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dc.contributor.authorByrne, Greg
dc.contributor.authorFeighery, Con
dc.contributor.authorJackson, John
dc.contributor.authorKelly, Jacinta
dc.date.accessioned2012-02-01T10:25:22Z
dc.date.available2012-02-01T10:25:22Z
dc.date.issued2012-02-01T10:25:22Z
dc.identifier.citationClin Immunol. 2010 Sep;136(3):426-31. Epub 2010 May 21.en_GB
dc.identifier.issn1521-7035 (Electronic)en_GB
dc.identifier.issn1521-6616 (Linking)en_GB
dc.identifier.pmid20488756en_GB
dc.identifier.doi10.1016/j.clim.2010.04.017en_GB
dc.identifier.urihttp://hdl.handle.net/10147/207452
dc.description.abstractThe detection of antibodies directed against tissue transglutaminase (tTG) in serum is a sensitive and specific test for suspected coeliac disease. tTG is a ubiquitous, multifunctional enzyme that has been implicated in many important physiological processes as well as the site-specific deamidation of glutamine residues in gluten-derived peptides. This modification of gluten peptides facilitates their binding to HLA-DQ2, which results in amplification of the T-cell response to gluten. The purpose of this study was to investigate the possibility that patient IgA autoantibodies directed against tTG interfere with the crosslinking activity of the enzyme. IgA autoantibodies against tTG were isolated/depleted from patient serum and tested for their capacity to interfere with tTG activity in vitro using a sensitive fluorescence-based activity assay. We have demonstrated that autoantibodies cause significant inhibition of tTG-mediated crosslinking at equimolar and 2:1 ratios of antibody to enzyme.
dc.language.isoengen_GB
dc.subject.meshAdulten_GB
dc.subject.meshAgeden_GB
dc.subject.meshAged, 80 and overen_GB
dc.subject.meshAutoantibodies/*blooden_GB
dc.subject.meshCeliac Disease/*enzymology/*immunologyen_GB
dc.subject.meshFemaleen_GB
dc.subject.meshGlutens/immunology/metabolismen_GB
dc.subject.meshHLA-DQ Antigens/metabolismen_GB
dc.subject.meshHumansen_GB
dc.subject.meshImmunoglobulin A/blooden_GB
dc.subject.meshMaleen_GB
dc.subject.meshMiddle Ageden_GB
dc.subject.meshRecombinant Proteins/antagonists & inhibitors/immunology/metabolismen_GB
dc.subject.meshT-Lymphocytes/immunologyen_GB
dc.subject.meshTransglutaminases/*antagonists & inhibitors/*immunology/metabolismen_GB
dc.subject.meshYoung Adulten_GB
dc.titleCoeliac disease autoantibodies mediate significant inhibition of tissue transglutaminase.en_GB
dc.contributor.departmentNational Children's Research Centre, Our Lady's Children's Hospital, Crumlin,, Dublin 12, Ireland. greg.byrne@ucd.ieen_GB
dc.identifier.journalClinical immunology (Orlando, Fla.)en_GB
dc.description.provinceLeinster
html.description.abstractThe detection of antibodies directed against tissue transglutaminase (tTG) in serum is a sensitive and specific test for suspected coeliac disease. tTG is a ubiquitous, multifunctional enzyme that has been implicated in many important physiological processes as well as the site-specific deamidation of glutamine residues in gluten-derived peptides. This modification of gluten peptides facilitates their binding to HLA-DQ2, which results in amplification of the T-cell response to gluten. The purpose of this study was to investigate the possibility that patient IgA autoantibodies directed against tTG interfere with the crosslinking activity of the enzyme. IgA autoantibodies against tTG were isolated/depleted from patient serum and tested for their capacity to interfere with tTG activity in vitro using a sensitive fluorescence-based activity assay. We have demonstrated that autoantibodies cause significant inhibition of tTG-mediated crosslinking at equimolar and 2:1 ratios of antibody to enzyme.


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