Evidence map›Paper›PMID 30136165›Full record

ReviewCellular and molecular life sciences : CMLS2018

Anti-type 2 transglutaminase antibodies as modulators of type 2 transglutaminase functions: a possible pathological role in celiac disease.

Stefania Martucciello, Gaetana Paolella, Carla Esposito, Marilena Lepretti, Ivana Caputo

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.1field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

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

13 citing papers in PubMed, 19 citations in OpenAlex.

  1. Review
  2. Review
  3. The Role of Transglutaminase 2 in Cancer: An Update.International journal of molecular sciences · 2024
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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 at 1 institution in 1 country.

Stefania MartuccielloDepartment of Chemistry and Biology, University of Salerno, via Giovanni Paolo II, 132, 84084, Fisciano (SA), Italy.
Gaetana PaolellaDepartment of Chemistry and Biology, University of Salerno, via Giovanni Paolo II, 132, 84084, Fisciano (SA), Italy.
Carla EspositoDepartment of Chemistry and Biology, University of Salerno, via Giovanni Paolo II, 132, 84084, Fisciano (SA), Italy.
Marilena LeprettiDepartment of Chemistry and Biology, University of Salerno, via Giovanni Paolo II, 132, 84084, Fisciano (SA), Italy.
Ivana CaputoDepartment of Chemistry and Biology, University of Salerno, via Giovanni Paolo II, 132, 84084, Fisciano (SA), Italy. icaputo@unisa.it.ORCID http://orcid.org/0000-0003-2825-9711
University of Salerno · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Auto-antibodies to the ubiquitous enzyme type-2 transglutaminase (TG2) are a specific hallmark of celiac disease (CD), a widely diffused, multi-factorial disease, affecting genetically predisposed subjects. In CD an inflammatory response, at the intestinal level, is triggered by diet consumption of gluten-containing cereals. Intestinal mucosa displays various degrees of atrophy and hyperplasia, with consequent global intestinal dysfunction and other relevant extra-intestinal symptoms. Through deamidation of specific glutamines of gluten-derived gliadin peptides, TG2 strongly enhances gliadin immunogenicity. In addition, TG2 cross-linking activity may generate complexes between TG2 itself and gliadin peptides, and these complexes seem to cause the auto-immune response by means of an apten-carrier-like mechanism of antigen presentation. Anti-TG2 antibodies can be early detected in the intestinal mucosa of celiac patients and are also abundantly present into the serum, thus potentially reaching other organs and tissues by blood circulation. Recently, the possible pathogenetic role of auto-antibodies to TG2 in CD has been investigated. Here, we report an overview about the genesis of these antibodies, their specificity, their modulating ability toward TG2 enzymatic or non-enzymatic activities and their biological effects exerted by interacting with extracellular TG2 or with cell-surface TG2. We also discuss the auto-immune response occurring in CD against other TG members (i.e. type 3 and type 6) and analyze the occurrence of anti-TG2 antibodies in other auto-immune CD-related diseases. Data now available let us to suppose that, even if antibodies to TG2 do not represent the triggering molecules in CD, they could be important players in disease progression and manifestations.

Indexed as

AnimalsAutoantibodiesBiocatalysisCeliac DiseaseEpitopesGliadinGTP-Binding ProteinsHumansProtein Glutamine gamma Glutamyltransferase 2TransglutaminasesAutoantibodiesEpitopesGliadinGTP-Binding ProteinsProtein Glutamine gamma Glutamyltransferase 2TransglutaminasesAnti-TG2 auto-antibodiesAuto-immune diseasesCeliac diseaseHumoral auto-immune responsePost-translational modificationsType-2 transglutaminase

Identifiers

PMID30136165
PMCPMC11105699
OpenAlexW2888184509

What OpenQuestion holds

Textmetadata
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Registered trials

None linked

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.