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 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 lysate of the glycogen-induced macrophages in rat peritoneal exudate was fractionated by centrifugation and extraction into a water extract, 1 M KCl extract and residue fractions. Approximately 50% of the neutral protease activity toward casein in the lysate was recovered in the KCl extract fraction, which was practically devoid of acid protease, cathepsin D. The pH optimum of the neutral protease toward casein and urea-denatured hemoglobin was pH 8.5. The activity was inhibited strongly by DFP or chymostatin and only partially by HgCl2 or PCMB. Addition of a salt to the reaction medium caused enhancement of the activity with an optimum concentration of 0.25 M: KCl, KBr, KI, NaCl, NaBr, NaI, and MgCl2 were all almost equally effective. When the enzyme preparation was filtered through a column of Sephadex G-75 gel in the presence of 1 M KCl, a larger molecular weight fraction at the void volume was obtained in addition to a smaller molecular weight fraction showing a caseinolytic activity insensitive to KCl concentration. The former was found to have a specific inhibitory effect on the latter activity.
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PMID:The occurence of a neutral protease and its inhibitor in rat peritoneal macrophages. 1 54

The object of this investigation was to determine whether the pathological events which occur during the Arthus and mixed hypersensitivity reaction could be monitored biochemically and whether changes in enzyme concentrations would reflect the severity of tissue damage either in the skin itself or in the lymph draining the lesion. The initial increase in vascular permeability which resulted in oedema formation in the tissue was reflected by a large increase in the water and protein content of the tissues, however, there was no increase in either the protein concentration or flow of the lymph. The increases in the total enzyme content in the lesion could not always be related to the macroscopic appearance of the reaction site. However, the severity of the reaction did appear to be related to the concentration of cathepsin D in the oedema fluid present at the reaction site. Although the release of enzymes was reflected in the local lymph in the case of LDH and beta-glucuronidase there was no increase in of the concentration cathepsin D in the lymph draining the lesion.
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PMID:Biochemical and cellular changes in skin and lymph during Arthus and mixed hypersensitivity reactions in rabbits. 13 25

The effect of chloroquine phosphate, a membrane stabilizing agent, on castration-induced involution in the prostate was investigated in adult Sprague-Dawley rats. Chloroquine phosphate (75 mg per kg of body weight) was administered daily by gastric tube on 4 consecutive days beginning 1 day before castration. Control rats received water. All animals were sacrificed 7 days after castration and the ventral prostates were analyzed. The chloroquine group had a mean prostatic weight 17 per cent greater than that of the water-fed control group (P less than 0.01) despite a modest loss in body weight. The activity of cathepsin D, a lysosomal enzyme, in the prostate of treated rats was double that measured in control rats. Histologically, prostates from chloroquine treated rats contained more lysosomal particles that were larger than those from control rats. Serum testosterone reached castrate levels in both groups of animals within 24 hr of castration. These results indicate that it is possible to reduce the rate of prostatic regression by chloroquine, although at a small magnitude, probably through the action of membrane stabilization.
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PMID:Partial inhibition of castration-induced involution in rat prostate by chloroquine. A preliminary observation. 46 12

An inhibitor of papain and other SH-proteases was purified 520-fold from human epidermis extracts by acetone fractionation, heat treatment, papain-Sepharose affinity chromatography, and Sephadex G-50 chromatography. The purified inhibitor had a molecular weight of 12,600 and contained no hexose, as tested by the anthrone reaction. The inhibitor survived in a boiling water bath, in 5% trichloroacetic acid, 20 mM Na3PO4 (pH 12.1) and 4 M NH4OH (pH 11.9). By isoelectric focusing 2 major activity peaks with pI's of 4.6 and 4.8, and a minor peak with a pI of 4.9 was fractioned, and 3 corresponding protein bands were seen after analytical isoelectric focusing. Immunization of rabbits with the purified inhibitor yielded a highly specific anti-inhibitor serum. The purified inhibitor inhibited papain, ficin, human cathepsins B and C, and slightly inhibited bromelain. No inhibition of serine proteases (bovine trypsin and chymotrypsin A, porcine elastase) or an acid protease (human cathepsin D) was observed. Evidence was obtained that the inhibitor formed a complex with both dithiothreitol-activated papain and enzymatically inactive mercuripapain.
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PMID:Purification and some characteristics of the human epidermal SH-protease inhibitor. 68 77

We have developed an efficient method for labeling the Asn-linked oligosaccharides of recombinant glycoproteins synthesized in Xenopus laevis oocytes. By coinjecting GDP-[3,4-(3)H]mannose with mRNA for human cathepsin D, it was possible to incorporate as much as 1800 cpm per oocyte into each of the two Asn-linked oligosaccharides of this glycoprotein. Overall, about 50% of the microinjected GDP-[3,4-(3)H]mannose was incorporated into Asn-linked oligosaccharides, a 10-fold greater value than that obtained when [2-(3)H]mannose was microinjected. Less than 10% of the injected GDP-[3,4-(3)H]mannose was metabolized to water or converted to amino acids. This technique should facilitate studies of Asn-linked oligosaccharide biosynthesis, processing, and structure in recombinant proteins synthesized in Xenopus oocytes.
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PMID:A method for [3H]mannose labeling of Asn-linked oligosaccharides on recombinant glycoproteins synthesized in Xenopus oocytes. 144 67

