Tissue transglutaminase ELISA positivity in autoimmune disease independent of gluten-sensitive disease

Sárdy, Miklós; Csikós, Márta; Geisen, Christof; Preisz, Klaudia; Kornseé, Zoltán; Tomsits, Erika; Töx, Ulrich; Hunzelmann, Nicolas; Wieslander, Jörgen; Kárpáti, Sarolta; Paulsson, Mats; Smyth, Neil

doi:10.1016/j.cca.2006.08.006

Cited by 33 publications

(27 citation statements)

References 29 publications

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“…This serological protocol gives very good results, but there are some problems linked to the finding of false positives for anti-tTG [4] and to the reproducibility of EmA [22]. Indeed, false positives for anti-tTG have been described as ranging from 3 to 12%, mainly in the presence of very low ELISA activities (lower than two times the cutoff) in patients with inflammatory bowel disease, food allergy, irritable bowel syndrome, giardiasis, and other intestinal infections, and in autoimmune disorders [23][24][25]. The problem of these false positives cannot be solved by EmA, because the reliability of EmA testing is outstanding only in a few laboratories skilled in immunofluorescent assays [6,22].…”

Section: Discussionmentioning

confidence: 92%

Usefulness of Antibodies to Deamidated Gliadin Peptides in Celiac Disease Diagnosis and Follow-up

et al. 2007

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The prevalence of the recently described deamidated gliadin peptide antibodies was compared with that of the routinely used antigliadin, antiendomysial, and tissue transglutaminase antibodies in the sera of 128 untreated celiac patients and 134 controls. Sensitivity and specificity for celiac disease were 83.6 and 90.3% for IgA and 84.4 and 98.5% for IgG antibodies to deamidated gliadin peptides. The new test displayed higher diagnostic accuracy than antigliadin antibodies and, although less sensitive than antiendomysial and tissue transglutaminase antibodies, showed significantly higher specificity than tissue transglutaminase antibodies (P < 0.001). Persistence of peptide antibodies after gluten withdrawal was an expression of low compliance with the diet and of the lack of improvement of the intestinal mucosa. The combined use of tissue transglutaminase and deamidated gliadin peptide antibodies seems to be a very useful tool for celiac disease diagnosis. Moreover, antibodies to deamidated gliadin peptides can be helpful in disease follow-up.

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Section: Discussionmentioning

confidence: 92%

Usefulness of Antibodies to Deamidated Gliadin Peptides in Celiac Disease Diagnosis and Follow-up

et al. 2007

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“…A test that combines measurement of antibody binding to wild-type TG2 and to one with modified celiac epitope could distinguish in future between celiac-type and nonspecific anti-TG2 antibodies seen in other autoimmune diseases, tumors, or tissue injury (29).…”

Section: Discussionmentioning

confidence: 99%

A single conformational transglutaminase 2 epitope contributed by three domains is critical for celiac antibody binding and effects

Simon-Vecsei

Király

Bagossi

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

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The multifunctional, protein cross-linking transglutaminase 2 (TG2) is the main autoantigen in celiac disease, an autoimmune disorder with defined etiology. Glutamine-rich gliadin peptides from ingested cereals, after their deamidation by TG2, induce T-lymphocyte activation accompanied by autoantibody production against TG2 in 1-2% of the population. The pathogenic role and exact binding properties of these antibodies to TG2 are still unclear. Here we show that antibodies from different celiac patients target the same conformational TG2 epitope formed by spatially close amino acids of adjacent domains. Glu153 and 154 on the first alpha-helix of the core domain and Arg19 on first alpha-helix of the N-terminal domain determine the celiac epitope that is accessible both in the closed and open conformation of TG2 and dependent on the relative position of these helices. Met659 on the C-terminal domain also can cooperate in antibody binding. This composite epitope is diseasespecific, recognized by antibodies derived from celiac tissues and associated with biological effects when passively transferred from celiac mothers into their newborns. These findings suggest that celiac antibodies are produced in a surface-specific way for which certain homology of the central glutamic acid residues of the TG2 epitope with deamidated gliadin peptides could be a structural basis. Monoclonal mouse antibodies with partially overlapping epitope specificity released celiac antibodies from patient tissues and antagonized their harmful effects in cell culture experiments. Such antibodies or similar specific competitors will be useful in further functional studies and in exploring whether interference with celiac antibody actions leads to therapeutic benefits.conformational epitope | endomysial antibodies | immunotherapy

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“…There are reports in rheumatoid arthritis describing patients positive for IgA-TTG and negative for IgA-EMA [33] or IgG-TTG [34]. Also, IgA-and/or IgG-TTG have been reported in systemic lupus erythematosus [32,35], granulomatosis with polyangiitis [36], ankylosing spondylitis (IgA and IgG) and psoriatic arthritis (IgA and IgG) [37]. Differences observed between epitope specificity and the IgA-or IgG-TTG isotype observed may derive from the different mechanisms acting on the enzyme during the process that leads to autoimmunity…”

Section: Autoimmunitymentioning

confidence: 99%

IgA and IgG Antitransglutaminase 2 Antibodies in the Diagnosis of Celiac Disease

Villanueva¹,

Rojas²,

Araya³

2017

IJCD

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Screening for celiac disease (CD) dramatically improved when techniques able to measure blood autoantibodies against tissue transglutaminase 2 (TTG) were developed. Although typically increased in CD, these antibodies are not pathognomonic since they are also detected in several other autoimmune processes. IgA deficiency among celiac patients is more frequent than in general population (up to 25% vs 1-3%). This led to develop kits able to measure IgG-TTG, which until today represent a helpful diagnostic tool during diagnosis of CD in IgA deficient individuals. Today, commercial kits measuring IgG-TTG (and other) antibodies are widely available, are frequently used and create confusion in diagnosing CD in IgA-sufficient individuals. This is attributed to the fact that sensitivity and specificity of IgG-TTG is lower when applied to IgA-sufficient persons, and also because IgG-TTG is detected in several autoimmune disorders, with variable frequency and isotypes depending on the condition. Evidence analyzed indicate that to date available data: i) is insufficient to understand the difference of classes and subclasses detected in CD and other autoimmune conditions; ii) does not support the use of IgG-TTG for diagnosing CD in IgA-sufficient individuals and therefore iii) IgG should not be used in the routine diagnostic process of CD.

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Tissue transglutaminase ELISA positivity in autoimmune disease independent of gluten-sensitive disease

Cited by 33 publications

References 29 publications

Usefulness of Antibodies to Deamidated Gliadin Peptides in Celiac Disease Diagnosis and Follow-up

Usefulness of Antibodies to Deamidated Gliadin Peptides in Celiac Disease Diagnosis and Follow-up

A single conformational transglutaminase 2 epitope contributed by three domains is critical for celiac antibody binding and effects

IgA and IgG Antitransglutaminase 2 Antibodies in the Diagnosis of Celiac Disease

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