Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0268596 (EMA)
 2,520 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Systemic lupus erythematosus (SLE) and coeliac disease (CD) are diseases of an autoimmune origin that share the human leukocyte HLA-B8 and HLA-DR3 histocompatibility antigens, yet the co-association of CD with SLE is mainly based on case reports. Thus, the real prevalence of CD in SLE is unclear. The aim of this study was to determine the prevalence of antitissue transglutaminase (anti-tTG) in SLE and the relation between SLE and CD. In this case-control study, 100 patients with SLE, and 120 healthy subjects were studied. Sera from all participants were analysed for the presence of IgA and IgG anti-tTG antibodies using a human recombinant tissue transglutaminase (tTG) immuno-enzymatic assay. Anti-tTG positive patients and controls were further tested for antiendomysial (EMA) antibodies by an indirect immunofluorescence and HLA typing (DQalpha1*0501-DQbeta1*0201 allele determination). Subjects who had EMA or the mentioned allele, underwent duodenal biopsy to confirm a possible diagnosis of CD. Anti-tTG antibodies (IgA or IgG isotypes) were found in three of the 100 SLE patients (overall prevalence of 3%): one had the IgA and two the IgG isotypes. Only 1 of 120 healthy subjects (0.8%) had a low positive reaction for IgA anti-tTG. Only the IgA anti-tTG positive SLE patient was diagnosed as having CD based on a positive IgA-EMA and small bowel biopsy findings. The two IgG anti-tTG positive SLE patients and the IgA anti-tTG positive healthy subject were classified as false positives (EMA negative and HLA DQalpha1*0501-DQbeta1*0201 allele negative). In conclusion, anti-tTG antibodies were found at a low rate in SLE patients and mostly did not indicate the presence of CD. Thus, serological screening for CD is not recommended in SLE, unless a clinical suspicion of CD is present.
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PMID:IgA and IgG tissue transglutaminase antibodies in systemic lupus erythematosus. 1517 59

To investigate the detectability and expressiveness of salivary and fecal anti-gliadin (AGA), anti-endomysium (EMA) and anti-tissue-transglutaminase (ATA) antibodies, 127 salivary and 160 fecal samples of healthy volunteers and salivary and fecal samples of 17 patients with histologically proven and 9 patients with suggested celiac disease were investigated in this study. With all salivary parameters and fecal IgA AGA, IgM AGA, IgA EMA and IgG EMA, healthy volunteers and patients showed partially overlapping results. The most promising results in our study with higher concentrations in patients with celiac disease were obtained by fecal scIgA AGA and a combined determination of fecal IgA AGA, IgG AGA and IgM AGA. Further investigations should be performed with fecal IgA EMA and scIgA ATA based on human recombinant tissue-transglutaminase. One patient with histologically proven celiac disease had normal serological but high fecal scIgA AGA and scIgA ATA values. This patient emphasizes the importance of fecal antibody determination for the diagnosis of celiac disease, at least in patients with suggested celiac disease and negative serum antibodies.
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PMID:Comparison of different salivary and fecal antibodies for the diagnosis of celiac disease. 1548 30

A number of serologic tests are available commercially for identifying individuals who require an intestinal biopsy examination to diagnose celiac disease (CD). The aim of this study was to determine which test, or combination of tests, was most sensitive and specific for this purpose. We performed a literature review of studies that determined the sensitivity and specificity of serologic tests for CD. Studies that compared biopsy examination-confirmed cases of CD with controls with normal intestinal histology were selected for analysis. Sensitivities and specificities for the antigliadin tests were highly variable. Immunoglobulin (Ig)G-based antigliadin (AGA) tests generally were poor in both parameters whereas the IgA-based test was poorly sensitive but more specific. The IgA endomysium (EMA-IgA) and tissue transglutaminase (TTG-IgA) tests were both highly sensitive and specific with values for both parameters exceeding 95% in most studies. There were no identifiable differences between adults and children with respect to these tests. There was no evidence that a combination of tests was better than a single test using either the EMA IgA or TTG IgA. Either the EMA-IgA or TTG-IgA test is most useful for identifying individuals with CD. The variability and generally lower accuracy associated with the AGA tests make them unsuitable for screening purposes. There is no advantage to using a panel of tests as opposed to a single test. Because these data were obtained largely from studies conducted in a research setting, it is possible the tests will be less accurate when used in the clinical setting.
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PMID:What are the sensitivity and specificity of serologic tests for celiac disease? Do sensitivity and specificity vary in different populations? 1582 23

