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 specific activity of three lysosomal proteinases (cathepsins B1, D, and L) as well as acid phosphatase and beta-galactosidase has been determined in the liver of both 7-10 day-old and young adult rats. Cathepsin B1 in suckling rats is markedly lower than in adults, while cathepsin D is only moderately lower and cathepsin L does not significantly differ. The activity of acid phosphatase is similar in the two groups of animals whereas that of beta-galactosidase in suckling rats is approx. twice as high as in adults. The activity of lysosomal hydrolases thus appears to be regulated individually during the development. Moreover it is suggested that the low activity of cathepsin B1 may be related to the low rate of cell protein catabolism characteristic of the developing liver (Conde and Scornik, 1977).
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PMID:Lysosomal hydrolase activities in the developing rat liver. 677 67

The weight of the liver and its DNA content definitely increase in rats transplanted with the ascites hepatoma AH-130 (Yoshida). The specific activity of cathepsin B1 decreases progressively in the liver during the first week after transplantation reaching one third of the initial levels, whereas that of cathepsin D shows the opposite behaviour increasing to levels 40% higher than in controls. The activity of the two proteinases in the blood plasma varies in a similar way, though the modifications are even more pronounced than in the liver. The relevance of the changes in tissue proteinase activities to the liver growth in tumour-bearing animals is discussed.
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PMID:Effect of a fast-growing ascites hepatoma (Yoshida AH-130) on proteinase activities in the rat liver. 700 67

The purpose of this study was to determine whether or not alternations in tumor growth induced by changes in thyroid status were mediated through changes in key enzymes, whose activity is known to be influenced by thyroid hormones. The activities of three lysosomal enzymes (cathepsin B1, cathepsin D, and acid phosphatase) and thymidylate synthetase were measured in implanted mammary tumors as well as in the livers of host animals that were either euthyroid, hypothyroid, or hyperthyroid. Hypothyroidism produced no significant change in enzyme activity in the tumors. Hyperthyroidism, on the other hand, did cause a significant increase in the activity of all lysosomal enzymes in the tumors, but did not affect thymidylate synthetase levels. In the livers of the host animals, hypothyroidism produced a significant decrease in cathepsin B1 and a significant increase in acid phosphatase but did not change cathepsin D or thymidylate synthetase levels. Hyperthyroidism produced a significant increase in all enzymes measured in the livers of the host animals. The significant decrease in tumor weight with hypothyroidism did not correlate with the insignificant changes in the enzymes tested. Similarly, there was no correlation between the significant increase in the enzymes levels found with hyperthyroidism and the insignificant change in tumor weight.
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PMID:Effect of altered thyroid status on lysosomal enzymes and thymidylate synthetase activity in tumors and livers of host animals. 707 81

Thiol-activated cathepsin was isolated from bovine cerebral hemispheres and cerebellum. The enzyme from the hemispheres was purified by the affinity sorbent chromatography method with the sepharose-4B-immobilized protein substrate, azocasein, and with subsequent separation of nonspecifically sorbed protein by column gel-chromatography on Sephadex G-100. The cathepsin pH-optimum was 6.0. The coincidence in cellular (neuron and glia enriched fractions) and subcellular distribution of cathepsin D and thiol-activated cathepsin activities shows the probable lysosomal origin of the latter. The data obtained about the influence of the various proteolytic enzyme inhibitors and activators on the thiol-activated cathepsin activity show a definite similarity of the enzyme with the thiol proteinases of the rat liver lysosomes, cathepsin B1 and L.
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PMID:[Purification and properties of thiol-activated cathepsin from bovine cerebrum and cerebellum]. 710 70

