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

The HEp2 cell cultures appeared highly sensitive in detecting the antinuclear antibodies (ANAb) in systemic sclerosis, principally anticentromere antibodies of the CREST syndrome. The immunoblotting used with either complex cellular extracts from HeLa and rabbit thymus or purified nuclear components (high mobility group (HMG) proteins and histones) is able to identify precisely the ANAb targets and to contribute to diagnosis. With nuclear extracts of HeLa cells, the sera from 75.8% of CREST syndrome subjects stained 18 and 22 kD proteins. Corresponding antibodies were also detected in 72.7% of these patients, on HEp2 centromers by indirect immunofluorescence. With the same extracts, 33.3% of sera from diffuse sclerosis/acrosclerosis patients contain antibodies staining 86, 73, 32 and 30kD. These sera also stain 77, 66 and 63kD from thymus extracts. Corresponding antibodies will be the anti-SCL-70 antibodies defined by double immunodiffusion. The anti-HMG antibodies were infrequent in systemic sclerosis, rheumatoid arthritis (RA) and systemic lupus erythematosus (SLE) and consequently without interest for diagnosis. The anti-whole histones antibodies which are less frequent in diffuse sclerosis/acrosclerosis (35.7%) than in SLE (41.3%) recognize especially H1 and H2A in the first diseases, H1 and H2B in SLE and H1 and H3 in RA.
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PMID:Antinuclear antibodies detected by indirect immunofluorescence on HEp2 cells and by immunoblotting in patients with systemic sclerosis. 249

Patients of some rheumatic autoimmune diseases like systemic lupus erythematosus have in their sera autoantibodies to vimentin, the main protein of intermediate sized filaments of the cytoskeleton of connective tissue cells. Immunoprecipitation and Western blotting techniques have been used to detect the interaction between human anti-vimentin autoantibodies and the two peptides that resulted from the cleavage of vimentin by N-chlorosuccinimide. Both methods and also immunoabsorption of sera with the isolated peptides suggest that the interaction of vimentin and immunoglobulins is mainly carried out through a peptide of 30kD mol. wt located close to the amino-terminal part of the vimentin molecule. The same results were obtained when a serum from a rabbit immunized with human vimentin was used.
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PMID:Human vimentin autoantibodies preferentially interact with a peptide of 30kD mol. wt, located close to the amino-terminal of the molecule. 389 28