کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
3256962 | 1207381 | 2013 | 8 صفحه PDF | دانلود رایگان |
Post-translational modification of proteins by deamidation or transamidation by tissue transglutaminase (tTG) has been suggested as a possible mechanism for the development of autoimmunity. Sequence analysis of protein kinase C delta (PKCδ) identified an amino acid motif that suggested the possibility that PKCδ was a glutamine substrate of tTG and MALDI-TOF analysis of synthesised peptides from PKCδ proved that this was the case. Polymerisation experiments using recombinant tTG and biotinylated hexapeptide substrate incorporation assays demonstrated that PKCδ is a substrate for tTG-mediated transamidation. Elevated levels of anti-PKCδ antibodies were detected in sera from patients with coeliac disease (p < 0.0001) but not from patients with other autoimmune disorders. These data suggest that a subset of patients with coeliac disease produce autoantibodies against PKCδ and that this response may stem from a tTG–PKCδ substrate interaction.
► We examine the possibility that PKCδ is a substrate for tissue transglutaminase.
► A peptide derived from PKCδ is deamidated and transamidated by tTG.
► Interaction between tTG and PKCδ results in heterodimer formation.
► Some patients with coeliac disease produce anti-PKCδ autoantibodies.
Journal: Clinical Immunology - Volume 147, Issue 1, April 2013, Pages 1–8