Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.22.1 (DNase II)
 429 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. The rat uterus contains acid cathepsin, beta-glucuronidase, beta-galactosidase, acid phosphatase and deoxyribonuclease II at concentrations comparable with those found in liver. Two non-hydrolytic uterine enzymes, cytochrome c oxidase and aspartate aminotransferase, display only 2-6% of the activity found in liver. 2. The concentrations of acid cathepsin and beta-glucuronidase are significantly decreased in pregnancy and increase 3-4-fold during post-partum involution. 3. The concentrations of beta-galactosidase and acid phosphatase are not decreased in pregnancy and increase only 2-3-fold during involution. 4. The concentrations of these four acid hydrolases increase linearly during the first 4 days post partum and reach their peak values at the same time that wet weight and collagen content fall to their lowest point. 5. The concentration of deoxyribonuclease is depressed in pregnancy but does not rise above normal in the post-partum period. 6. Only a small proportion of each hydrolytic activity can be isolated in the mitochondrial-lysosomal fraction of sucrose homogenates of the rat uterus. This proportion increases during involution. However, the extensive mitochondrial rupture occurring during homogenization indicates that the technique is probably too harsh to obtain a true measure of the proportion of lysosomes present in the intact tissue. 7. There are no significant changes in either the concentration or subcellular distribution of the five acid hydrolases in the livers of the experimental rats during pregnancy or involution. In each case the largest proportion of the activity is found in the mitochondrial-lysosomal fraction of liver homogenates. 8. The results are interpreted in terms of the lysosomal theory of intracellular digestion.
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PMID:Acid hydrolases of the rat uterus in relation to pregnancy, post-partum involution and collagen breakdown. 589 45

1. An homogenate of bovine adrenal medulla contains significant amounts of six acid hydrolases: acid ribonuclease, acid deoxyribonuclease, cathepsin, acid phosphatase, beta-glucuronidase and arylsulphatase. Most of the activity of each enzyme could be sedimented in the large-granule fraction at 242,000 g-min.2. Differential centrifugation indicated the presence of three populations of particles, which sedimented at slightly different rates; these are, in order of decreasing sedimentation rate, mitochondria, particles containing the acid hydrolases, and chromaffin granules.3. The three types of particle could be separated by ultracentrifuging the large-granule fraction in a sucrose density gradient. Most of the activity of each hydrolase was recovered in a layer intermediate between those formed by mitochondria and chromaffin granules.4. The large-granule fraction therefore contains particles which are defined by their enzyme content as lysosomes.5. Highly purified chromaffin granules, containing less than 5% of the activity of each acid hydrolase, were obtained from the gradient.
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PMID:The localization of lysosomal enzymes in chromaffin tissue. 594 47

The effect of methylnitrosourea (MNU) on cerebellar and cerebral DNA, RNA, protein, lysosomal enzymes (acid DNase, RNase, phosphatase, and beta-glucuronidase), and 2',3'-cyclic nucleotide 3'-phosphohydrolase (2',3'-CNPase) activities was studied in rats from birth through 12 days of age. Subcutaneous injection of MNU in a dose of 0.625 mmol/kg caused a suppression of increase in weights and content of DNA, RNA, and protein of cerebellum, but no changes in those of the cerebrum or in body weight. Ratios of protein and RNA to DNA were substantially elevated by MNU in the cerebellum but not in the cerebrum. Acid DNase and acid RNase activities of MNU-treated rats were significantly elevated beyond the increase of these activities in controls in the cerebellum, but no change in these activities by MNU was observed in the cerebrum. A slight elevation in acid phosphatase activity was observed in the cerebellum but not in the cerebrum after MNU pretreatment. Beta-glucuronidase and 2',3'-CNPase activities were not changed in the cerebellum or in the cerebrum. These results suggest that in the developing brain, especially in the cerebellum at the mitotic stage, MNU caused cell damage and inhibited cell mitosis.
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PMID:Cytotoxic effects of methylnitrosourea on developing brain. 619 99