The effect of curing agents (salt, nitrate, ascorbic acid and glucose) and processing parameters (pH, water activity and drying and cooking temperatures) on pork muscle cathepsins B, D, H and L as well as leucyl, arginyl and tyrosyl hydrolysing activities is reported. Salt (60 g/l) showed a powerful inhibitory effect, especially on cathepsin D and aminopeptidase activities where less than 13% of the original activity was recovered. Cathepsin H was also affected (38% of the original activity) while cathepsins B and B+L recovered 72.5 and 63.0%, respectively. Nitrate (0.2-0.25 g/l) and ascorbic acid (0.2-0.4 g/l) did not significantly affect the enzyme activities. On the other hand, 0.5-2 g/l of glucose activated both cathepsins B and D with an increase of 39.5 and 28.5% and also leucyl and arginyl hydrolysing activities which were 75.0 and 24.0%, respectively. No aminopeptidase activity was detected when assayed in 100 mM sodium citrate buffer, pH 5.1. Cathepsin H was also very affected at that pH and only 12.0% of activity was recovered. A decrease in water activity, especially below 0.84, also affected the enzyme activities which were found below 50%. Temperatures in the usual range of the drying process (22 and 30 degrees C) gave substantial enzyme activities (around 40-50 and 80%, respectively).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Activities of pork muscle proteases in model cured meat systems. 161 Sep 40

The inhibitory effect of a protein isolated from rat serum on lysosomal acid cholesteryl ester hydrolase (acid CEH; EC.3.1.1.13) activity was studied. An inhibitor was purified from rat serum following ultracentrifugation and heat treatment using column chromatography on Sephacryl S-200 and ultrafiltration. The purified inhibitor appeared as a single protein band in sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis. The molecular weight of the inhibitor was 28,000 Daltons as judged by gel filtration on Sephacryl S-200 and SDS-polyacrylamide gel electrophoresis. The purified inhibitor was shown to be apolipoprotein A-I (apo A-I), the major apolipoprotein of high-density lipoprotein (HDL), using immunoprecipitation with rat anti-apo A-I immunoglobulin (Ig)G. Inhibition of acid CEH activity by apo A-I was dependent on the concentration of apo A-I. The values of Vmax obtained were similar with or without apo A-I. Apo A-I of various other mammalian species, including human, bovine and rabbit, also inhibited acid CEH activity. Other apolipoproteins, such as apo A-II and apo B, also showed inhibiting activity. On the other hand, apo A-I had no effect on the activity of other enzymes found in lysosomes, such as cathepsin D, beta-glucuronidase and acid phosphatase. The results suggest that apolipoproteins may play a role in the regulation of hydrolysis of cholesteryl esters in lipoproteins, that have been transferred to the liver, and that the inhibition of acid CEH activity by apo A-I may be a characteristic of the lipid-binding protein or be due to changes of the lipid/water interface.
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PMID:Properties of an acid cholesteryl ester hydrolase inhibitor from rat serum. 212 53

The effect of curing agents (nitrate, glucose, ascorbic acid and chloride) and physical parameters (temperature, water activity and pressure) on porcine muscle cathepsin D has been studied. Chloride (in the assayed range 0 to 75 g Cl-/L) showed a strong inhibitory effect. Nitrate (in the assayed range 0 to 800 mg/L) and high concentrations of ascorbic acid (4 to 8 g/L) slightly inhibited cathepsin D. However, its activity increased when glucose was added up to 4 g/L. Cathepsin D activity was maximal when incubated at 33 to 53 degrees C, was affected by a decrease in water activity and unaffected by pressure.
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PMID:Activity of cathepsin D as affected by chemical and physical dry-curing parameters. 238 14

The role of two phosphatases (acid and alkaline phosphatase) and a lysosomal aspartyl endopeptidase (cathepsin D) in producing rat brain oedema was studied in 3 different rat cerebral areas (i.e. frontal cortex, hippocampus and striatum) at 1, 2 and 3 d after vasogenic brain oedema induction. The percentage of water content in the frontal cortex increased immediately, 1 d after oedema induction and remained high for 2 and 3 d after oedema induction. In the hippocampus and the striatum the water content only increases 3 d after oedema induction. In the oedematous hemisphere (right), when compared to the contralateral hemisphere (left), the acid phosphatase activity decreases in the hippocampus, while the alkaline phosphatase increases in the frontal cortex and striatum; cathepsin D increases only in the striatum. The changes caused by the enzymatic activities were significant only 2 and 3 d after oedema induction. The results of this study show that: (i) the vasogenic oedema induced in experimental conditions was not sufficient to cause a massive liberation of lysosomal enzymes and (ii) brain areas adjacent (below) to the site of the experimental oedematous lesion (frontal cortex) were influenced by oedema induction.
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PMID:Phosphatases and cathepsin D activities after vasogenic oedema: an experimental study. 256 48


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