Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0024141 (systemic lupus erythematosus)
 44,322 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A 20-year-old patient had systemic lupus erythematosus and extensive generalized discoid disease that failed to respond to conventional treatment with topical steroids and high doses of hydroxychloroquine sulfate (Plaquenil). The skin lesions responded dramatically to 100 mg of azathioprine sodium daily, flared when the drug treatment was discontinued, and again responded on reinstatement of the same dosage of azathioprine. The case report suggests that extensive discoid skin lesions can be successfully treated with oral azathioprine.
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PMID:Successful treatment of generalized discoid skin lesions with azathioprine. Its use in a patient with systemic lupus erythematosus. 403 29

Surface radioiodination of lymphocytes by the lactoperoxidase procedure has permitted demonstration of an assortment of different antibodies to lymphocytes in the sera of patients with systemic lupus erythematosus. One type of antibody proved of special interest because it appeared to be associated with inhibition of the responder cells in the mixed leukocyte culture reactions. This reacted with an antigen on T cells and thymocytes which on sodium dodecyl sulfate acrylamide gel electrophoresis showed a molecular weight of approximately 15,000 daltons. The possible relation of this antigen to T cell receptors and products of immune response genes is discussed.
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PMID:Antibodies to a specific surface antigen of T cells in human sera inhibiting mixed leukocyte culture reactions. 454 34

The activity of phospholipase inhibitory protein, lipomodulin, partially purified from rabbit neutrophils, was markedly decreased after treatment with sera from patients with rheumatic diseases such as systemic lupus erythematosus, rheumatoid arthritis, and dermatomyositis. The decrease of the protein's inhibitory activity on phospholipase A2 paralleled the amount of [35S]methionine-labeled lipomodulin precipitated by the sera. Absorption of patients' sera with anti-human IgM (mu chain) or protein A-agarose, but not with anti-human IgG (gamma chain), decreased their ability to decrease the activity of lipomodulin on phospholipase A2 or to precipitate the radioactive lipomodulin. The IgM fraction of patients' sera could precipitate [35S]methionine-labeled lipomodulin (40,000 daltons) which comigrated with highly purified lipomodulin on gel electrophoresis with sodium dodecyl sulfate. All of these observations suggest that the sera of many patients with rheumatic diseases contain autoantibody against lipomodulin. A monoclonal antibody against lipomodulin was also obtained. Stimulating human fibroblasts with bradykinin in the presence of monoclonal antilipomodulin antibody markedly enhanced arachidonic acid release due to the activation of phospholipase(s) in the intact cells, and this stimulatory effect was blocked by adding purified lipomodulin. These findings suggest that lipomodulin regulates the activity of phospholipase(s) on the cell surface and that autoantibodies against lipomodulin may play a role in certain symptoms of rheumatic diseases, especially by the formation of prostaglandins and other metabolites of arachidonic acid.
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PMID:Presence of autoantibody for phospholipase inhibitory protein, lipomodulin, in patients with rheumatic diseases. 611 91

A nuclear antigen associated with cell proliferation (proliferating cell nuclear antigen [PCNA]) and blast transformation is recognized by autoantibodies in the sera of some patients with systemic lupus erythematosus. Using this autoantibody as a reagent, PCNA was purified 120-fold by ammonium sulfate fractionation, DEAE chromatography, and Sephadex G200 gel filtration. The antigenicity of PCNA was sensitive to trypsin but resistant to ribonuclease and deoxyribonuclease, suggesting that the antigenic determinant resided in protein and not nucleic acids. PCNA was inactivated at 56 degrees C for 30 min. Isoelectrophoretic focusing showed that the pI was 4.8. Analysis of immunoprecipitates on polyacrylamide gels showed the presence of IgG heavy and light chains and a single polypeptide band of 33,000 mol wt. This polypeptide band was the reactive antigen in immunoblotting (Western transfer) assays.
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PMID:Characterization of proliferating cell nuclear antigen recognized by autoantibodies in lupus sera. 614 19

A low molecular weight DNA fragment was isolated from DNA/anti-DNA antibody immune complexes found in patients with active systemic lupus erythematosus (SLE). Total sera were treated with 40% saturated ammonium sulfate to isolate gamma-globulin fraction and phenolized to partition proteins and nucleic acids. After being treated with RNAase, the sample was labeled at the 5' end with 32P-phosphate and electrophoresed in an 8% polyacrylamide gel, which was dried and autoradiographed. The sample that migrated at positions of molecular weight between 20,000 and 28,000 was susceptible to DNAase I but resistant to S1-nuclease. The data suggest that the immune complexes of SLE patients contain double-stranded DNA with 30 to 40 base pairs.
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PMID:Isolation of DNA from DNA/anti-DNA antibody immune complexes in systemic lupus erythematosus. 616 Nov 79

Sera from majority of patients with seropositive rheumatoid arthritis, which generally lacked detectable anti-double stranded DNA in Farr, Crithidia luciliae, and microcomplement fixation assays, exhibited high levels of dsDNA binding in the presence of 3.5% polyethylene glycol when using intrinsically labeled 3H-PM2 DNA as antigen. Except for SLE, such increased dsDNA binding was absent in normal and a variety of other disease sera, including those from patients with seronegative rheumatoid arthritis. In contrast to the situation in SLE, in which dsDNA binding is mediated by specific anti-DNA antibody, the increased dsDNA binding activity in seropositive rheumatoid arthritis was shown to be dependent upon complex low avidity interactions involving DNA, IgG, IgM rheumatoid factor, and low density lipoproteins. Analysis of the composition of the polyethylene glycol serum precipitates by 2-dimensional gel diffusion, immunoelectrophoresis, and sodium dodecyl sulfate polyacrylamide gel electrophoresis failed to reveal the presence of additional DNA-binding proteins unique to seropositive rheumatoid arthritis. The only feature distinguishing high DNA binding sera from those with low DNA binding activity was an increased amount of polyethylene glycol-insoluble IgG in the former, presumably reflecting IgG/IgG and/or IgG/IgM complexes. The significance of these unusual DNA/low density lipoprotein/IgG/rheumatoid factor complexes with respect to the diagnostic specificity and pathophysiology of the DNA/anti-DNA system is discussed.
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PMID:Nature of double-stranded DNA binding activity in seropositive rheumatoid arthritis: formation of low avidity DNA/rheumatoid factor/IgG/low density lipoprotein complexes. 616 94

