Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.21.1 (DNase)
7,655 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Poly(adenosine diphosphate-ribose) and ds-DNA binding activity have been measured in thirty-nine systemic lupus erythematosus (SLE) sera, nineteen rheumatoid arthritis sera, fourteen sera from non-SLE rheumatic and non-rheumatic diseases and in ten normal sera. Antibodies to poly(ADP-ribose) were found only in the SLE and in three SLE-like rheumatic diseases. Anti-DNA antibodies, on the other hand, were found not only in the SLE and SLE-like diseases, but also in rheumatoid arthritis and chronic active hepatitis. Estimation of poly(ADP-ribose) binding was, therefore, more specific for, and more discriminatory of SLE from other diseases, than the estimation of ds-DNA binding. The results indicate that the estimation of poly(ADP-ribose) binding in serum may be more useful in the diagnosis of SLE than the presently employed estimation of DNA binding using the Amersham kit. DNA-anti-DNA immune complexes are detected in some of the SLE sera after deoxyribonuclease I digestion, confirming earlier reports of the existence of circulating DNA-anti-DNA complexes in SLE patients. Snake venom phosphodiesterase treatment of some of the SLE sera also resulted in increased poly(ADP-ribose) binding activity, suggesting the existence of poly(ADP-ribose)-anti-poly(ADP-ribose) immune complexes in the circulation of SLE patients. This observation raises the possiblity that poly(ADP-ribose) immune complexes may play some part in the pathogenesis of some cases of SLE.
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PMID:The significance of antibodies to poly(adenosine diphosphate-ribose) in systemic lupus erythematosus. 31 59

Autoantibody reactive with tRNA was identified by immunoprecipitation of Hela cell extract. Four out of 56 sera from patients with autoimmune chronic active hepatitis (CAH), and four out of 35 sera from patients with primary biliary cirrhosis (PBC) contained antibody directed against gel-purified tRNA in Hela cell extract, but no sera obtained from CAH type B, CAH non-A, non-B, or healthy volunteers did. Further studies on these eight anti-tRNA sera disclosed that 6 of the 8 sera that immunoprecipitated tRNA from Hela cell extract, reacted with purified tRNA, but reacted with neither 5sRNA nor ribosomal RNA species. After proteinase and deoxyribonuclease digestion of Hela cell extract, the epitope for these 6 sera was conserved, and the antigen was sensitive to ribonuclease (anti-tRNA serum). Purified Hela cell DNA digested with Eco RI or Hind III (denatured or non-denatured) could not be immunoprecipitated by these sera. In a patient with autoimmune CAH, the anti-tRNA antibody was weakly positive at week 2 and disappeared 2 months after steroid therapy started, "in parallel" with disappearance of anti-nuclear antibody. In the other 2 sera, the antigen was sensitive to proteinase.
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PMID:Autoantibody specific for transfer ribonucleic acid (tRNA) in patients with autoimmune chronic active hepatitis and primary biliary cirrhosis. 177 87

Hepatitis B (HB) core particle, in biopsied liver specimens from patients with chronic active hepatitis (type B) were stained with immunoperoxidase and chromotrope aniline blue (a non-immunological method) and the following results were obtained. HB core particles were more clearly stained with chromotrope aniline blue than with immunoperoxidase. Numerous HB core particles were seen not only in the nuclei of hepatocytes but also in the cytoplasm in HBeAg seropositive patients with severe chronic active hepatitis. DNAase digestion indicated that the HB core particles which stained with immunoperoxidase and chromotrope aniline blue contained DNA. Small amounts of HB core particles were seen in both the nuclei and cytoplasm of all anti-HBe seropositive patients with either moderate or severe chronic active hepatitis.
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PMID:Localization of hepatitis B core antigens in chronic active hepatitis using immunoperoxidase and chromotrope aniline blue staining. 244 47

A radioimmunoassay (RIA) was developed for the detection of liver-kidney microsomal (LKM) autoantibodies. These were detected in four of 62 patients with HBsAg negative chronic active hepatitis (CAH) and in one patient with mixed connective tissue disease (MCTD). LKM antibodies were not detected in other hepatic and non-hepatic diseases. Other autoantibodies, especially anti-mitochondrial ones, do not react in this assay system. Sera positive for LKM antibodies by RIA showed a cytoplasmic staining of hepatocytes and proximal renal tubules by immunofluorescence. The LKM antigen was detected by RIA in microsomes prepared from rat liver, kidney, stomach, heart, lung, and skeletal muscle. It was destroyed after treatment with trypsin and chymotrypsin, but preserved after treatment with RNAase, DNAase and neuraminidase. Upon centrifugation of purified rat liver microsomes in CsCl gradient, LKM reactivity was detected at a density of 1.20 g/ml. In addition, the M2 antigen of the inner mitochondrial membrane specific for primary biliary cirrhosis (PBC) was localized at 1.28 g/ml in these density gradient fractions. The LKM antigen could not be solubilized. The presence of LKM antibodies characterizes a distinct subgroup of HBsAg negative CAH; they do not occur in PBC.
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PMID:Detection of liver-kidney microsomal autoantibodies by radioimmunoassay and their relation to anti-mitochondrial antibodies in inflammatory liver diseases. 646 82

Antinucleolar antibody (ANoAb) was tested for in sera from 25 patients with systemic lupus erythematosus (SLE), 61 with progressive systemic sclerosis (PSS), 22 with chronic active hepatitis (CAH) and 28 healthy persons, using immunofluorescence reactivity with acetone-fixed monolayers of cultured human fibroblasts, and a procedure to reveal ANoAb when other antinuclear antibodies were concurrently present. ANoAb was found on direct testing in sera from 6 patients with SLE, 15 with PSS and 7 with CAH, but not in any of 28 sera from healthy persons; homogeneously reactive antinuclear antibody was also present in the serum of these 6 cases of SLE, in 6 of the 15 with PSS and in 3 of the 7 with CAH and, in SLE specifically, pre-treatment of fibroblast monolayers with DNase "unmasked" the presence of ANoAb in a further 7 sera which had shown only homogeneous nuclear staining in fibroblasts. ANoAb belonged to the IgG, IgM and IgA class in sera from cases of SLE and PSS, and to only the IgG and IgM class in sera from cases of CAH. ANoAb titres were highest in patients with PSS. ANoAb were sensitive to RNase in 5 cases, to RNase and DNase in 6, and were sensitive to combinations of RNase, DNase, NaC1, and trypsin in the remaining cases. We conclude that (i) fibroblast monolayers are a suitable substrate for the demonstration of ANoAb, (ii) homogeneous staining of cell nuclei may mask ANoAb, so that the incidence of ANoAb becomes higher in SLE than in PSS, (iii) low-titre ANoAb in CAH not visualized in frozen tissue sections may be detected on fibroblast monolayers, and (iv) nucleolar antigens probably include RNA, RNA bound to DNA, and RNA bound to proteins.
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PMID:Antinucleolar autoantibodies demonstrated by monolayers of human fibroblasts in sera from patients with systemic lupus erythematosus, progressive systemic sclerosis and chronic active hepatitis. 674 43