New assays for antibodies to deamidated gliadin peptides (DGP) expressing celiac disease-specific epitopes were evaluated using 154 sera previously tested for endomysial immunoglobulin A (IgA) (EMA), transglutaminase IgA (TGA), and conventional gliadin antibodies. DGP antibody results showed 97% concordance with EMA and TGA results. Of 56 sera negative for EMA and TGA but positive for conventional gliadin antibodies, 54 (96%) were negative for DGP antibodies.
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PMID:Evaluation of the INOVA diagnostics enzyme-linked immunosorbent assay kits for measuring serum immunoglobulin G (IgG) and IgA to deamidated gliadin peptides. 1642 13

One of the most reliable sero-diagnostic tests for coeliac disease (CD) is the measurement, by ELISA, of serum IgA antibodies to tissue transglutaminase (tTG) adsorbed to the wells of microtitre plates. In spite of its reliability, however, some discrepancies exist with the results obtained by the antiendomysium histological assay (EMA) and by biopsy the accepted gold standard. Among the reasons for these differences in titres between the ELISA and the last 2 mentioned assays are the conformational changes that proteins undergo on adsorption and the importance of conformational epitopes on tTG for diagnosing CD. To address this problem, a novel procedure was developed using guinea-pig tTG (gptTG) free in solution to interact with IgA antibodies in the sera of CD patients. Any immune complexes so formed are then captured by anti-tTG antibodies preadsorbed to the wells of microtitre plates. This immunocapture method was optimized for the amount of soluble gptTG needed to interact with all the IgA's anti-tTG present in fixed dilutions of serum samples, the amount of rabbit IgG anti-gptTG used to coat the wells of microtitre plates and the order of addition of the reaction components. Comparison of the IgA titres obtained by immunocapture with those by EMA and ELISA (adsorbed tTG) on 9 highly positive and 6 weakly positive sera from clinically characterized CD patients and 5 negative sera from non-CD control subjects revealed that the IgA titres by the immunocapture procedure were well correlated with those obtained by EMA, whereas the titres on ELISA showed discrepancies with both immunocapture and EMA.
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PMID:Development of an immunocapture method for measuring IgA antibodies to tissue transglutaminase in the sera of patients with coeliac disease. 1654 71

Anti endomysial and anti transglutaminase (EMA/TTG) antibodies measurements in large population groups, show that celiac disease is significantly more common than previously thought and 0.5-1% of the population suffer this condition. The recognition of atypical clinical presentations by active screening of high risk groups is a successful global initiative. In Chile there is little awareness of the enormous changes occurred in this field. Available national information on typical presentation of the disease shows that it is found in 1:1836 live births, figure that is comparable to European societies. Two urgent tasks are required in our country. First, to asses the Chilean population using EMA and/or TTG. Second, to improve the legal aspects that regulate consumer information about gluten content in processed foods. We here review the most relevant aspects to be considered to improve the management of celiac patients and the tasks that require the participation of health authorities for their implementation.
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PMID:[Improving the management of celiac disease: an urgent challenge]. 1667 11

Celiac disease is an immune mediated enteropathy initiated by ingestion of gluten, in genetically susceptible individuals. With changing epidemiology, celiac disease initially thought to affect only Europeans, has been increasingly reported from other parts of the world including India. However, its true prevalence in India is still not known, as the diagnosis is being missed. The gold standards for diagnosis have been characteristic small intestinal mucosal changes on gluten and a full clinical remission on its removal from the diet. Presence of serological antibodies, which disappear on gluten free diet further confirms the diagnosis. The understanding of the histopathology of celiac disease has changed over the years. The small bowel mucosal lesion of celiac disease is an evolutionary process with normal mucosal architecture and an increase in intraepithelial lymphocytes at one end of the spectrum and classical flat mucosa at the other. In the Indian subcontinent celiac disease has a heterogeneous histological presentation and the diagnosis may be missed if it is based only on severe mucosal changes or the serology is not considered when moderate or mild mucosal changes are present. The last two decades have shown that antiendomysical (Anti EMA) and anti tissue transglutaminase antibodies (anti-tTGA) have a sensitivity and specificity of more than 95% to diagnose celiac disease. Anti EMA tests being operator dependent are more liable to errors and anti- tTGA may be preferred for large scale screening. However, the different source of tTGA antigen, varied techniques of production and the use of arbitrary units by different commercial kits can influence the diagnostic accuracy of the anti-tTGA assay. There is a strong genetic association of celiac disease with HLA-DQ2 or DQ8. The presence of HLA-DQ2 hetrodimer in more than 97% of a group of North Indian patients with celiac disease indicates that this population has a similar genetic risk for the disease. HLA DQ2 typing can be used for ruling out celiac disease where the diagnosis is equivocal as it has a negative predictive value of greater than 95%. Given the protean clinical manifestation and the heterogeneous histology a standard algorithm for diagnosis of celiac disease is important.
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PMID:Diagnosis of celiac disease. 1693 66

