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 levels of six lysosomal enzymes (acid phosphatase, beta-acetylglucosaminidase, cathepsin D, beta-galactosidase, arylsulfatase A, and beta-glucuronidase) and four neutral and alkaline hydrolases (esterase, inorganic phyrophosphatase, alkaline phosphatase, and 5'-nucleotidase) were measured in osteoarthritic, rheumatoid and control synovia. All enzyme levels in diseased synovium except esterase values in osteoarthritis were significantly elevated compared with controls. The mean values of the group of acid hydrolases and the group of neutral and alkaline hydrolases in osteoarthritic synovia were 1.9- and 2.0-fold greater than those of control specimens. In rheumatoid synovia, the values were 4.2- and 4.5 fold greater than control for the same enzymes. Levels in rheumatoid synovia were significantly higher than those in osteoarthritic synovia with the exception of 5'-nucleotidase. Only a limited correlation between the extents of inflammation present in the synovia and the levels of a lysosomal marker enzyme (cathepsin D) was observed. These results demonstrate that whatever the mechanism, increased levels of acid hydrolases as well as certain neutral and alkaline hydrolases are present in osteoarthritic and rheumatoid synovia, and these enzymes are probably contained in the synovial lining cells.
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PMID:Acid, neutral, and alkaline hydrolases in arthritic synovium. 0 9

Six patients with liver metastases from carcinoid or colon carcinoma underwent hepatic derterialization. This operation, known to cause both tumor necrosis and liver cell damage, caused considerable increases of several lysosomal acid hydrolases in the circulation. Thus, beta-glucosidase showed a small temporary increase during the operation, followed by a slower but higher reaction reaching a maximum 12 to 36 hours postoperatively. Similar reactions were noted for beta-glucuronidase, acid phosphatase, beta-galactosidase, arylsuphatase A, and N-acetyl-beta-glucosaminidase while no reactions were found for cathepsin D. Very high enzyme levels occurred in a patient dying from bleeding complications in the postoperative period.
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PMID:Plasma activities of lysosomal enzymes after hepatic dearterialization in man. 0 1

1. The distribution of acid protease activity in various tissues of Japanese monkey (Macaca fuscata fuscata) was investigated with hemoglobin as a substrate at pH 3.0. The activity per protein weight in crude extracts was highest in spleen and lung, and decreased in the order: spleen, lung greater than kidney, testis greater than brain greater than liver, placenta greater than thyroid gland, muscle. The activity in crude muscle extract was about one-tenth those of spleen and lung. The activity per wet tissue weight was in roughly the same order except for a lower activity per wet weight of brain. 2. Upon chromatography of each crude extract on a Sephadex G-100 column, one major activity peak was eluted at a position corresponding to a molecular weight of about 41,000. This enzyme activity is attributed to cathepsin D [EC 3.4.23.5]. In addition, a minor activity peak was eluted in the case of spleen, lung and kidney at the break-through position, corresponding to a molecular weight of more than 100,000. This activity peak is presumably due to cathepsin E. These acid protease activities were, in most cases, strongly inhibited by pepstatin, an acid protease-specific peptide inhibitor. 3. The distribution of acid protease activity was investigated in the brain of crab-eating monkey (Macaca fascicularis). The activity was fairly evenly distributed among several regions of the brain, and its distribution was similar to those of other acid hydrolases, especially N-acetyl-beta-D-glucosaminidase [EC 3.2.1.30] and acid phosphatase [EC 3.1.3.2], which are marker enzymes of lysosomes.
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PMID:The structure and function of acid proteases. VII. Distribution and some properties of acid proteases in monkey tissues. 1 47

