Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

Twelve acid hydrolases, 4 near-neutral hydrolases, and alkaline phosphatase were demonstrated in 0.34 M sucrose homogenates of Trypanosoma cruzi strain Y: p-nitrophenylphosphatase and alpha-naphthylphosphatase, with optimum pH at approximately 6.0; alpha=ga;actpsodase. beta=ga;actpsodase. beta=g;icpsodase, N-acetyl-beta-glucosaminidase, cathepsin A and peptidase I and III, with optimum pH between 5.0 and 6.0; and arylsulfatase, cathepsin D, alpha-arabinase and alpha-mannosidase with optimum pH at approximately 4.0. alpha-Glucosidase, glucose-6-phosphatase and peptidase II had optimum pH at approximately 7.0. beta-Glycerophosphatase had a broad pH-activity curve from 4,0 to 7.4, with maximum activity at pH 7.0. The main kinetic characteristics of these enzymes and their quantitative assay methods were studied. No activity was detected for alpha-fucosidase, beta-xylosidase, beta-glucuronidase, elaidate esterase, acid lipase, and alkaline phosphodiesterase.
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PMID:Acid and neutral hydrolases in Trypanosoma cruzi. Characterization and assay. 4 19

The changed patterns of proteolytic activity in brain and spinal cord of Lewis rats were examined in 4 different morphological variants of EAE: ordinary induced by the standard emulsion, hyperacute induced by an emulsion plus pertussis vaccine, passive induced by donor EAE cells, and monocytic induced by treatment of passive EAE with the immunosupressive drug tilorone. The following enzymatic changes were found: firstly, in ordinary EAE there was a 2--3.5-fold increase in cathepsins A and C (E.C. 3.4.14.1) in spinal cord one day following the appearance of paralysis with a smaller change in hindbrain, and none in the forebrain regions. With recovery from paralysis, levels of cathepsin A remained high in upper cord, and cathepsin C levels fell to about half. In contrast, increase in cathepsin D(E.C. 3.4.23.5) was smaller and occurred only 4--5 days after paralysis with the largest change in spinal cord areas and with only a small decrease on recovery from paralysis. Secondly, in hyperacute EAE, the increase in all cases was smaller with the largest change in cathepsin A level in upper spinal cord. In passive EAE, the most significant increase occurred only in the lower spinal cord for cathepsins A and C, and fourthly, in monocytic EAE induced by tilorone, there was an exceptionally large, 3-fold increase in cathepsin C in lower cord as compared to a 1.5-2 fold increase for other cathepsins. No major differences were observed on comparison of antigens from different sources (guinea pig and bovin spinal cord myelin peptide). An attempt is made to relate enzymatic changes to the morphological features of each variant with special reference to the nature of the infiltrating cells.
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PMID:Proteolytic enzymes in ordinary, hyperacute, monocytic and passive transfer forms of experimental allergic encephalomyelitis. 84 13

The cathepsins D from trout muscle and from bovine spleen, as well as cathepsin A from bovine spleen are inhibited by a crude proteinase inhibitor from potato tubers. Cathepsins C and B1 are not inhibited. It was shown by isoelectric focussing that several inhibitors for cathepsin D are present in potatoes. Those with isoelectric points at pH 9.2, 9.1, 9.0, 8.9, 8.5 inhibit cathepsins D both from trout muscle and from bovine spleen. In addition some inhibitors with isoelectric points at pH 6.6, 6.5, and 6.2 were observed, which inhibit cathepsin D from trout muscle only.
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PMID:[Inhibition of cathepsins from trout muscle and from bovine spleen by proteinase inhibitors of potato tubers (author's transl)]. 100 25

Protein breakdown in submandibular glands rendered hypertrophic by amputation of the lower incisor teeth in rats was investigated. Reduced protein breakdown was observed in the hypertrophic gland tissues, and was found to be inhibited by 20 mM epsilon-amino-n-caproic acid, an inhibitor of serine protease, and 50 microM leupeptin, an inhibitor of trypsin, plasmin, papain and cathepsin B, but not by 2 mM PMSF (phenylmethylsulfonyl fluoride), an inhibitor of serine protease, 10 microM pepstatin, an inhibitor of cathepsin D and 20 microM antipain, an inhibitor of cathepsin A and B. These results suggest that some serine proteases and leupeptin-sensitive proteases (presumably cathepsin B) participate in protein breakdown in hypertrophic gland tissues, and that hypertrophy of the submandibular glands is closely related to the reduced protein breakdown in these tissues.
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PMID:Protein breakdown in submandibular glands rendered hypertrophic by amputation of lower incisor teeth in rats. 223 Sep 61