A new method for differentiation of specific DNA-binding by human sera from non-specific binding was evaluated with sera from patients with systemic lupus erythematosus in different stages of the disease. An addition of dextran sulfate or calcium chloride to Farr's radioimmunoassay mixture reduced non-specific binding of thermally denatured [3H]DNA of the patient sera without much effect on the specific binding. The measurement of DNA-binding value by the sera in these addition systems provides accurate information with regard to the pathophysiological state of the disease.
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PMID:Differentiation of specific DNA binding activity of SLE sera from non-specific binding by an addition of dextran sulfate and calcium chloride to the Farr assay system. 617 85

Purified serum antibodies of patients suffering from mixed connective tissue disease were tested for their immunological specificity against nuclear constituents of HeLa S3 cells. In the indirect immunofluorescent staining technique, using cells and nuclei as targets, a typical speckled intranuclear staining pattern was obtained, that persisted after degradation and extraction of all nucleic acids and their associated proteins. This treatment of nuclei with detergents, DNase, RNase and high salt concentrations leave intact only the so-called nuclear matrix which is an intranuclear proteinaceous network. Further proof that nuclear matrix proteins were targets of the autoimmune reaction was obtained after separation of these proteins by sodium dodecyl sulfate polyacrylamide gel electrophoresis and electrophoretic transfer to nitrocellulose (blotting). A specific number of blot-transferred matrix proteins reacted with purified serum antibodies of 10 patients with mixed connective tissue disease, whereas this reaction was negative with normal healthy individuals. IgG preparations of 7 patients with systemic lupus erythematosus showed a weak, if any, reaction with matrix constituents. Obviously, in some connective tissue diseases serum antibodies are expressed which are directed to specific nuclear matrix antigens.
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PMID:Anti-nuclear matrix antibodies in mixed connective tissue disease. 618 28

Plasma androgen levels were determined by radio-immunoassay in 19 female patients (aged 14 to 42 years) with systemic lupus erythematosus (SLE). In 11 patients studied in the active phase of the disease, prior to any corticosteroid therapy, mean (+/- SEM) plasma concentrations (ng/ml) of the following androgens were significantly reduced as compared with controls (12 normal women aged 19-37 years): testosterone (0.119 +/- 0.021 vs 0.330 +/- 0.034, p less than 0.001), dihydrotestosterone (0.078 +/- 0.013 vs 0.150 +/- 0.014, p less than 0.01), dehydroepiandrosterone (1.60 +/- 0.16 vs 4.30 +/- 0.50, p less than 0.001), dehydroepiandrosterone sulfate (480 +/- 102 vs 1020 +/- 92, p less than 0.001), and androstenedione (0.69 +/- 0.22 vs 1.45 +/- 0.18, p less than 0.02). In 8 patients studied while in post-therapeutic remission, six months to seven years after corticosteroid withdrawal, plasma concentrations of the same androgens (except androstenedione) were also significantly reduced as compared with controls, although to a lesser degree. In neither of the two patient groups were cortisol and estradiol levels significantly different from controls. Our results suggest that low plasma androgen levels could be a permanent disorder in female SLE patients, at least in severe forms of the disease.
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PMID:[Plasma androgens in women with disseminated lupus erythematosus]. 622 Feb 98

Lipomodulin, purified to near homogeneity from rabbit peritoneal neutrophils, was phosphorylated by cyclic AMP-dependent protein kinase from bovine heart with concomitant loss of its ability to inhibit phospholipase A2 from porcine pancreas. Phosphorylation of lipomodulin was confirmed by the incorporation of 32P from [gamma-32P]ATP. To demonstrate that lipomodulin undergoes phosphorylation in vivo, rabbit peritoneal neutrophils were incubated with 32P and lipomoculin was isolated by immunoprecipitation with serum from a patient with systemic lupus erythematosus which has anti-lipomodulin antibody. Analysis of 32P-labeled immunoprecipitates by sodium dodecyl sulfate electrophoresis revealed a single peak of radioactivity that comigrated with [35S]methionine-labeled lipomodulin. The administration of a chemoattractant, N-formyl-methionyl-leucyl-phenylalanine to intact rabbit neutrophils, resulted in a marked increase in arachidonate release from the cells and an increase in 32P incorporation into lipomodulin. A close correlation was found between the extent of phosphorylation of lipomodulin and the rate of arachidonate release. Phosphorylation of lipomodulin in neutrophils gradually returned to the control level with corresponding cessation of arachidonate release. In contrast to the in vitro system, phosphorylation of lipomodulin and release of arachidonic acid from peptide-stimulated neutrophils required Ca2+ entry into the cells. These results suggest that the phosphorylation-dephosphorylation of lipomodulin, phospholipase inhibitory protein, is an important mechanism for chemotactic receptor-mediated regulation of arachidonic acid release in rabbit neutrophils.
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PMID:The regulation of lipomodulin, a phospholipase inhibitory protein, in rabbit neutrophils by phosphorylation. 626 23


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