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)

Acid and neutral deoxyribonucleases (DNases) of the cow snout epidermis were investigated by the microdisc-electrophoresis of polyacrylamide gels containing highly polymerized DNA and by isoelectric focusing techniques. The nucleases were characterized with respect to their pH optimum. An acid DNase at pH 5.0 was detected as a single distinct band after the electrophoretic separation. After isoelectric focussing also, only one acid DNase activity with an isoelectric point (IP) of 6.2 was detectable. Neutral DNases at pH 7.4 were demonstrated as major and minor bands by their different electrophoretic mobilities. In the isoelectric focusing system also, two neutral DNases, a major one (IP, 4.6) and a minor one (IP, 6.4), were found. Characterization with respect to their histologic location showed acid and neutral DNases across the epidermal layers with the highest activities in the upper layers, where DNA concentration had been shown to be lowest. In correlation with their subcellular distribution, the highest activities of both acid and neutral DNase were found in the 105,00 X g supernatant of the subcellular fractions.
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PMID:Microdisc-electrophoretic study of deoxyribonucleases in cow snout epidermis. 662 44

Bovine serum albumin was found to have an inhibitory effect on acid DNase from rat small intestinal mucosa. The inhibitory activity showed pH-dependency. Thus, the highest inhibition was observed at about pH 4.3 but conversely the enzyme was activated at about pH 4.7. The inhibitory effect was heat-inactivated most strongly at about pH 5, but at more acidic or alkaline pHs, no inactivation was observed. Inhibitory activities of serum albumin of various species were comparable with that of bovine serum albumin. Acid DNases from guinea pig kidney and small intestinal mucosa and from rat spleen and kidney were similarly inhibited by the albumin. The acid DNase displays typical Michaelis-Menten kinetics but the kinetics became sigmoidal in the presence of the inhibitor. With increasing inhibitor concentration, the sigmoidal shape became more pronounced, and at high concentration, the DNA was able to compete with the inhibitor and to reverse its action. Among the cyanogen bromide-cleaved fragments of bovine serum albumin, fragment C (derived from the carboxyl-terminal two-thirds of the albumin) had an inhibitory effect comparable to that of intact bovine albumin, but fragment N (derived from the amino-terminal one-third of the albumin) had no activity. Reduced fragment C showed a markedly decreased effect and lost the activity completely after separation into its three component peptides. Acetylation of bovine serum albumin completely destroyed its inhibitory activity.
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PMID:Inhibitory effect of bovine serum albumin on acid deoxyribonuclease from rat small intestinal mucosa. 663 Jan 63

We studied metabolism of brain DNA in three myelin deficient mutants qk, jp and jpmsd mice. The DNA content, the in vivo incorporation of [14C]thymidine in DNA and the activity of acid DNase in tissues (cerebellum and cerebrum) from normal littermates and affected mice were compared. The results showed that neither the DNA content, the incorporation of [14C]thymidine in DNA nor the activity of acid DNase in brain were altered in qk affected mice. In jpmsd mice, however, the DNA content as well as the incorporation of thymidine in DNA were reduced in both cerebellum and cerebrum, but the activity of acid DNase was reduced in cerebrum only. In jp mice, although the DNA content was reduced in both cerebellum and cerebrum, the incorporation of thymidine in DNA and the activity of acid DNase were reduced in cerebrum only. The data suggest a) that in qk mutants DNA metabolism and hence cell (glial) proliferation is not affected; b) that in jpmsd mutants DNA synthesis, and thus the cell proliferation is reduced in cerebellum as well as in cerebrum of the affected mice and c) that in jp mutants the synthesis of DNA and the cell proliferation is reduced in cerebrum but not in cerebellum.
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PMID:Brain DNA metabolism in myelin deficient mutant jp, jpmsd and qk mice. 667 43

Adrenaline (10-6 g/ml) and insulin (10-6-8 IE/ml) cause changes of the acid DNase and phosphatase activity in hepatic cells of rat embryos on the 20th day of development. Adrenaline stimulates granular endoplasmatic reticulum development, increases the number and size of lysosomes, breaks their integrity. Insulin practically has no effect on the DNase activity, but labilizes the lysosome membrane.
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PMID:[Characteristics of the reaction of the embryonic hepatocyte to the effect of insulin and adrenaline]. 702 32

The levels of Acid and Alkaline DNases were measured in the serum of patients with: (a) Cancer of the Genitourinary Tract (confirmed by biopsy), (b) with inflammatory diseases and non-malignant tumours of the Genitourinary tract, (c) healthy blood donors. In the first group the results showed that the Acid DNase level was raised in 62% and Alkaline DNase in 43%. In the second group acid DNase was increased in 30% and Alkaline DNase in 13%. In the third group Acid and Alkaline DNase levels were normal. These results suggest that the measurement of Acid and Alkaline DNases could be considered as malignant diseases markers, in spite of false positive and false negative results in some cases.
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PMID:The role of acid and alkaline DNases as tumour markers in cancer of the genitourinary tract. 711 81

