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)

The role of nutrition in modulating autoantibody expression in murine lupus has become well documented. One such nutritional factor, zinc deficiency, has received significant attention because of the well-known effects of zinc on the immune function of genetically normal animals. Moreover zinc-deficient diets retard autoantibody production in NZB, NZB/W, and MRL/1 mice; such deprivation also enhances survival in all three strains. Because zinc nutriture influences vitamin A metabolism, it has been postulated that the immunologic effects of zinc deficiency are mediated in part by the reduction of vitamin A levels seen in zinc deprivation. To explore this possibility we studied the influence of vitamin A deficiency, in zinc well-nourished mice, on autoantibody production in NZB mice. Groups of NZB mice, beginning at 6 mo of age, were fed a vitamin A-deficient diet or a control diet ad libitum or pair-fed to the deficient group. The diet contained casein as the protein source and contained adequate levels of trace elements and vitamins. Despite our hypothesis that the reduction of autoantibodies in zinc-deficient NZB mice might be mediated by secondary vitamin A deficiency, we found that vitamin A-deficient animals manifested more severe hypergammaglobulinemia and an earlier onset of both NTA and IgM anti-erythrocyte autoantibodies than did vitamin A-sufficient mice. These results illustrate the importance of rigorous studies of select nutritional parameters and warn of the possibility of clinical harm in feeding inappropriate diets to patients with systemic lupus erythematosis.
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PMID:Nutritional factors and autoimmunity. IV. Dietary vitamin A deprivation induces a selective increase in IgM autoantibodies and hypergammaglobulinemia in New Zealand Black mice. 660 78

Antibodies to DNA define an important autospecificity that arises in systemic lupus erythematosus (SLE). To elucidate the molecular features that may explain the pathogenesis of SLE, a heterologous system for expression of cloned V genes is often desirable. Here, a single-chain Fv coding domain was constructed by using the heavy- and light-chain V genes of a high-affinity site-directed mutant of the murine anti-dsDNA autoantibody, 3H9. This scFv was joined in frame to the c-jun leucine zipper for dimerization, and to two affinity tags, domain B of the staphylococcal protein A and a pentahistidine peptide, for purification. Dimerization of the scFv was determined by size-exclusion chromatography. The yields of the scFv following affinity purification on IgG agarose or Ni-NTA agarose were compared, and the activities of the resulting protein fractions were determined. A two-step purification of periplasmic extracts on Ni-NTA agarose and IgG agarose, followed by elution with 3.5 M MgCl(2), yielded scFv with the highest specific activity. The final purified material bound DNA by ELISA, electrophoretic mobility shift assay, and immunofluorescence of fixed Hep-2 cells. Antibodies purified in this fashion should have applications in structure/function studies in which it is essential to generate highly purified antigen-combining sites.
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PMID:Tandem affinity tags for the purification of bivalent anti-DNA single-chain Fv expressed in Escherichia coli. 1054 78

Using recombinant TpNs proteins of Treponema pallidum as antigens, ELISAs are proved to be of higher sensitivity and specificity. However, they can be further increased by using multiple TpNs antigens. According to the epitope analysis, we firstly used linking primers PCRs to obtain an artificial fusion gene segment tpE17-47 containing epitopes of both TpN17 and TpN47. Subsequently, we conducted the prokaryotic expression systems of entire tpN17 and tpN47 genes and tpE17-47 fusion gene. SDS-PAGE analysis and BioRad Gel Image Analysis System showed that the recombinant proteins rTpN17, rTpN47 and rTpE17-47 expressed stably, with 36%, 20% and 28% yields of total bacterial protein, respectively. After purified by Ni-NTA affinity chromatography, all the three recombinant proteins could be recognized by T. pallidum antibody positive sera from syphilis patients. The positive rate of rTpE17-47-ELISA for detecting serum specimens in clinically 630 cases with syphilis was 98.6%. This rate was slightly higher than that by Treponema pallidum particle agglutination (TPPA) (97.9%) (P > 0.05), but significantly higher than those by rTpN17-ELISA (83.8%), rTpN47-ELISA (83.3%) and rapid plasma reagin (RPR) (72.1%) (P < 0.01). Furthermore, both ELISAs and TPPA for detecting the serum specimens in 25 cases with SLE, 36 cases with RA and 250 healthy cases were all negative. RPR showed positive in 1 case with SLE, 2 cases with RA and 2 healthy cases. This could be a novel serological screening or diagnostic method of syphilis with advantages of quickness, convenience, safety, sensitivity and specificity.
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PMID:[Recombinant expression of the fusion antigen based on Treponema pallidum TpN17 and TpN47 epitope peptides and establishment and application of the associated ELISA]. 1993 56