Forty-seven human leukaemia/lymphoma cell lines belonging to myelocytic, monocytic, non-T/non-B, T-, and B-lineage and representing different levels of maturation as well as fresh cells from normal and leukaemic subjects were examined for immunological markers and cytochemically for acid phosphatase, alkaline phosphatase, alpha-naphthyl acetate esterase (pH 5.8 and 8.0), alpha-naphthyl butyrate esterase (pH 5.8 and 8.0), non-specific esterase, chloroacetate esterase, chymotrypsin-like protease, deoxyribonuclease II, beta-glucuronidase, sudan black, and periodic acid Schiff's staining. Strong sudan black, nonspecific esterase, and chloroacetate esterase reaction was obtained only for myelocytic and monocytic cell lines with the reaction intensity increasing progressively in more mature cells. Focal acid phosphatase reaction like T-ALL was found in all T-ALL cell lines, whereas myeloid/monocytoid lines had semicircular distribution and B-cell lines cytoplasmic distribution of activity. Acid phosphatase activity appeared to decline with maturation along both myeloid and T-cell lineage. High activity of alpha-naphthyl acetate esterase and alpha-naphthyl butyrate esterase both at pH 5.8 and 8.0 and of beta-glucuronidase was found in myeloid/monocytoid lines although both B- and T-cell lines in contrast to peripheral blood B-cells also had significant esterase activity. alpha-Naphthyl butyrate esterase activity declined with increasing cell maturation along myeloid lineage. Except for weak activity in two B-cell lines alkaline phosphatase was not detected in any cell lines. Monocyte esterase activity was inhibited by sodium fluoride whereas acid phosphatase, only from hairy cell leukaemia line, was resistant to L-tartarate. Although periodic acid Schiff's staining could not distinguish myeloid, T-, B-, or non-T/non-B cell lines it gave characteristic reaction (large number of coarse granules against a clear background forming a ring around the nucleus) with erythroblastic leukaemia cell line and along myeloid series its intensity increased in more mature cells. Deoxyribonuclease II and chymotrypsin-like protease staining were not discriminatory. The results of this study show that cytochemical staining characteristics of various leukaemia/lymphoma cell lines are comparable to those of corresponding cells from patients and that the intensity and pattern of expression of these activities are related to cell type and degree of cell maturation. These studies give further credence to the use of these cell lines in cell differentiation, differential drug cytotoxicity, and many other studies.
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PMID:Cytochemical comparison of immunologically characterized human leukaemia/lymphoma cell lines representing different levels of maturation. 619 Apr 91

Bloodstream forms of Trypanosoma brucei have been screened for the presence of enzymes that could serve as markers for the plasma membrane, flagellar pocket, lysosomes, endoplasmic reticulum and Golgi apparatus in order to study the subcellular organization of the digestive system of the parasite. Acetylesterase, acid DNase, acid phosphatase, acid phosphodiesterase, acid proteinase, acid RNase, alanine aminotransferase, galactosyl transferase, alpha-glucosidase, inosine diphosphatase and alpha-mannosidase were partially characterized and their assays optimized for pH-dependent activity, linearity of reaction with respect to incubation time and enzyme concentration, and the effect of inhibitors and activators. The association of these enzymes with particulate material and the presence of structural latency were investigated. Acid proteinase and alpha-mannosidase are particle-bound and latent in cytoplasmic extracts; they can be activated and solubilized in part by Triton X-100. Similar results were obtained for acid phosphatase, acid phosphodiesterase and inosine diphosphatase. Neutral alpha-glucosidase, though partly sedimentable, does not show latency and is readily solubilized by the detergent. Galactosyl transferase is firmly membrane-bound even in the presence of 0.1% Triton X-100. Cell fractionation by differential centrifugation and density equilibration on sucrose gradients revealed that both alpha-mannosidase and acid proteinase are associated with organelles that band at a density of about 1.20 g/cm3. Inosine diphosphatase, galactosyl transferase, acid phosphatase and acid phosphodiesterase sediment predominantly as microsomal constituents equilibrating at densities between 1.13 and 1.15 g/cm3. In addition, inosine diphosphatase and galactosyl transferase exhibit considerable activity at higher densities (1.18-1.25 g/cm3). Neutral alpha-glucosidase is mainly recovered in the nuclear and microsomal fraction; its particulate part equilibrates as a single band at rho = 1.22 g/cm3. Acetylesterase and acid DNase are largely soluble, whereas acid RNase does not produce distinct sedimentation and banding profiles. In intact cells, neutral alpha-glucosidase and acid phosphatase appear to be highly accessible to their substrates. It is tentatively concluded that (a) acid proteinase and alpha-mannosidase are lysosomal enzymes, (b) acid phosphatase and acid phosphodiesterase are associated with the flagellar pocket and part of the former enzyme probably with the endoplasmic reticulum, (c) galactosyl transferase is a constituent of the Golgi apparatus, and (d) alpha-glucosidase may serve as a marker for the plasma membrane. Inosine diphosphatase may also be derived from the latter structure.
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PMID:Subcellular fractionation of Trypanosoma brucei bloodstream forms with special reference to hydrolases. 624 76

