prior endurance training existed after 1 month detraining. Our observations suggest that the severity of exercise injuries is related to the strength of the exercise stimulus and the level of preceding physical activity and can be characterized by the lysosomal changes.
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PMID:Lysosomal changes related to exercise injuries and training-induced protection in mouse skeletal muscle. 672 Mar 24

Male NMRI-mice, aged 3, 6, 9, and 12 months, were made to run for a period of 4 4 at a speed of 13.5 m/min on a motor-driven treadmill, 5 days after exertion, selected enzymatic estimates of acid and alkaline proteolytic as well as energy metabolic capacities were analyzed from the cardiac muscle and from the red and white parts of m. quadriceps femoris (MQF). The activities of alkaline and myofibrillar proteases increased most considerably in skeletal muscles with age. Cathepsin D and beta-glucuronidase activities were less affected in both muscles. Prolonged running increased the activities of cathepsin D, dipeptidyl aminopeptidase I and beta-glucuronidase in the white and, especially in the red part of MQF. This stimulation of acid hydrolytic capacity was more prominent at the ages of 3 and 6 months than in the older animals. The estimates of alkaline proteolytic or energy metabolic capacities were not affected by prolonged running. In cardiac muscle, no significant changes were recorded in acid hydrolytic or energy metabolic capacity. Histological observation showed no necrosis or other pathological phenomena in the proximal part of m. rectus femoris after excretion. We suggest that the increased acid proteolytic capacity is involved in subcellular regenerative processes of skeletal muscle fibres. The smaller lysosomal response of older mice may indicate a reduced potential capacity for cellular repair.
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PMID:Effects of age and prolonged running on proteolytic capacity in mouse cardiac and skeletal muscles. 702 79

The content of 5 lysosomal hydrolases was examined in the rat liver and blood serum after compression of hind limb soft tissues in the presence of a long-term intake of excess doses of pyridoxine, riboflavin and glutamic acid. It was shown that the 14-day application of the drug complexes dramatically increased the overall content of cathepsin C, arylsulfatases A and B, beta-glucuronidase and p-acetyl-beta-D-galactosaminidase and reduced the overall content of cathepsin D in the rat liver. The non-sedimented content of the enzymes did not practically differ from the control magnitudes. In the blood serum, the content of cathepsin C and B1 approximated that seen in the control, while that of arylsulfatases A and B and p-acetyl-beta-D-galactosaminidase decreased, whereas the beta-glucuronidase content was 75% higher as compared to the basic characteristics. In the presence of administering the drug complexes, severe mechanical injury entailed the lowering of the content of the majority of rat liver lysosomal hydrolases. Besides, one could observe an essential fall of the non-sedimented content of cathepsin C and arylsulfatases A and B. The blood serum demonstrated an appreciable decrease in the content of cathepsins C and B1, p-acetyl-beta-D-galactosaminidase and arylsulfatases A and B. Thus, the fall of the non-sedimented content and diminished release of lysosomal hydrolases into the systemic circulation attest to the preservation of the structural and functional integrity of the liver cell lysosomal system during severe mechanical injury in the presence of combined excess intake of pyridoxine, riboflavin and glutamic acid.
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PMID:[Effect of pyridoxine, riboflavin and glutamic acid on lysosomal hydrolase activity in the liver and serum of rats during traumatic stress]. 715 Jul 36

1. Growing rats were fed either ad lib. or with six (equal) meals offered every 4 h (from 10.00 hours). Rats of each group were killed at intervals of 4 h beginning at 11.00 hours. Activities of cathepsin A (carboxypeptidase A; EC 3.4.12.2), C (dipeptidyl peptidase; EC 3.4.14.1) and D (endopeptidase D EC 3.4.23.5) were measured in liver and muscle homogenates and free amino acids in blood were determined. 2. In the rats fed ad lib. activities of carboxypeptidase A and endopeptidase D in liver and muscle showed significant variation, with maximum activity in the light period. In general, meal-feeding only caused minor differences in cathepsin activities; although significant differences occurred for carboxypeptidase A. For the later enzyme a peak in activity occurred in the dark as well as in the light period. 3. Irrespective of the feeding schedule, the lower concentration of free essential amino acids of blood occurred generally during the night period. With the controlled-feeding schedule there is an increase of essential amino acids and a slight decrease of non-essentail amino acids of blood.
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PMID:Variations through the day of hepatic and muscular cathepsin A (carboxypeptidase A; EC 3.4.12.2), C (dipeptidyl peptidase; EC 3.4.14.1) and D (endopeptidase D; EC 3.4.23.5) activities and free amino acids of blood in rats: influence of feeding schedule. 719 24


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