Evidence map›Paper›PMID 9486109›Full record

ArticleImmunology1997

Autoantibodies to evolutionarily conserved epitopes of enolase in a patient with discoid lupus erythematosus.

V M Gitlits, J W Sentry, M L Matthew, A I Smith, B H Toh

Abstract read
In one paragraph

Article in Immunology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

6 citing papers in PubMed.

  1. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

V M GitlitsDepartment of Pathology and Immunology, Monash Medical School, Prahran, Victoria, Australia.
J W Sentry
M L Matthew
A I Smith
B H Toh

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although the pathology of discoid lupus erythematosus is well documented the causative agents are not known. Here, we report the identity of the target antigen of an autoantibody present in high titre in the serum of a patient with discoid lupus erythematosus. We have demonstrated that the antigen is enolase; first, because it has properties consistent with this glycolytic enzyme (47,000 MW, cytosolic localization and ubiquitous tissue distribution). Secondly, limited amino acid sequence determination after trypsin digestion shows identity with alpha-enolase. Finally, the autoimmune serum immunoblots rabbit and yeast enolase and predominantly one isoelectric form of enolase (PI approximately 6.1). These results indicate that the reactive autoepitopes are highly conserved from man to yeast. The results also suggest that the autoantibodies are most reactive to the alpha-isoform of enolase, although it is possible that they may also be reactive with gamma-enolase, and have least reactivity to beta-enolase. The anti-enolase autoantibodies belong to the immunoglobulin G1 (IgG1) isotype. This is the first report of IgG1 autoantibodies to evolutionarily conserved autoepitopes of enolase in the serum of a patient with discoid lupus erythematosus. Previous reports of autoantibodies to enolase have suggested associations with autoimmune polyglandular syndrome type I and cancer-associated retinopathy. This report and an earlier report of what is likely to be enolase autoantibodies in two patients without systemic disease suggest that enolase autoantibodies have a broad association and are not restricted to any particular disease.

Indexed as

AgedAged, 80 and overAmino Acid SequenceAnimalsAutoantibodiesElectrophoresis, Polyacrylamide GelEpitopesEvolution, MolecularFemaleHumansImmunoblottingLupus Erythematosus, DiscoidPhosphopyruvate HydrataseRatsRats, Sprague-DawleySpecies SpecificityAutoantibodiesEpitopesPhosphopyruvate Hydratase

Identifiers

PMID9486109
PMCPMC1363797

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.