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

Some lysosomal enzymes (viz., acid DNase, acid RNase and beta-glucuronidase) were estimated in different parts of the rabbit Fallopian tube during different hours post coitum (p. c.). At estrus, alterations of acid RNase and beta-glucuronidase were observed in different anatomical segments of the Fallopian tube but acid DNase was undetectable. When these enzymes were compared at different hours p.c., it was noticed that when the ovum reaches ampullary (A), ampullary-isthmic junction (AIJ) and isthmic (I) segments of the Fallopian tube at the respective hours 14, 24 and 70, the acid DNase activity showed increased value in these parts when compared to their preceding groups. Acid RNase also showed similar type of pattern except that it was not altered at 14 hr p. c. At 144 hr p. c. both the enzymes had no significant alteration over 70 hr value, beta-glucuronidase, however, did not show this type of pattern in all the segments till 144 hr p. c. The increased activity of acid RNase and DNase in AIJ and I segments of the tube till 70 hr p. c. suggests the increased lysosomal activity in the tubal fluid produced by secretory cells. The possible involvement of these lysomal factors in the process of fertilization and preparation of ovum prior to implantation is suggested.
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PMID:Variations of lysosomal enzymes in different parts of rabbit Fallopian tube during ovum transport. 722 24

The uptake in vitro was studied of 3H-labeled DNA-anti-DNA complexes by neutrophils and monocytes from human blood. Complexes were prepared from 3H-labeled circular double-stranded (dS) DNA of bacteriophage PM2 and anti-dsDNA-containing sera from patients with systemic lupus erythematosus. After phagocytosis, cells and medium were separated. The cells were treated with DNase to remove adherent and noningested complexes before the cell-associated radioactivity was counted. Thus, only complexes inside the cells were measured. The medium was analyzed for acid-precipitable radioactivity. In this way, we found that neutrophils only phagocytose the complexes, whereas monocytes phagocytose the complexes and degrade the antigen. In contrast, both types of phagocyte degraded the antigen in tetanus-anti-tetanus complexes. The degradation took place after phagocytosis, inside the cells. The difference in DNA degradation between neutrophils and monocytes correlated with the difference in acid DNase activity of the lysosomal fractions: monocytes contained DNase activity, neutrophils did not. With complexes made from DNA with 131I-labeled anti-DNA, we found that both cell types degraded the antibody. Uptake of complexes and degradation of antigen increased with incubation time and cell concentration and was saturable with respect to complex concentration. The processes were inhibited by 5 mM mono-iodoacetic acid or by low temperatures.
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PMID:Phagocytosis and degradation of DNA-anti-DNA complexes by human phagocytes. I. Assay conditions, quantitative aspects and differences between human blood monocytes and neutrophils. 730 85

After incubation with DNA human lymphocytes release neutral and acid DNase activities into the culture medium; the release depends on DNA concentration and time of cultivation. The electrophoretic mobility of the released neutral DNase activity is in accordance with DNase I and the electrophoretic mobility of the released acid DNase activity with DNase II. The released DNase activities do not originate from dead cells and are not influenced by blast cell formation. The anesthetic halothane can inhibit the released neutral and acid DNase activities. Inhalation anesthesia can possibly disturb the correlation between DNA and DNases in human blood.
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PMID:Secretion of neutral and acid DNases in cultivated human lymphocytes after incubation with DNA; possible consequences for inhalation anesthesia. 754 35

The sequence preference of a Drosophila lysosomal DNase was studied on the Drosophila hsp 70 heat-shock and histone recombinants, which carry six different genes, and the surrounding spacer sequences. The distribution of cleavage sites was random in respect of the locations of gene and spacer sequences. However, in the presence of 10 mM spermidine, a major transition was observed: the coding sequences became more susceptible than the spacer regions to nuclease attack. A similar transition was induced in the sequence preference of DNase I if the digestion was performed in the presence of spermidine at pH 5.2. At pH 7.5, spermidine does not influence the sequence preference of DNase I, which indicates the involvement of DNA protonation in this transition. In the presence of spermidine, the distributions of preferred and protected sequences were almost indistinguishable for these nucleases, suggesting that the protonated DNA, and not the enzymes, is the target of spermidine. A Drosophila embryonal protein was detected and partially purified which induced the same transition as observed in the presence of spermidine. The purified protein preferentially protected the spacer DNA sequences against acid DNase or DNase I cleavage in the hsp 70 heat-shock and histone gene recombinants. The protection was concentration dependent and occurred only at pH 5.2. The transition of nuclease specificity is probably due to a conformational change in the protonated DNA, induced by the binding of either the embryonal protein or spermidine.
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PMID:Spermidine-induced alteration in the gene-spacer discrimination of nucleases in protonated DNA. 848 53


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