Histological confirmation of infiltrative lesions via small bowel biopsy is the gold standard for diagnosing celiac disease. Four serum antibody assays may serve as a first-step diagnostic tool to identify biopsy candidates: immunoglobulin A tissue transglutaminase (IgA tTG), IgA endomysial antibody (IgA EMA), IgA antigliadin antibody (IgA AGA), and IgG antigliadin antibody (IgG AGA). IgA tTG and IgA EMA offer the best diagnostic accuracy. Patients with selective IgA deficiency may have falsely negative IgA assays (strength of recommendation [SOR]: B, based on a systematic review, multiple small cross-sectional studies, and expert opinion).
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PMID:Clinical inquiries: What blood tests help diagnose celiac disease? 1713 49

Clinical studies have estimated a 10- to 20-fold increased risk for celiac disease (CD) in patients with selective IgA deficiency (SIgAD). For this reason, screening for CD is mandatory in SIgAD patients, but it represents a special challenge since the specific IgA class antibodies against gliadin (AGA), endomysium (EMA), and tissue-transglutaminase (tTG) are not produced in patients with CD. IgG class counterparts of these antibodies may be informative; in particular IgG EMA has been demonstrated to be a valid marker for diagnosing CD in SIgAD cases, but it is not used much in clinical laboratories, because it is cumbersome and involves some technical difficulties. Even if it was widely used in clinical laboratories, the measuring of IgG AGA has shown a less-than-optimum diagnostic accuracy, so that now it tends to be substituted by tests for anti-tTG IgG, for which the few available studies have shown diagnostic performances superior to AGA. Since it is not known whether various available methods for measuring IgG anti-tTG antibodies offer similar diagnostic performances, we have compared the results obtained from nine second-generation commercial methods (D-tek, Phadia, Immco, Orgentec, Radim, Euroimmun, Inova, Aesku, Generic Assays), measuring IgG anti-tTG antibodies in 20 patients with CD and SIgAD and in 113 controls (9 patients with SIgAD without CD, 54 patients with chronic liver disease, and 50 healthy individuals). Diagnostic sensitivity, calculated by means of ROC plot analysis, ranged between 75% and 95%, and specificity ranged from 94% to 100%. In the same population, the diagnostic sensitivity and specificity of AGA IgG were 40% and 87%, respectively. Even though they perform differently, all IgG anti-tTG methods evaluated are reliable serological assays for the diagnosis of CD in SIgAD patients, with diagnostic accuracy superior to the AGA IgG method. The methods that use a mix of tTG and gliadin peptides as the antigenic preparation have a specificity slightly lower than that of the methods that use only tTG.
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PMID:Diagnostic accuracy of IgA anti-tissue transglutaminase antibody assays in celiac disease patients with selective IgA deficiency. 1778 8

In 1997, a German group demonstrated that the antigen of the biomarker EMA (endomysial antibodies) in coeliac disease is a calcium-dependent thiol enzyme, transglutaminase type 2 (TG2). This most important discovery opened up an exciting field of research aimed at a better understanding of the pathogenesis of coeliac disease, a T-cell-driven autoimmune disorder with a prevalence of about 1%. The accidental activation of TG2, possibly caused by a stress-induced local deficiency of zinc in the intestinal wall, might play a key role where the enzyme catalyzes an atypical deamidation of specific glutamine residues of food gliadins. The genetic contribution is HLA DQ2 or DQ8, which can form a complex with the TG2-modified gliadin residues, resulting in an immune response with the formation of antibodies against both gliadin and the enzyme. Indeed, the immunopathogenesis of coeliac disease can now be recognized partly at the molecular level. Progress has already improved the opportunities for laboratory diagnostics and, hopefully, new ways of treating and preventing coeliac disease will become available. These exciting developments might stimulate research within other fields of autoimmune disorders. With its focus on TG2, this review highlights some of the intriguing mechanisms of the pathogenesis of coeliac disease, such as the structure of the neo-antigen, the involvement of calcium and zinc, and the effects of coeliac antibodies on TG2 activity. Moreover, the many pitfalls due to dubious laboratory practice are addressed, as is the potential when a fundamental biological mechanism is understood at the molecular level.
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PMID:Transglutaminase and the pathogenesis of coeliac disease. 1824 2


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