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 DNA strategy was designed to characterize the antigenic site(s) within a lambda gt11 cloned 35-amino-acid antigenic peptide, identified with antibodies from patients with chronic Chagas' heart disease (cChHD) and systemic lupus erythematosus (SLE) as the C-terminal portion of a Trypanosoma cruzi P ribosomal protein. The 198-bp cDNA insert was digested with AluI, resulting in two DNA segments that were recloned in lambda gt11. To identify specific antigenic determinants, the recombinant phage and the purified recombinant antigens were probed with sera from clinically characterized subjects. Chronic ChHD and SLE sera defined a linear epitope common to both diseases within the 15 C-terminal residues of the parasite P ribosomal protein. It is also shown that the cloned 35-amino-acid peptide contained an antigenic site unique to cChHD.
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PMID:The cloned C-terminal region of a Trypanosoma cruzi P ribosomal protein harbors two antigenic determinants. 169 12

Antibodies to ribosomal protein components were examined in sera from 89 patients with active systemic lupus erythematosus (SLE). The anti-P, anti-S10 and anti-L12 antibodies were detected in 37, 28 and 2 patients, respectively. They were not detected in patients with various autoimmune diseases other than SLE or in healthy donors, which indicates that antiribosomal protein antibodies in sera are specific for patients with SLE. These antibodies are prevalent in patients with SLE and should provide good markers for the diagnosis of this disease.
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PMID:Autoantibodies against ribosomal proteins found with high frequency in patients with systemic lupus erythematosus with active disease. 178 88

As autoantibodies are thought to participate in the pathogenesis of renal inflammation in systemic lupus erythematosis (SLE) we investigated associations between serological markers of disease activity in SLE and the activity of renal histopathological lesions in thirty-five patients with lupus nephritis (LN). We found the following prevalence of serum auto-antibodies in LN: IgG antinuclear antibodies (ANA) 100%, IgM ANA 69%, IgA ANA 60%, IgG anti-dsDNA 60%, IgM anti-dsDNA 71%, IgA anti-dsDNA 60%, anti-RNP 20%, anti-Sm 14%, anti-SSA 31%, anti-SSB 14%, anti-histone 37%, anti-cardiolipin 80% and antibody to ribosomal protein (anti-P) 6%. No correlation was found between serological parameters and the WHO-classification of biopsies. The activity-index of histological lesion, assessed according to the NIH-renal histology scoring system, correlated with IgM ANA and IgM anti-dsDNA titers. Of all the specific features of histological renal inflammation, glomerular proliferation showed the best overall correlation with serological parameters of disease activity. Anticardiolipin antibodies were correlated with overall disease activity, but not with renal histological activity. Thus, serological markers of disease activity did not adequately reflect the amount of renal inflammation in LN and cannot replace renal biopsy as a diagnostic tool.
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PMID:Relation between serological data at the time of biopsy and renal histology in lupus nephritis. 194 73

In two siblings with systemic lupus erythematosus (SLE), who experienced two episodes of psychosis each, a longitudinal study of autoantibodies, including antibodies to ribosomal P proteins, is described. In two of three evaluable periods of 15 weeks antedating psychosis a rise followed by a spontaneous drop in anti-P levels was recorded. In the third period antibodies to ribosomal protein P were absent. It is concluded that results with single samples are not informative, and that frequent measurement of antibodies to ribosomal protein P in patients with SLE may have limited predictive value for psychosis.
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PMID:A prospective study on antiribosomal P proteins in two cases of familial lupus and recurrent psychosis. 224 Dec 67

New antibodies reactive with a 20 KDal ribosomal protein of the large subunit were found in sera from two of eighty patients with systemic lupus erythematosus. This antigenic protein was identified as L12 by the mobility in two-dimensional gel electrophoresis. Both sera also contained anti-P activity against three acidic phosphoproteins (P proteins), but this activity was completely inhibited by preincubation with the isolated P proteins. Therefore, these anti-L12 can be useful for studying the function of L12 in protein synthesis.
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PMID:Autoantibodies specific for the 20-KDal ribosomal large subunit protein L12. 224 50

All nine SLE (systemic lupus erythematosus) sera with antiribosomal antibody activity targeted the same three ribosomal protein antigens, of molecular masses 38 and 17/19 kD when analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blotting. One serum reacted with an additional protein of approximately kD. Ribosomal subunit fractionation by composite gel electrophoresis and sucrose density ultracentrifugation showed that these proteins were part of the large subunit. Isoelectric focusing in agarose, and two-dimensional polyacrylamide gel electrophoresis revealed that the antigens had pI between 4.5 and 6.5, but that the 17/19 kD antigens were more acidic than the 38 kD antigen. Similarities in the molecular masses, charges, as well as the presence of highly conserved crossreactive epitopes, failure to bind to carboxymethylcellulose at pH 4.2, and extractability of the 17/19 kD proteins by 400 mM NH4Cl-ethanol at 0 degrees C indicated that these antigens were analogous to the proteins P0 (38 kD) and P1/P2 (17/19 kD) described previously (25, 36). Co-identity was confirmed using reference antibodies and antigen. Although antibodies to these proteins were only found in 5-10% of more than 50 sera screened by radioimmunoassay or Western blotting, the selective production of antibodies to epitopes on three (out of a total of more than 80) ribosomal proteins may provide further clues to autoantibody induction of SLE.
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PMID:Lupus autoantibodies target ribosomal P proteins. 241 May 26

