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Transglutaminase 2

tissue transglutaminase, TG2, transglutaminase 2
Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. The protein encoded by this gene acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. Finally, the encoded protein is the autoantigen implicated in celiac disease. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Transglutaminase, IgA, HAD, CAN, AGE
Papers using tissue transglutaminase antibodies
Protein 4.2: a complex linker.
Polymenis Michael, In PLoS ONE, 2008
... TG2 expression in these stably transfected cells was induced by incubation with 2 µg/mL doxycycline (Sigma Aldrich, Inc) ...
Circuit-breakers: optical technologies for probing neural signals and systems
Zeng Hongkui et al., In Frontiers in Systems Neuroscience, 2006
... -Tg2-CreERT2;Ai9, in which the CreERT2 recombinase expression from the BAC transgenic line ...
Epithelial--mesenchymal and mesenchymal--epithelial transitions in carcinoma progression
Lee Ming-Ting et al., In Molecular Cancer, 2006
... Anti-TG2 was purchase from Thermo Scientific (Fremont, CA) ...
Prolyl endopeptidase-mediated destruction of T cell epitopes in whole gluten: chemical and immunological characterization.
Buckle Ashley M., In PLoS ONE, 2004
... Synthesis of peptides and purification of recombinant human TG2Synthetic peptides were purchased from GL Biochem Ltd (Shanghai, China) ...
Polyriboinosinic polyribocytidylic acid (poly(I : C)) induces stable maturation of functionally active human dendritic cells.
Batra Surinder K., In PLoS ONE, 1998
... The antibodies used were anti-TG2 IgG produced in rabbit (Abcam, ab421) and Alexa fluor ...
Papers on tissue transglutaminase
Serum thyrotropin level of 30 μIU/mL is inadequate for preablative thyroglobulin to serve as a prognostic marker for differentiated thyroid cancer.
Lin et al., Beijing, China. In Endocrine, Feb 2016
The initial and last measurements of ps-Tg were marked as Tg1 and Tg2, respectively, with a median interval of 8 days, so does TSH.
Tissue transglutaminase-2 promotes gastric cancer progression via the ERK1/2 pathway.
Su et al., Shanghai, China. In Oncotarget, Feb 2016
Tissue transglutaminase-2 (TG2), a multifunctional member of the transglutaminase family, has been shown to be critical for tumor initiation and progression.
Fully-automated, chemiluminescence IgA and IgG anti-tissue transglutaminase (tTG) antibodies serum assays for the screening of celiac disease.
Lippi et al., Merano, Italy. In J Immunol Methods, Feb 2016
MATERIALS AND METHODS: The IgA and IgG anti-tissue transglutaminase (tTG) antibodies (Quanta Flash® IgA and Quanta Flash® IgG tTG, Inova Diagnostics, San Diego, CA, USA) were measured with the fully-automated BIO-FLASH® analyzer (Inova Diagnostics) in serum samples of 727 consecutive patients without a diagnosis of CD.
Cyclic AMP is a key regulator of M1 to M2a phenotypic conversion of microglia in the presence of Th2 cytokines.
Pearse et al., Miami, United States. In J Neuroinflammation, Dec 2015
The combination of cyclic AMP and IL-4, but neither alone, induced an Arg-1(+)/iNOS(-)cell phenotype with concomitant expression of other M2-specific markers including TG2 and RELM-α.
Pharmacological approaches in celiac disease.
Verdu et al., Hamilton, Canada. In Curr Opin Pharmacol, Dec 2015
Celiac disease is an autoimmune enteropathy triggered by the ingestion of gluten, characterized by immune responses toward gluten constituents and the autoantigen transglutaminase 2. The only current treatment available for celiac disease is a gluten-free diet, however there are a plethora of therapies in development for the treatment of celiac disease (e.g.
New insights into immune mechanisms underlying autoimmune diseases of the gastrointestinal tract.
Corazza et al., Pavia, Italy. In Autoimmun Rev, Dec 2015
While the pathogenic role of specific circulating autoantibodies, i.e., respectively anti-parietal cell, anti-tissue transglutaminase, anti-enterocyte and anti-neutrophil cytoplasmic, is still controversial, some common T-cell mediated mechanisms for inflammation - increase in T helper cell type 1/type 17 pro-inflammatory cytokines- or losing self-tolerance-abnormal regulatory T cell function - are recognized as crucial mediators of the tissue damage causing atrophy of the stomach mucosa in autoimmune atrophic gastritis, villous flattening of the small bowel in celiac disease and autoimmune enteropathy, and mucosal ulceration of the colon in ulcerative colitis.
Study of the mechanism underlying the inhibitory effects of transglutaminase II on apoptosis in the osteosarcoma MG-63 cell line under hypoxic conditions.
Chen et al., Binzhou, China. In Oncol Lett, Dec 2015
UNASSIGNED: The aim of the present study was to investigate the association between the apoptosis phenomenon in the MG-63 osteosarcoma cell line, and transglutaminase II (TG2) expression.
