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)

Cardiac hypertrophy was produced in rats by constriction of the ascending aorta. Removal of the constricting band 10 days after operation resulted in rapid decline in left ventricular (LV) weight and total ventricular RNA. Activities of acid RNase and beta-glucuronidase were elevated 3 days after aortic constriction. Activities of cathepsin D and alkaline RNase were unchanges. Activities of cathepsin D and acid RNase were unchanged 1 and 3 days after removal of constricting band. Ca2+-activated, neutral protease (CAF) isolated from postmitochondrial muscle supernatant was partially purified and characterized. CAF specifically degrades alpha-actinin when incubated with isolated myofibriles in the presence of Ca2+.
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PMID:Lysosomal and neutral hydrolase activity during the regression of cardiac hypertrophy. 0 53

Exogenous hen lysozyme or endogenous rat lysozyme labeled with 131I was intravenously injected to rats with the same dosage, respectively, and the uptake and degradation of injected 131I-labeled rat lysozyme in liver and kidney were studied in comparison with those of 131I-labeled hen lysozyme. 1. Although the serum levels of both enzymes injected were almost indentical during the first 6 h, the liver uptake of 131I-labeled hen lysozyme was 2.2-fold more than that of 131I-labeled rat lysozyme at the peak time of 5 min after injection. The uptake and clearance of 131I-labeled rat lysozyme in the kidney were exclusively slow as compared with those of 131I-labeled hen lysozyme. 2. The intracellular distribution in the liver and kidney were examined by the differential centrifugation after injection of each lysozyme. The protein-bound radioactivity of each subcellular fraction was found to be the highest in the 12 000 X g (10 min) fraction in the liver and the 19 600 X g (20 min) fraction in the kidney. The relative specific activity of 12 000 X g fraction of the liver after injection increased with the time lapse. On the other hand, the relative specific activity of 105 000 X g (1 h) fraction of the liver attained a maximum within 5 min after injection and thereafter decreased. It was assumed that the mechanism of the uptake of injected 131I-labeled rat lysozyme in the liver and kidney was similar to that of 131I-labeled hen lysozyme. 3. The degradation of exogenous or endogenous lysozyme in subcellular particles was examined. From the effect of pH, activator and inhibitor on the degradation, the proteolytic enzyme to degrade the injected 131I-labeled hen lysozyme was indicated to be mainly cathepsin BL, with the optimal pH of about 5.0, and the injected 131I-labeled rate lysozyme was mainly degraded by cathepsin D, with the optimal pH of about 3.5 The in vitro degradation of exogenous and endogenous lysozymes showed a tendency similar to the in vivo clearance from the liver and kidney.
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PMID:Studies on biotransformation of lysozyme. III. Comparative studies on biotransformation of exogenous and endogenous lysozyme in rats. 1 53

The distribution and biochemical properties of the renin activity present in the dog brain were compared with those of the lysosomal enzyme cathepsin D. Renin and cathepsin activity were present in all brain regions studied, in association with high angiotensinase activity. Brain renin activity was partially purified by ammonium sulfate fractionation and Sephadex gel filtration, resulting in the removal of angiotensinase activity. The specific brain renin activity increased approximately one hundred times during this procedure; cathepsin D activity accompanied the brain renin activity throughout the purification and showed a similar increase in specific activity. The renin and cathepsin activity in the partially purified preparation behaved identically during isoelectric focusing. The partially purified renin and cathepsin activity exhibited saturation kinetics with their respective substrates and were without activity above pH 6.0. Both enzyme activities were irreversibly inhibited by the pepsin inhibitor pepstatin, in nanomolar concentrations. These data, in conjunction with the literature concerning brain cathepsin, suggest that the renin activity in brain is due to cathepsin D, and that this renin activity exhibited by cathepsin D may be of limited significance under physiological conditions.
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PMID:Renin activity in dog brain: enzymological similarity to cathepsin D. 18 Dec 41

An insoluble preparation of rat liver cathepsin D was obtained by coupling the enzyme to Enzacryl Polyacetal (EPA-cathepsin) and to CNBr-activated Sepharose 4B. EPA-cathepsin was active toward the synthetic hexapeptides (Gly-Phe-Leu)2 and did not split hemoglobin. The optimum pH of splitting was displaced upward by 1.5 units to pH 5.0. The enzyme exhibited maximum activity at 60 degrees C. No appreciable loss of activity was seen on storage of the enzyme for 4 months or after repeated use of the preparations. Coupling of rat liver cathepsin D to activated Sepharose gave preparations active towards both protein and synthetic substrates. The preparations were totally inactive in acid media and exhibited maximum activity at pH 7.0, that is, under physiological conditions. Optimum temperature was 65 degrees. The specific activity of the preparations (pH 7.0, 65 degrees) was 60-110 percent that of the free enzyme in acid media. Proteolytic activity of the Sepharose-coupled cathepsin D was not inhibited by pepstatin, whereas that of the free enzyme was fully inhibited by this reagent. A sarcoma cathepsin, similar in some of its properties to the rat liver enzyme, was also coupled to CNBr-activated Sepharose 4B. The preparation split protein substrates at pH 7.0 and possessed enhanced thermostability. The enzymes fixed on Sepharose showed increased stability.
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PMID:Some properties of cathepsins chemically fixed to carriers. 23 96

