Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.23.5 (cathepsin D)
 4,130 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Hormonal and cholinergic influences on lysosomal and digestive enzyme activities in pancreatic tissue were studied in normal adult rats. Hormonal stimulation by the cholecystokinin analogue, caerulein, induced a marked enhancement of the activities of cathepsin D and N-acetyl-beta-D-glucosaminidase in pancreatic tissue, whereas the activities of amylase and lipase tended to decrease. Acid phosphatase activity was not affected. Further, caerulein was found to induce a significant increase of cathepsin D output in bile-pancreatic juice. This output largely parallelled that of amylase. Cholinergic stimulation by the muscarinic agonist carbachol, at a dose level giving the same output of amylase as caerulein, did not affect pancreatic activities of cathepsin D and N-acetyl-beta-D-glucosaminidase. Further, cholinergic stimulation induced an increase of amylase activity and a slight decrease of acid phosphatase activity in pancreatic tissue. Lipase activity was not affected. No apparent effect on cathepsin D output in bile-pancreatic juice was encountered after cholinergic stimulation. The activities of neither the digestive nor the lysosomal enzymes were influenced by the administration of secretin. The results suggest a possible lysosomal involvement in caerulein-induced secretion and/or inactivation of pancreatic digestive enzymes, whereas cholinergic stimulation seems to act through different mechanisms.
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PMID:Hormonal and cholinergic influences on pancreatic lysosomal and digestive enzymes in rats. 619 43

Activities of acid phosphatase and cathepsin D were studied in liver, spleen tissues and in blood serum of Wistar male rats with a body mass of 180-200 g within various periods after total gamma-irradiation using 137Cs (1.9 Gr/min) at doses of 7.5 and 30 Gr. Acid phosphatase was maximally activated in the non-sedimented fraction of spleen within 72 hrs at the dose of 7.5 Gr; activity of cathepsin D was decreased in the fraction and exceeded the control values only within 11 days. Activity of both enzymes was decreased in the fraction of precipitate. In liver tissue the enzymatic activity was only slightly altered at the dose used. The dose of 30 Gr altered the acid phosphatase activity both in spleen and liver tissues; the enzymatic activity was increased in non-sedimented fraction and--decreased in precipitate. In blood serum the acid phosphatase activity increased gradually up to the animal death.
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PMID:[Effect of lethal and superlethal doses of gamma-irradiation on the lysosomal enzyme activity in radio-sensitive and radio-resistant tissues in the rat]. 652 27

Enzymatic activity was investigated in metal-binding proteins from rat epidermal cells. Tris-HCl buffer soluble and KSCN solubilized proteins were extracted stepwise from granular and cornified cells of 2-day old rat epidermis. Each extract was separately applied to a Cu2+ or Zn2+ chelate Sepharose 6B column and the proteins were eluted with buffers of different pHs and finally with EDTA solution. Metal chelate-binding proteins were found in both soluble and solubilized proteins but there was a larger amount in the latter. Affinity of the proteins to bind with Cu2+ chelate was greater than that with Zn2+ chelate. In Tris-HCl buffer extract, histidase activity was detected in Cu2+ chelate-binding proteins, but not in Zn2+ chelate-binding proteins. Acid phosphatase, cysteine proteinase, dipeptidase, cathepsin D, beta-galactosidase, gelatin hydrolase, and superoxide dismutase did not bind to metal chelates although these enzymes, except acid phosphatase, were inhibited by Cu2+, but not by Zn2+. In contrast, KSCN solubilized metal chelate-binding proteins showed plasminogen activator, acid phosphatase, and gelatin and casein hydrolases while histone hydrolase did not bind to either chelate column. Since metal-binding proteins in rat epidermal cells have been shown previously to be histidine- and cysteine-rich proteins concentrated in keratohyalin granules, interaction of metals and the structural proteins with certain enzymes may be involved in the regulation of epidermal cell functions.
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PMID:Enzymatic activity of metal-binding proteins in epidermal cells. 653 44

The enzymatic activity of 6 acid hydrolases was studied in rat epididymal homogenates following castration, testosterone replacement and during postnatal growth. Acid phosphatase and N-acetyl-beta-D-glucosaminidase activity decreased after castration and increased with hormonal treatment as well as during growth. Beta-Glucuronidase and cathepsin D activity increased during the involution of the organ and decreased or did not change with hormone treatment or during sexual maturation. Arylsulphatase and deoxyribonuclease did not recover normal activity after hormonal treatment. Their activities were particularly high in epididymal and rete testis fluid of normal animals.
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PMID:Effect of androgens on the activity of acid hydrolases in rat epididymis. 711 73