The specific enzymic properties, membrane or particle binding capacities, and the total activities of certain acid hydrolases, including cathepsin D, acid phosphatase, arylsulfatase, and five acid glycosidases have been compared in normal canine antral and fundic mucosae and in liver. The two major regions of the gastric mucosa, whose cell populations are comparable in type but have very distinct functions, also differ in many properties of their lysosomal enzymes. These differences necessitate several major modification in their method of assay. Using optimal conditions, the activities of most of these enzymes were found to differ: levels in the antrum, in spite of its high water and mucin-glycoprotein content, were significantly greater, suggesting that the high lysosomal hydrolytic activity may be associated with the rapid autophagic processes of normal turnover of its surface epithelial and mucous neck cells. Lysosomal membrane stability or latency is also greater in the antrum; this may account, in part at least, for antral resistance to erosions brought about by stress.
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PMID:Acid hydrolases. Assay of activity and latency in the varied mixed cell populations of canine gastric mucosa. 1 64

The enzymatic activity of five acid hydrolases: acid phosphatase, arylsulfatase A, deoxyribonuclease, beta-glucuronidase, and cathepsin D, was assayed in fetal (fifteenth and eighteenth days of pregnancy) and neonatal (Days 0, 5, 10, and 15 post-partum) mouse liver. With the exception of cathepsin D, the activity increased around birth to levels varying according to the enzyme. Histochemical observations of other authors appear to justify, at least in part, the present results, which indicate that late days of fetal development and early neonatal life may constitute a transitional stage to full lysosomal enzyme functionality of the adult organ. The livers of the mothers were also assayed for the same enzymes. Each activity showed a peculiar pattern which was, in turn, different from that found in the liver of the litter for the same enzyme, probably as a cause of the metabolic requirement of the gland. The hypothesis that the lysosomes are heterogeneous in their enzyme composition is suggested by the variety of enzymatic patterns found in the liver of the litters and their mothers.
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PMID:The development of lysosomal apparatus. I. Lysosomal enzyme activities in the liver of mice at perinatal stages and those of their mothers. 2 3

Cryptorchidism of the mature rat testis led to degeneration of the seminiferous tubules and changes in enzyme patterns and activities. Spermatogenic stages 1-4, containing pachytene primary spermatocytes in late meiotic prophase, and stage 5, containing recently formed round spermatids, were damaged by 48 h. Within 96 h stages showed a loss of germinal cells into the lumen and this was almost complete by 192 h. Acid phosphatase showed increased histochemical activity in the basal area of the seminiferous tubule up to 96 h of cryptorchidism, and at 192 h much of the activity was located in large lipidcontaining bodies within the remaining seminiferous epithelium. Total and free biochemical acid phosphatase decreased during cryptorchidism in parallel with cell loss; there were no significant changes in total cathepsin D activity but free enzyme activity was increased throughout the experimental period indicating increased lability of lysosomes in the Sertoli cell. Lactate dehydrogenase activity was mainly tubular but succinate dehydrogenase also showed interstitial activity. Lipoamide dehydrogenase (NADH) was found mainly in the interstitium. During cryptorchidism both lactate and succinate dehydrogenase activity decreased in the tubules parallel to the loss of germinal cells, whereas lipoamide dehydrogenase (NADH) activity increased in both interstitial and tubular areas. It is suggested that the initial lesion in the seminiferous epithelium, produced by cryptorchidism is in the Sertoli cell and that germ cell damage may result from reduced function of the Sertoli cell.
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PMID:The effect of cryptorchidism on the quantitative histology, histochemistry and hydrolytic enzyme activity of the rat testis. 2 15

These experiments test whether creatine, a product of muscular contraction, stimulates myofibrillar protein synthesis. It was found that skeletal muscle cells formed both in vitro and in vivo and cardiac muscle cells formed in vivo synthesize myofibrillar proteins faster when supplied creatine in vitro. The rates of synthesis and/or accumulation of three myofibrillar proteins-myosin heavy chain actin, and creatine kinase-were stimulated by creatine. In contrast, the rates of synthesis of total protein and of deoxyribonucleic acid (DNA) and the activities of several nonmyofibrillar enzymes were not altered by creatine. These include lactic dehydrogenase, cathepsin D, acid phosphatase, and beta-acetylglucosaminidase. It is concluded that creatine selectively stimulated the rate of synthesis of contractile proteins in skeletal and cardiac muscle in vitro and may play a role in muscle hypertrophy.
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PMID:Creatine: a possible stimulus skeletal cardiac muscle hypertrophy. 12 40