In vitro degradation of insoluble vitreous collagen by the action of collagenolytic cathepsin was studied biochemically. Among bovine ocular tissues, the uvea and the retina showed relatively high collagenolytic activity. The ciliary body revealed the highest specific activities of both cathepsin B and collagenolytic cathepsin. Leupeptin and p-chloromercuribenzoate inhibited both cathepsin B and collagenolytic cathepsin in the ciliary body lysosomes. Pepstatin inhibited cathepsin D, but did not affect cathepsin B and collagenolytic cathepsin. It is suggested that distribution and properties of collagenolytic cathepsin are similar to those of cathepsin B in the bovine eye.
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PMID:The distribution and some properties of collagenolytic cathepsin in the bovine eye. 30 80

Cathepsin D was originally known simply as 'cathepsin' and was first purified in the late 1930s. Nowadays the enzyme is purified by conventional column chromatography, and by isoelectric focusing (which resolves isoforms), but affinity chromatography with pepstatin--Sepharose is also important. Cathepsin D is a glycoprotein of about 42,000 molecular weight; sometimes it comprises a single polypeptide chain but often this is found to have been 'nicked' about two-thirds of the way from one end. Cathepsin D is an 'aspartic proteinase' and may be one of the more primitive members of the family. The activity of cathepsin D is expressed exclusively at acidic pH values and the specificity shows a strong preference for cleavage near hydrophobic amino acids. Specific inhibition of cathepsin D with antibodies and pepstatin has provided strong evidence that the enzyme plays a part in intralysosomal proteolysis but there is as yet little evidence for extracellular activity.
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PMID:Cathepsin D: the lysosomal aspartic proteinase. 39 96

A content of neutral sugars and N-acetyl-glucosamine in homogeneous cathepsin D preparations from a variety of vertebrate organs was determined. A more detailed study of the carbohydrate component was carried out with chicken liver cathepsin D preparation. It was shown that carbohydrates constitute 20% of the molecule of this cathepsin and contain glucosamine (11.6%) and mannose (10%). Removal of the major portion of the carbohydrates by treatment with mixture of glycosidases did not lead to any significant decrease of biological activity. This finding suggests that the carbohydrate component is not essential for the biological activity of the enzyme. Analysis of distribution of carbohydrates in the peptides of the trypsin hydrolyzate of cathepsin D allows conclusion that the enzyme molecule has several carbohydrate chains attached to different sites of the molecule.
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PMID:[Study of the carbohydrate component of cathepsin D]. 59 21

The action of uterine cathepsin D on the insulin A-chain (S-sulfo) and porcine glucagon was compared with the action of bovine dental pulp cathepsin on the same substrates. Differences observed with respect to molecular and catalytic properties suggest that different gene products (coding for the same function) are used during cell differentiation.
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PMID:Specificity and some physical properties of cathepsin D from bovine uterus and dental pulp. 105 48

Cathepsin D expression was assessed by immunohistochemistry in 59 node-negative and 77 node-positive infiltrative ductal not otherwise specified (NOS) breast carcinomas and compared with overall survival at 90 months. Cancer cells in 60% (81/136) of the tumors expressed cathepsin D. In the stroma of 33% (18 of 55) cathepsin D negative tumors, numerous strongly cathepsin D positive, benign macrophage-like cells were found. Multivariate analysis showed no significant correlation of cathepsin D expression and overall survival for all patients for node-negative and node-positive patients and for patients with vimentin-positive and -negative tumors. However, in node-negative but not in node-positive patients, a trend for better survival for patients with cathepsin-positive vimentin-negative tumors and worse survival for those with cathepsin-positive vimentin-positive tumors was noted. Due to the low number of patients in these subgroups, neither trend reached significance. Cathepsin D expression was independent of patient age, size, and histologic grade of tumor, and vimentin expression. However, in the node-positive group, negative correlation of cathepsin D and vimentin expression was found. We suggest that prognostic significance of cathepsin D in infiltrative ductal NOS breast carcinomas may be associated with the pathway of its synthesis rather than with its mere presence in tumor cells.
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PMID:Cathepsin D in invasive ductal NOS breast carcinoma as defined by immunohistochemistry. No correlation with survival at 5 years. 133 83

Upon receptor-mediated endocytosis of very-low-density lipoprotein (VLDL) and vitellogenin into growing chicken oocytes, the protein moieties of these lipoproteins are proteolytically cleaved. Unlike the complete lysosomal degradation in somatic cells, enzymatic ligand breakdown in oocytes generates a characteristic set of polypeptides, which enter yolk storage compartments for subsequent utilization by the embryo. Here, we demonstrate directly that the catalyst for the intraoocytic processing of both apolipoprotein B and vitellogenin is cathepsin D. The enzyme was purified from oocytic yolk, preovulatory follicle homogenates, and liver by affinity chromatography. When plasma VLDL and vitellogenin were incubated with the purified enzyme, fragments indistinguishable from those found in yolk were generated from both precursors under identical, mildly acidic conditions. Amino-terminal sequencing of the pure enzyme demonstrated 88% identity with mammalian cathepsin Ds over 34 residues. On the basis of this information, a full-length clone specifying chicken preprocathepsin D was isolated from a chicken follicle cDNA library by screening with a human cathepsin D probe. Whereas previous studies have demonstrated that the receptors for lipoproteins in somatic cells and oocytes, respectively, of the chicken are the products of different genes, Southern and Northern blot hybridization experiments showed that the enzymes expressed in oocytes and liver are the product of a single gene, giving rise to a 3.3-kb transcript. The primary structure of the 335-residue mature protein suggests a high degree of conservation of known crucial features of aspartyl proteases; however, the absence of the so-called processing region and of an aromatic residue in a region thought to partake in catalysis raise questions with possible evolutionary implications.
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PMID:Molecular cloning and functional characterization of chicken cathepsin D, a key enzyme for yolk formation. 141 23


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