Autolysosomes were isolated from rat livers treated with leupeptin by a combination of differential and Percoll density gradient centrifugation techniques. The purified autolysosome fraction was verified by morphological analysis to be highly purified and to contain contaminants which were scarcely detectable. The enrichment of the lysosomal enzyme activities in the purified autolysosomes over the homogenate was 12-, 14-, 22-, and 24-fold for beta-glucuronidase, acid phosphatase, beta-N-acetylglucosaminidase, and cathepsin D, respectively. Measurement of the activity of the marker enzymes for various subcellular organelles also proved that the purified autolysosome fraction was essentially free from contamination by other organelles. When the autolysosomes isolated from rat livers treated with leupeptin for 1 h were disrupted by osmolysis, acid hydrolases were easily solubilized. Acid phosphatase, however, became membrane bound in the autolysosomes prepared at longer periods of time after the leupeptin treatment. The autolysosomes exhibited enhanced permeability of the membranes after a short duration of time after the leupeptin treatment (30 and 60 min) and became stabilized later. These changes in the properties of the autolysosomes with time after the leupeptin treatment may be interpreted as meaning that progressive rearrangement of the lysosomal constituents occurred within the autolysosomes with time after the genesis.
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PMID:Isolation and characterization of autolysosomes which appeared in rat liver after leupeptin treatment. 711 55

Ammonia is a natural lysosomotropic compound. Concentrations of ammonium acetate > 2 mM impaired the phagocytic activity of BV-2 cells, an immortalized microglial cell line, as was determined by the uptake of fluorescent latex microspheres of different sizes. In contrast, an increase in the uptake of fluorescent dextran was observed with the elevation in ammonium acetate concentrations. This indicates that ammonia affects phagocytotic and pinocytotic activities of BV-2 cells differently. Interferon-gamma- and polyinosinic-polycytidylic acid-stimulated secretion of IL1 alpha as well as LPS-stimulated secretion of IL6 decreased with an elevation in ammonium acetate concentrations. The constitutive secretion of IL1 alpha was not significantly affected by ammonium acetate. However, an increase in LPS-stimulated IL1 alpha secretion was observed at 10 mM and 20 mM ammonium acetate. High concentrations of ammonia affected the activity of lysosomal enzymes of the BV-2 cells. Acid phosphatase and alpha-glucosidase activities increased with the increase in ammonium acetate up to 20 mM. The activity of cathepsin D was increased at 5 mM, but decreased at higher ammonia concentrations. The effects of ammonia on microglial functions are discussed with respect to pathogenetic mechanisms of dementia of the Alzheimer type.
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PMID:Effect of ammonia on endocytosis, cytokine production and lysosomal enzyme activity of a microglial cell line. 782 5

Chronic administration of Senna occidentalis seeds induces an experimental toxic myopathy characterized by skeletal muscle fibers atrophy, decrease in histochemical activity of cytochrome oxidase, and increase of the acid phosphatase activity in muscle fibres at the light microscopic level. The mechanisms that lead to the increase of this lysosomal enzyme activity are not known and could be related to other biochemical disturbs than the mitochondrial function impairment. The main aim of the present study is to localize the acid phosphatase activity using a cytochemical method at transmission electron microscopy level and to quantify cathepsin D in muscle of rats chronically intoxicated with Senna occidentalis seeds by immunoblotting. Acid phosphatase was observed in lysosomes and over profiles of some organelles apparently not involved by lysosomal membrane. In addition immunoblotting demonstrated a decrease in the content of the precursor and of the mature form of cathepsin D in samples of muscles and liver of intoxicated animals. We concluded that there is a selective increase in acid phosphatase activity in muscle--and maybe in other tissues--of animals intoxicated with Senna occidentalis, that can be related to the skeletal muscle atrophy and the intense decrease in weight gain of these animals. Further studies should be performed to establish the mechanisms of selectivity in increase of lysosomal enzymes in different situations and pathological states.
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PMID:The lysosomal enzymes acid phosphatase and cathepsin D in rats intoxicated with Senna occidentalis seeds. 1045 11