T cell epitopes and post-translationally modified epitopes in type 1 diabetes.
James et al., Seattle, United States. In Curr Diab Rep, Nov 2015
Modifying enzymes such as peptidyl deiminases and tissue transglutaminase are activated in response to beta cell stress, providing a mechanistic link between post-translational modification and interactions with the environment.
Seronegative Celiac Disease and Immunoglobulin Deficiency: Where to Look in the Submerged Iceberg?
Di Leo et al., Bari, Italy. In Nutrients, Sep 2015
Immunohistochemistry/immunofluorescence tissue transglutaminase (tTG)-targeted mucosal immunoglobulin A (IgA) immune complexes in the intestinal mucosa of SNCD patients may be useful.
Celiac disease: Autoimmunity in response to food antigen.
Sollid et al., Oslo, Norway. In Semin Immunol, Sep 2015
Post-translational modification (deamidation) of gluten peptides by transglutaminase 2 (TG2) is essential for the peptides to act as HLA-DQ-restricted T-cell antigens.
Risk of pediatric celiac disease according to HLA haplotype and country.
TEDDY Study Group et al., Sierra Leone. In N Engl J Med, 2014
In addition, nearly all children with celiac disease have serum antibodies against tissue transglutaminase (tTG).
Continuous throughput and long-term observation of single-molecule FRET without immobilization.
Lemke et al., Heidelberg, Germany. In Nat Methods, 2014
We demonstrate the power of our method by studying a variety of complex nucleic acid and protein systems, including DNA Holliday junctions, nucleosomes and human transglutaminase 2.
Treatment of children and adolescents with Hodgkin lymphoma without radiotherapy for patients in complete remission after chemotherapy: final results of the multinational trial GPOH-HD95.
Schellong et al., Berlin, Germany. In J Clin Oncol, 2013
Patients in treatment group 1 (TG1; early stages) received two cycles of vincristine, prednisone, procarbazine, and doxorubicin or vincristine, prednisone, etoposide, and doxorubicin chemotherapy; additional two or four cycles of cyclophosphamide, vincristine, prednisone, and procarbazine were added in TG2 (intermediate stages) or TG3 (advanced stages), respectively.
Tissue transglutaminase overexpression does not modify the disease phenotype of the R6/2 mouse model of Huntington's disease.
Lesort et al., Birmingham, United States. In Exp Neurol, 2012
An increase in TG2 does not significantly modify the onset nor the progression of the behavioral phenotype and neuropathological features of R6/2 transgenic mice.
Interactions among secretory immunoglobulin A, CD71, and transglutaminase-2 affect permeability of intestinal epithelial cells to gliadin peptides.
Heyman et al., Paris, France. In Gastroenterology, 2012
On binding to apical CD71, SIgA (with or without gliadin peptides) enters a recycling pathway and avoids lysosomal degradation, allowing transcytosis of bound peptides. This process may be facilitated by Tgase2 in celiac disease.
Ataxia-Telangiectasia, Mutated (ATM)/Nuclear Factor κ light chain enhancer of activated B cells (NFκB) signaling controls basal and DNA damage-induced transglutaminase 2 expression.
Brown et al., Gainesville, United States. In J Biol Chem, 2012
work establishes a novel ATM-dependent signaling loop where TG2 and NFkappaB activate each other resulting in sustained activation of NFkappaB and acquisition of a drug-resistant phenotype
Transglutaminase is essential for IgA nephropathy development acting through IgA receptors.
Monteiro et al., Paris, France. In J Exp Med, 2012
demonstrate that TGase2 is responsible for a pathogenic amplification loop facilitating IgA1-sCD89 deposition and mesangial cell activation, thus identifying TGase2 as a target for therapeutic intervention in this disease
High abundance of plasma cells secreting transglutaminase 2-specific IgA autoantibodies with limited somatic hypermutation in celiac disease intestinal lesions.
Sollid et al., Oslo, Norway. In Nat Med, 2012
this study reveals several previously unrecognized aspects of the TG2-specific autoantibody response in celiac disease, primarily the abundance and mutation profile of TG2-specific plasma cells, and the limited inhibitory activity of the antibodies
Expression TGM2 and BNIP3 have prognostic significance in laryngeal cancer patients receiving surgery and postoperative radiotherapy: a retrospective study.
Hu et al., Hangzhou, China. In J Transl Med, 2011
BNIP3 expression and TGM2 expression are independent prognostic factors in laryngeal SCC patients receiving postoperative radiotherapy.
Defective CFTR induces aggresome formation and lung inflammation in cystic fibrosis through ROS-mediated autophagy inhibition.
Maiuri et al., Milano, Italy. In Nat Cell Biol, 2010
Defective CFTR-induced upregulation of reactive oxygen species (ROS) and tissue transglutaminase (TG2) drive the crosslinking of beclin 1, leading to sequestration of phosphatidylinositol-3-kinase (PI(3)K) complex III and accumulation of p62, which regulates aggresome formation.
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