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 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

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

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

The paper presents the results of study of 28 synovial exudations in which the uricase method was used for uric acid determination with simultaneous pyrophosphatase and cathepsin C and D activity determination. The presence of crystals in these exudations was investigated as well. From the study follows that a higher uric acid level and higher pyrophosphatase activity coincide with the finding of urate and pyrophosphate crystals. The reported method of examination applies also to other identifications of microcrystals or crystalline split of urates or calcium pyrophosphate dihydrate in the exudation. The activity of cathepsin D permits to conclude on potential participation of peptides and/or polypeptides in the formation of crystals in the exudation.
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PMID:[Study of crystals in synovial exudations with simultaneous determination of adequate enzymes]. 722 82

Adult rats fed proteins as a meal given during the daytime exhibit alterations of liver protein metabolism characterized by simultaneous stimulations of protein synthesis and degradation, particularly during the hours following protein ingestion. The purpose of the present work was to determine if the stimulation of liver protein breakdown could be related to biophysical alterations of the lysosomal system. There is a growing amount of evidence to suggest that the lysosomal vacuolar system is involved in the physiological regulation of overall proteolytic rate. Rats, trained to eat a protein meal 2 hrs after the onset of light, were killed 6, 9, 18, 21 and 24 hrs after protein intake. Three fractions were isolated from 0.25 M sucrose liver homogenates after differential centrifugation. The mitochondrial-lysosomal fraction was further analyzed by isopycnic centrifugation in sucrose gradients. Three specific lysosomal enzyme activities were assessed: N-acetyl-beta-D glucosaminidase (marker), cathepsin D and cathepsin C (proteolytic enzymes). Total activities remained unchanged at all time-points, but the distributions between the different fractions recovered after differential centrifugation were altered 6 and 9 hrs after protein intake. A significantly higher percentage of N-acetyl-beta-D-glucosaminidase, cathepsin D and cathepsin C activities were recovered in the M + L fraction, suggesting a shift towards lysosomal forms of lighter density. This was confirmed by density gradient analysis. Thus, even in adapted rats, acute administration of protein during the daytime quickly induced biophysical alterations in the lysosomal system. The lysosomal distribution pattern observed at 6 and 9 hrs after protein intake might be due to lysosome enlargement by active autophagy and/or by the sequestration of lighter cellular material.
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PMID:[Rapid modifications of the rat hepatic lysosomal system as a function of the nutritional state]. 734 31

Degradation of metallothionein (MT) from rat liver was examined. Degradation of apo-MT by liver homogenate was greater than that by cytosol. At pH 5.5, degradation by homogenate was more than that at pH 7.2. These findings suggest that proteases that function at acidic pH are probably involved in MT degradation. Because lysosomes are the principal subcellular organelles that contain acid proteases (cathepsins), we compared the degradation of apo-MT by lysosomes and cytosol. Apo-MT was degraded about 400 times faster by lysosomal fraction than by cytosolic fraction. To determine the relative importance of different cathepsins, we used different inhibitors. Leupeptin, which inhibits cathepsins B and L, inhibited the degradation of apo-MT by 80%, implying that cathepsins B and/or L might be very important in the intracellular turnover of MT. Cathepsin D appeared to be the least significant, because apo-MT degradation was reduced by about 20% by inhibiting cathepsin D. When we extended this study with purified cathepsins, we obtained the same answer, i.e., the ability of different cathepsins to degrade apo-MT was in the following order: cathepsin B >> cathepsin C > cathepsin D. While apo-MT was susceptible to degradation, ZnMT and CdMT were highly resistant to degradation. Coincubation of ZnMT or CdMT with either lysosomal extract or purified cathepsins did not result in any appreciable degradation even after 16 hr. However, longer incubations did result in some degradation, especially by purified cathepsin B. Interestingly, CdMT degraded little faster than ZnMT by both lysosomal extract as well as purified cathepsin B.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:In vitro and in vivo studies on the degradation of metallothionein. 784 89

To examine localization of cysteine and aspartic proteinases, and ubiquitin in rat and human urinary bladders, immunocytochemistry was applied to the tissues. In semi-thin sections, immunoreactivity for cathepsins B and D was densely localized throughout epithelial layers of rats and humans, while that for cathepsins H and L was mainly localized in rat superficial and human intermediate cells. Immunoreactivity for cathepsin C was relatively high in rat and human epithelia, especially in humans. Immunoreactivity for ubiquitin was detected in rat and human epithelial cells. By electron microscopy, vesicular or heterogeneously dense lysosomes labeled with immunogold particles indicating cathepsin B were seen in rat and human epithelial cells; particularly, they often appeared near fusiform vesicles in rat superficial cells and in human intermediate and superficial cells. By double immunostaining, lysosomes with or without vesicular structures were co-labeled with immunogold particles showing both cathepsin B and ubiquitin. The results suggest that cathepsins B, C, H, and L, and cathepsin D are involved in the lysosomal system of rat and human bladder epithelia. Moreover, considering that ubiquitin is a cofactor in the soluble ATP-dependent proteolysis, the results may also indicate that epithelial cells actively form autophagolysosomes.
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PMID:Lysosomal cysteine and aspartic proteinases and ubiquitin in rat and human urinary bladder epithelium. 887 57


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