Canine liver lysosomes were purified by sucrose discontinuous density gradient centrifugation and then ruptured by sonication to obtain the soluble fraction. This soluble lysosomal fraction, which contained a 25-fold increase in acid phosphatase activity per mg of total protein when compared with the original homogenate, was incubated with a subfraction (1.110 less than d less than 1.210 g/cm3, HDL3) of canine high density lipoproteins (HDL) at pH 3.8. HDL3 proteolysis by lysosomal proteases, measured as the release of peptides and amino acids by the ninhydrin reaction, followed hyperbolic curves with straight lines (r = 0.99) obtained on Lineweaver-Burk plots. Km calculated from the Lineweaver-Burk plot was 635 mug of HDL3 protein per 0.5 ml of incubation mixture. Optimum HDL3 proteolysis was observed from pH 3.8 to 4.5. Incubation with the other subcellular organelle fractions did not result in HDL3 proteolysis. To evaluate the effects of enzyme inhibitors, iodoacetate, p-chloromercuribenzoate (both specific for the endopeptidase, cathepsin B (EC 3.4.22.1)) and pepstatin (specific for the endopeptidase, cathepsin D (EC 3.4.23.5) were tested. Iodoacetate and p-chloromercuribenzoate inhibited HDL3 proteolysis 100% and bovine serum albumin proteolysis 65%. Pepstatin inhibited HDL3 proteolysis 45% and bovine serum albumin proteolysis 70%. The in vitro data presented support the hypothesis that hepatic lysosomes play an important role in HDL3 catabolism in the dog. Furthermore, results obtained from enzyme inhibition studies suggest that a specific lysosomal endopeptidase, cathepsin B, may play the key role in HDL3 proteolysis.
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PMID:Proteolysis of canine apolipoprotein by acid proteases in canine liver lysosomes. 17 45

Polymorphonuclear leukocytes of rabbits and chickens after homogenization in 0.34 M saccharose or after multiple freezing and thawing were subjected to differential centrifugation at 150, 800, 10 000 and 50 000 X g. In the fractions obtained in this manner, total bactericidal activity as well as the activity of myeloperoxidase (E.C. 1. 11. 1. 7), catalase (E.C. 1.11.1.6), lysozyme (E.C. 3.2.1.17), cathepsin D (E.C. 3.4.4.23) and E, beta-D-glucuronidase (E.C. 3.2.1.31) and acid phosphatase (E.C. 3.1.3.2) were determined. Antibacterial activity was found in all fractions from rabbit leukocytes, but only in the first fraction from chick leukocytes. The fractions from rabbit leukocytes contained all enzymes under study while in the fractions from chicken leukocytes the presence of myeloperoxidase, catalase or cathepsin E could not be demonstrated. The highest bactericidal activity was found in the second obtained from the homogenate or rabbit leukocytes. The highest specific activity of myeloperoxidase and homogenate of rabbit leukocytes. The highest specific activity of myeloperoxidase and the lowest activity of cathepsin D were also demonstrated in this fraction. The addition of pepstatin to rabbit leukocytes before their disintegration resulted in the inhibition of the activity of cathepsin D and E and in an increase in the specific activity of myeloperoxidase as well as in total bactericidal activity in the individual fractions. These results testify that microbicidal mechanisms of phagocytes from individual species may differ and when the structure of lysosomes is damaged, the liberated hydrolytic enzymes may gradually inactivate antibacterial substances.
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PMID:Localization of antibacterial activity and hydrolytic enzymes in subcellular fractions of rabbit and chicken polymorphonuclear leukocytes. 17 6

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


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