Autoantibodies directed against a ribosomal small subunit protein of 20,000 molecular weight were found in sera from 5 of 44 patients with systemic lupus erythematosus (11%) and 5 of 48 MRL/lpr mice (10%). This ribosomal protein was identified as S10 on the basis of two-dimensional gel electrophoresis and immunoblotting, as well as immunoblots of the purified S10 protein. The S10 protein antigen was readily extracted from ribosomes at low salt (300 mM KCl) and low magnesium (0.5 mM) concentrations, consistent with the highly exposed location proposed for this protein on the 40S subunit. Anti-S10 antibodies were observed significantly more frequently in lupus sera containing both anti-Sm and antiribosomal P protein antibodies and in MRL/lpr sera with anti-Sm activity, suggesting a linked pattern of autoantibody response. Together with anti-Sm and antiribosomal P protein antibodies, anti-S10 represents a third autoantibody highly specific for lupus in humans and MLR/lpr mice.
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PMID:Antiribosomal S10 antibodies in humans and MRL/lpr mice with systemic lupus erythematosus. 247 35

To identify Trypanosoma cruzi target antigens in overt Chagas' heart disease, a parasite lambda gt11 cDNA library was screened with the serum of a patient with a severe chagasic heart involvement (JL). Using a phage dot array immunoassay, 5 highly antigenic clones, JL1, JL5, JL7, JL8, and JL9, were probed with sera from clinically characterized T. cruzi infected subjects. The correlation of cloned T. cruzi antigen recognition with the clinical status of the subjects led to the identification of a recombinant antigen, JL5, that reacted predominantly with sera from patients with Chagas' heart disease. The antigenic determinant of the JL5 recombinant was a small 35 amino acid peptide. The nucleotide and the deduced amino acid sequence, together with other experimental data, allowed identification as the C-terminal portion of a T. cruzi P ribosomal protein. The C-terminal undecapeptide in JL5, EDDDMGFGLFD, was highly homologous to the same region of the human P protein SD(D/E)DMGFGLFD. The latter sequence has been identified as the P protein epitope in systemic lupus erythematosus (SLE). Positive SLE sera reacted with the JL5 recombinant phage, suggesting that the T. cruzi P protein might induce antibodies with a similar specificity to that of P antibodies in SLE.
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PMID:Identification of major Trypanosoma cruzi antigenic determinants in chronic Chagas' heart disease. 247 75

Autoantibody to Sm Ag is a highly specific marker for the diagnosis of SLE. The Sm Ag exists in the cell nucleus as part of a ribonucleoprotein complex containing five small nuclear RNA. The major immunoreactive Sm species have been reported to be three polypeptides of m.w. 28,000/29,000 (B/B') and 16,000 (D). We report here that a m.w. 21,000 peptide is another major target of anti-Sm antibody. This peptide was originally identified by Western blotting as an acidic ribosomal protein (RP21) reactive with IgG from some SLE patients. Anti-RP21 is distinct from anti-ribosomal P protein antibody (anti-P) which has been previously identified as a lupus-specific autoantibody. Cell fractionation experiments showed that RP21 existed only in the ribosomal fraction and was never detected in other cellular compartments including nuclei. However, when nuclear extracts were used as Ag sources in immunoblotting, affinity-purified anti-RP21 was found to react with m.w. 28,000 and 16,000 peptides, suggesting that anti-RP21 reactivity might be due to the cross-reaction of anti-Sm. This was further confirmed by the evidence that two kinds of murine anti-Sm mAb independently derived from MRL/lpr mouse recognized RP21. These results indicate that anti-Sm antibodies in SLE are reactive with both nuclear and ribosomal ribonucleoproteins. Previous reports have described certain similarities, i.e., antibody subclass restriction and incidence, of anti-Sm and anti-P in both humans and autoimmune mice. Our present study demonstrated a close physical association of target molecules reactive with anti-Sm and anti-P, and might, therefore, provide some clue to the origin of these two types of lupus-specific autoantibodies.
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PMID:Identification of an acidic ribosomal protein reactive with anti-Sm autoantibody. 277 17

Sera from systemic lupus erythematosus (SLE) patients giving a fluorescent ribosomal pattern on tissue and cell preparations also showed precipitating autoantibodies against purified rat liver ribosomes. Ribosomal antigen is also present in rabbit thymus cellular extract (RTE), since the same sera gave precipitin lines against RTE in identity with ribosomes. Immunofluorescent staining was completely inhibited by serum absorption with ribosomes or with RTE. However ribosomal RNA and RNase or trypsin-treated ribosomes failed to react with these autoantibodies as demonstrated in immunoabsorption and immunodiffusion studies. These data suggest that these sera contain autoantibodies directed against some antigenic site composed of a portion of both RNA and ribosomal protein. Ribosomal autoantibodies were detectable at a low frequency in SLE patients characterized by an active disease and renal involvement.
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PMID:Anti-ribosomal ribonucleoprotein autoantibodies in systemic lupus erythematosus. 642 70


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