A study was made of the total and nonsedimented activity of 4 lysosomal proteinases in the liver, kidneys and blood serum of rats fed for 4 months krill protein isolate (AtlantNIRO) as the only source of protein or that replaced by 50% with a control protein (casein) contained by the 18% protein (in terms of caloricity) diet. The use of the krill isolate as the only source of protein brought about a significant increase in the total activity of cathepsin A and cathepsin D and in nonsedimented activity of cathepsins A, D, B and C in rat liver (by 95, 23, 32 and 50%, respectively). Meanwhile in the kidneys, there was an increase in the total activity of cathepsins A and D. Proteinases A, D, B and C were activated in the blood serum. The 50% replacement of the krill isolate by casein elicited a substantial decrease in the adverse effect of the krill protein isolate on metabolic processes in rats.
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PMID:[Effect of the consumption of krill protein isolates on lysosomal proteinase activity in rats]. 390 7

Low density lipoproteins have been implicated in the pathogenesis of atherosclerosis. A study has therefore been made of their proteolytic degradation by homogenates of cultured smooth muscle cells from the pig aorta. The pH optimum of proteolysis of 125I-labelled low density lipoproteins was 4.25, thus suggesting the involvement of lysosomal cathepsins. Proteolysis at acid pH started to become saturated at low density lipoprotein concentrations of approx. 20 microgram of protein/ml, but did not obey Michaelis-Menten kinetics. After a lag period of approx. 10 min, proteolytic degradation was linear with time up to at least 4 h incubation, but showed a sigmoidal relationship with homogenate concentration. When cathepsin D was inhibited by pepstatin, the proteolysis of 125I-labeled low density lipoproteins was inhibited by more than 90%, whereas when cathepsin B was inhibited by leupeptin, the rate of proteolysis decreased by approx. 50%. Antipain, which inhibits both cathepsins A and B, did not inhibit proteolysis any more than leupeptin, thus suggesting a minor role, if any, for cathepsin A. a combination of pepstatin and either leupeptin or antipain inhibited proteolysis completely. Cathepsins B and D acted synergistically in the degradation of 125I-labelled low density lipoproteins.
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PMID:Proteolytic degradation of low density lipoproteins by arterial smooth muscle cells: the role of individual cathepsins. 701 93

In vivo proteolytic modification of liver aldolase on administration of leupeptin, a thiol proteinase inhibitor of microbial origin, is reported. When leupeptin was injected into rats, the activity of aldolase in the liver decreased to 40% of that in control rats. Molecular properties of aldolase isolated from the livers of control rats and leupeptin-treated rats indicated that a decrease of aldolase activity is attributable to hydrolysis of a peptide linkage(s) near the carboxyterminal of the enzyme. Injection of leupeptin also caused marked increase in the activities of free lysosomal proteinases, such as cathepsin A and cathepsin D and moderate increase of cathepsin B and cathepsin L. Increase in free activity of cathepsin A returned to the level of control rats by 12 hr after injection of leupeptin, whereas 36 hr was required for recovery of decreased aldolase activity. When insulin was coinjected with leupeptin, increase in the activity of free cathepsin A and decrease of activity of aldolase produced by the injection of leupeptin was prevented. These findings indicate that modification of aldolase may be due to action of a lysosomal protease(s). Incubation of the purified aldolase with the lysosomal fraction produced the same changes in properties of aldolase as those observed in vivo on injection of leupeptin. The aldolase inactivating proteinase in the lysosomal fraction was inhibited by PMSF and leupeptin and not by pepstatin. Purified cathepsin A (a serine proteinase), cathepsin B and cathepsin L (thiol proteinase) are potent inactivators of aldolase but cathepsin H and cathepsin D are not. Cathepsin A, B and L are involved in inactivation of aldolase in lysosomes. Endogenous thiol proteinase inhibitor which inhibits lysosomal thiol proteinases (cathepsin B, L and H) is found in the cytosol fraction of liver. The level of thiol proteinase inhibitor actually decreased to 60% of that in control rats in leupeptin-treated rats, suggesting that non-thiol proteinase cathepsin A is a major factor in inactivation of aldolase in lysosomes. Not only leupeptin but also other proteinase inhibitors (antipain, E-64-D, chloroquine) caused increase of labilization of the lysosomes and decrease in aldolase activity. Physiological stimuli which are known to induce the labilization of the lysosomal membrane, such as starvation and glucagon, caused slight or no significant increase of activities of free cathepsin A and D and resulted in no apparent change in aldolase activity.
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PMID:Modification of rat liver fructose biphosphate aldolase by lysosomal proteinases. 705 71