This study was conducted to determine whether the application of high hydrostatic pressure could modify the enzymatic activity and membrane integrity of lysosomes in muscle. Several combinations of pressure (0-600 MPa) and time (0-300 s) were applied to two types of samples: purified enzymes (cathepsin D and acid phosphatase) in buffer solution and intact muscle (biceps femoris). The enzymes studied showed varying degrees of susceptibility depending on the level of pressure, holding time, and environment. Acid phosphatase activity was minimally affected by pressure in buffer solution, whereas cathepsin D was modulated significantly by the pressure and time applied. The activities of the enzymes extracted from meat increased with pressure. The cytochemical observations showed the presence of primary and secondary lysosomes in muscles. After pressurization, the membrane integrity of the lysosomes was modified. A correlation could be established between lysosomal enzymatic activities and the lysosome membrane breakdown.
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PMID:High-pressure effects on lysosome integrity and lysosomal enzyme activity in bovine muscle. 1088 69

Quercetin (QC) (5, 7, 3', 4' -tetra oxyflavonolol) is an ubiquitous flavonoid in many plants. The influence of QC on the growth of B16 melanotic melanoma in C57BL/6 mice and activity of some acid hydrolases in the tumor homogenates were investigated. Two series of experiments were carried out: In the first experimental group mice were inoculated s.c. with 10(6) of tumor cells (TC) suspended in 1 ml of saline. TC were obtained from the current serial passages. In the second series of experimental group mice were inoculated with melanoma cells preincubated 15 min. in different concentrations of QC. Mice of both series were divided into three subgroups. Mice of the first series were treated with QC i.p. every second day in a dose of 0.1 mg, 0.5 mg or 1.0 mg (total dose of 1.0 mg, 5.0 mg or 10.0 mg per mice). Animals of the second series did not obtain any treatment. After the nineteenth day of experiment the mice were killed, tumors excised and weighed. Tumor tissue pieces were homogenized for enzyme activity determination. Fragments of tumor tissue were taken for electron microscopy (EM) investigation. In mice injected i.p. with QC mean tumor weight was significantly higher than in control I. The mean tumor weight in the first experimental group was higher than in control from 170% to 196% and in the second experimental group from 69% to 147%. Enzymes activity was also higher in both experimental groups as compared to controls. Arylsulphatase activity in the first group was higher from 102% to 144% and in the second one - from 97% to 115% than in control I. Acid phosphatase activity was higher from 100% to 155% in the first experimental group and from 56% to 161% in the second one. Cathepsin D activity was greater from 133% to 333% and from 113% to 300%, respectively. EM studies revealed the presence of greater number of Golgi structures and primary lysosomes in experimental groups of tumors (mice treated with QC and mice with melanoma preincubated in QC). These results clearly indicate that QC significantly enhances melanotic melanoma growth and increases acid phosphatase and cathepsin D activity in these tumors. The mechanism of QC action on the melanotic melanoma is not fully understood and remains to be defined.
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PMID:Influence of quercetin on B16 melanotic melanoma growth in C57BL/6 mice and on activity of some acid hydrolases in melanoma tissue. 1132 32

In this work, we have investigated the involvement of DmCatD, a cathepsin D-like peptidase, and acid phosphatase in the process of follicular atresia of Dipetalogaster maxima, a hematophagous insect vector of Chagas' disease. For the studies, fat bodies, ovaries and hemolymph were sampled from anautogenous females at representative days of the reproductive cycle: pre-vitellogenesis, vitellogenesis as well as early and late atresia. Real time PCR (qPCR) and western blot assays showed that DmCatD was expressed in fat bodies and ovaries at all reproductive stages, being the expression of its active form significantly higher at the atretic stages. In hemolymph samples, only the immunoreactive band compatible with pro-DmCatD was observed by western blot. Acid phosphatase activity in ovarian tissues significantly increased during follicular atresia in comparison to pre-vitellogenesis and vitellogenesis. A further enzyme characterization with inhibitors showed that the high levels of acid phosphatase activity in atretic ovaries corresponded mainly to a tyrosine phosphatase. Immunofluorescence assays demonstrated that DmCatD and tyrosine phosphatase were associated with yolk bodies in vitellogenic follicles, while in atretic stages they displayed a different cellular distribution. DmCatD and tyrosine phosphatase partially co-localized with vitellin. Moreover, their interaction was supported by FRET analysis. In vitro assays using homogenates of atretic ovaries as the enzyme source and enzyme inhibitors demonstrated that DmCatD, together with a tyrosine phosphatase, were necessary to promote the degradation of vitellin. Taken together, the results strongly suggested that both acid hydrolases play a central role in early vitellin proteolysis during the process of follicular atresia.
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PMID:The Role of DmCatD, a Cathepsin D-Like Peptidase, and Acid Phosphatase in the Process of Follicular Atresia in Dipetalogaster maxima (Hemiptera: Reduviidae), a Vector of Chagas' Disease. 2609 Dec 89


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