Several gold salts were compared in kaolin-induced rat paw oedema, u.v. erythema in guinea pigs, delayed type hypersensitivity and humoral immunity in mice, and adjuvant-induced arthritis in the rat. In the latter the additional parameters of serum gold and copper levels and lysosomal enzyme activity were determined. In addition, the in vitro inhibition of several lysosomal enzymes derived from mouse macrophages was studied. The gold compounds examined were aurothiomalate, aurothioglucose, triethylphosphine gold chloride (SK & F 36914) and its glucopyranoside derivative (SK & F D-39162), triphenylphosphine gold chloride and sodium gold chloride dihydrate. SK & F 36914 and SK & F D-39162 has significant activity after oral dosage upon paw kaolin and u.v. erythema in rats and guinea pigs, respectively. Gastric swelling also occurred. In Wistar rats, adjuvant arthritis was little affected by the gold salts but in the Lewis rats there was suppression. In both strains there was less elevation in serum copper levels with treatment by SK & F 36914 and SK & F D-39162, but not by aurothiomalate. None of the compounds had any measurable effect on delayed hypersensitivity or humoral antibody levels in mice. The in vitro activities of cathepsin B1 and cathepsin D were inhibited by all the gold compounds. Reactivity of gold compounds with glutathione and cysteine in vitro was dependent on compound solubility and the nature of the gold ligand. Considerable differences exist between the profiles of activity for the different gold salts evaluated. These observations indicate that some gold salts do possess anti-inflammatory activity with a potency similar to that of indomethacin.
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PMID:Action of gold salts in some inflammatory and immunological models. 738 10

The early endosome is the first vacuolar compartment along the endocytic pathway. It is the site of internalization and initial processing of amyloid precursor protein (APP) and apolipoprotein E (ApoE), two proteins of etiological importance in Alzheimer's disease, and a putative site of beta-amyloid peptide (Abeta) formation. Here, we identify early endosomes in human pyramidal neurons, using specific compartmental markers and morphometry, and show that in Alzheimer's disease individual endosomes display up to 32-fold larger volumes than the normal average. Endosomal enlargement contributed to an average 2.5-fold larger total endosomal volume per neuron, implying a marked increase in endocytic activity. Endosomal alterations were evident in most pyramidal neurons in Alzheimer brain, detectable at early stages of the disease but absent in several other neurodegenerative disorders examined. In addition, mature and proenzyme forms of the proteases cathepsin B and cathepsin D, a candidate APP secretase, were identified in most early endosomes in Alzheimer brains but were detectable in only a minor proportion of endosomes in normal brain. Expression of the cation-dependent 46 kDa mannose 6-phosphate receptor was elevated in pyramidal neurons of Alzheimer brains, which could be a possible basis for the altered cathepsin trafficking pattern. Enhanced endocytic activity, coupled with increased trafficking to endosomes of proteases, which may have the ability under pathological conditions to generate Abeta, constitutes a potential mechanism by which beta-amyloidogenesis may become accelerated in sporadic AD and also be subject to influences by ApoE.
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PMID:Increased neuronal endocytosis and protease delivery to early endosomes in sporadic Alzheimer's disease: neuropathologic evidence for a mechanism of increased beta-amyloidogenesis. 923 26

The aspartic protease cathepsin D (Clan AA, Family A1) is expressed in the schistosome gut where it plays an apical role in the digestion of hemoglobin released from ingested erythrocytes. In this report, RNA interference approaches were employed to investigate the effects of knockdown of schistosome cathepsin D. Cultured schistosomules of Schistosoma mansoni were exposed by square wave electroporation to double stranded RNA (dsRNA) specific for cDNA encoding S. mansoni cathepsin D. RNAi-mediated reductions in transcript levels led to phenotypic changes including significant growth retardation in vitro and suppression of aspartic protease enzyme activity. In addition, black-pigmented heme, the end point by-product of normal hemoglobin proteolysis that accumulates in the schistosome gut, was not apparent within the guts of the treated schistosomules. Their guts appeared to be red in color, rather than black, apparently indicating the presence of intact rather than digested host hemoglobin. These phenotypic effects were apparent when either of two forms of dsRNA, a long form spanning the entire target transcript or a short form specific for the 3'-region was employed. Off-target effects were not apparent in transcript levels of the gut-localized cysteine protease cathepsin B1. Finally, cathepsin D may be an essential enzyme in the mammal-parasitic stages of schistosomes because schistosomules treated with dsRNA did not survive to maturity after transfer into Balb/c mice. These and earlier findings suggest that, given its essential function in parasite nutrition, schistosome cathepsin D could be developed as a target for novel anti-schistosomal interventions.
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PMID:RNA interference of Schistosoma mansoni cathepsin D, the apical enzyme of the hemoglobin proteolysis cascade. 1806 80


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