Under conditions of three-hour hypobaric hypoxia the total activity of acid phosphatase and DNase in the rat liver somewhat lowers. The activity of free enzymes increases by 27 and 37%, and that of bound ones decreases by 42 and 24 %, respectively. Cytochrome c being introduced to hypoxic animals, the total activity of the enzymes does not significantly change. Under these conditions the activity of free acid phosphatase increases by 16%, and bound one decreases by 24 %. The activity of free acid DNase somewhat rises (by 12%) and that of bound one lowers (by 15%). A preliminary administration of cytochrome c to the organism prevents the development of pronounced changes in the activity of the studied lysosomal enzymes in the liver under grave hypoxia.
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PMID:[Effect of cytochrome c on the activity of lysosomal enzymes in the rat liver under hypobaric hypoxia]. 627 Aug 55

The total and unsedimentable activity of acid DNase, RNase, phosphatase and arylsulfatases A and B was examined in the rat kidneys during long-term compression of soft tissues in the presence of high excitability of the sympathoadrenal system. Injection of adrenalin to rats with trauma reduced the total activity of DNase, acid phosphatase and arylsulfatases A and B, particularly at the late periods of soft tissue compression, whereas the total activity of acid RNase slightly increased as compared with control. Compression of soft tissues after adrenalin preinjection was accompanied by a substantial rise of unsedimentable activity of the lysosomal enzymes under study in the kidneys. The activity of the enzymes in cytosol progressively ascended as the time of soft tissue injury increased.
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PMID:[Effect of adrenaline on kidney lysosome function in rats during prolonged soft tissue crushing]. 649 22

Oral administration of lantana leaf powder to guinea pigs caused an increase in the hepatic postmitochondrial fraction:homogenate ratios of activities of lysosomal enzymes--acid phosphatase, cathepsin B and DNase II. Enzyme activities of glucokinase, aldolase, lactate dehydrogenase and glucose-6-phosphate dehydrogenase were elevated whereas activity of glutathione-S-transferase decreased. Alterations in the activities of lysosomal and cytosol enzymes appear to constitute an important biochemical lesion in the pathogenesis of guinea pig liver in lantana toxicity.
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PMID:Effect of lantana toxicity on lysosomal and cytosol enzymes in guinea pig liver. 683 12

Rats were fed an all liquid diet for 7-8 weeks. One group received 35% of the calories as ethanol while the other group was pair-fed carbohydrates. Peritoneal macrophages prepared from ethanol treated rats had lower phagocytosis via the Fe-receptor and reduced viability in the presence of endotoxin, but their lysosomal enzyme activities measured (beta-glucuronidase, cathepsin D, acid phosphatase and acid DNase) were not different from controls.
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PMID:Effects of long-term ethanol consumption on rat peritoneal macrophages. 720 Dec 27

We have examined the effect of chloroquine on rat liver lysosomal enzyme distributions after isopycnic centrifugation in a sucrose gradient. Chloroquine injection causes the large majority of cathepsin C, acid phosphatase and N acetyl glucosaminidase to migrate towards lower density regions; on the other hand only about 50% of arylsulfatase and acid deoxyribonuclease are subjected to such a density shift. To specifically mark hepatocyte lysosomes and sinusoidal cell lysosomes, rats were injected with galactosylated bovine serum albumin (A) or mannosylated bovine serum albumin (B) labelled with 125I tyramine cellobiose; A is selectively endocytosed by hepatocytes, B by sinusoidal cells. The radioactivity distribution is affected by chloroquine in the same way as cathepsin C, after injection of A though it is not influenced by chloroquine after the injection of B. These results show that chloroquine does not modify the density of liver sinusoidal cell lysosomes when it decreases the density of hepatocyte lysosomes. Such a difference could result from the fact that sinusoidal cell lysosomes do not accumulate chloroquine to the same extent as hepatocyte lysosomes. Chloroquine treatment could be useful to distinguish between hepatocyte lysosomes and sinusoidal cell lysosomes.
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PMID:Chloroquine allows to distinguish between hepatocyte lysosomes and sinusoidal cell lysosomes. 843 31


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