1. Growing rats were fed either ad lib. or with six (equal) meals offered every 4 h (from 10.00 hours). Rats of each group were killed at intervals of 4 h beginning at 11.00 hours. Activities of cathepsin A (carboxypeptidase A; EC 3.4.12.2), C (dipeptidyl peptidase; EC 3.4.14.1) and D (endopeptidase D EC 3.4.23.5) were measured in liver and muscle homogenates and free amino acids in blood were determined. 2. In the rats fed ad lib. activities of carboxypeptidase A and endopeptidase D in liver and muscle showed significant variation, with maximum activity in the light period. In general, meal-feeding only caused minor differences in cathepsin activities; although significant differences occurred for carboxypeptidase A. For the later enzyme a peak in activity occurred in the dark as well as in the light period. 3. Irrespective of the feeding schedule, the lower concentration of free essential amino acids of blood occurred generally during the night period. With the controlled-feeding schedule there is an increase of essential amino acids and a slight decrease of non-essentail amino acids of blood.
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PMID:Variations through the day of hepatic and muscular cathepsin A (carboxypeptidase A; EC 3.4.12.2), C (dipeptidyl peptidase; EC 3.4.14.1) and D (endopeptidase D; EC 3.4.23.5) activities and free amino acids of blood in rats: influence of feeding schedule. 719 24

The activity of cathepsin A, cathepsin D and other enzyme-markers of liver damage (ASPAT, ALAT, GGTP, LDH, AP) were measured in the serum of persons acutely intoxicated with ethanol and chronic alcoholics. Persons acutely intoxicated with ethanol had the unchanged activity of cathepsin A and cathepsin D while it increased in the chronic alcoholic serum.
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PMID:The activity of cathepsin A and cathepsin D in the serum of persons acutely intoxicated with ethanol and chronic alcoholics. 852 92

Mannose 6-phosphate (Man-6-P) is a posttranslational carbohydrate modification typical of newly synthesized acid hydrolases that signals targeting from the Golgi apparatus to the lysosome via Man-6-P receptors (MPRs). Using iodinated cation independent MPR as a probe in a Western blot assay, we surveyed levels of Man-6-P glycoproteins in a number of different rat tissues. Considerable variation was observed with respect to total amounts and types of Man-6-P glycoproteins in the different tissues. Brain contained 2-8-fold more Man-6-P glycoproteins than other tissues, with relative abundance being brain >> testis approximately heart > lung approximately kidney approximately ovary approximately spleen > skeletal muscle approximately liver approximately serum. Analysis of 16 different lysosomal enzyme activities revealed that brain contains lower activities than other tissues which suggested that decreased removal of Man-6-P results in increased levels of Man-6-P glycoproteins. This was directly demonstrated by comparing activities of phosphorylated lysosomal enzymes, purified by immobilized MPR affinity chromatography, with total activities. The phosphorylated forms accounted for a considerable proportion of the MPR-targeted activities measured in brain (on average, 36.2%) but very little in lung, kidney, and liver (on average, 5.5, 2.3, and 0. 7%, respectively). Man-6-P glycoproteins were also isolated from rat brain by MPR affinity chromatography on a preparative scale. Of the 18 bands resolvable by SDS-polyacrylamide gel electrophoresis, seven bands were NH2-terminally sequenced and identified as the known lysosomal enzymes cathepsin L, cathepsin A, cathepsin D, alpha-galactosidase A, arylsulfatase A, and alpha-iduronidase. One of the major Man-6-P glycoproteins was identified as palmitoyl protein thioesterase, which was not previously thought to be lysosomal. This finding raises important questions about the cellular location and function of palmitoyl protein thioesterase, mutations in which result in the neurodegenerative disorder, infantile neuronal ceroid lipofuscinosis.
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PMID:Rat brain contains high levels of mannose-6-phosphorylated glycoproteins including lysosomal enzymes and palmitoyl-protein thioesterase, an enzyme implicated in infantile neuronal lipofuscinosis. 870 98


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