ArticleAutoimmune diseases2013
Posttranslational Protein Modification in the Salivary Glands of Sjögren's Syndrome Patients.
Article in Autoimmune diseases, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers, 1 of them a synthesis that pooled it.
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Who cites it
6 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Sjögren's syndrome: novel insights from proteomics and miRNA expression analysis.Frontiers in immunology · 2023Pooled it
- The Post-Translational Modifications of Human Salivary Peptides and Proteins Evidenced by Top-Down Platforms.International journal of molecular sciences · 2023Review
- Reactive oxygen species inhibit catalytic activity of peptidylarginine deiminase.Journal of enzyme inhibition and medicinal chemistry · 2017Article
- Activation of Peptidylarginine Deiminase in the Salivary Glands ofJournal of immunology research · 2017Article
- Potential protein targets of the peptidylarginine deiminase 2 and peptidylarginine deiminase 4 enzymes in rheumatoid synovial tissue and its possible meaning.European journal of rheumatology · 2016Article
- Reduced glutathione as a physiological co-activator in the activation of peptidylarginine deiminase.Arthritis research & therapy · 2016Article
Corrections and comments
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Authors and funding
8 authors.
Funding
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Abstract
The present study investigated posttranslational reactions in the salivary glands of patients with Sjögren's syndrome. We analysed the biopsies of primary Sjögren's patients using immunohistochemistry and a tag-purified anticyclic citrullinated protein (CCP) antibody to detect citrullinated peptides, and the presence of peptidylarginine deiminase 2 (PAD2) was assessed simultaneously. The present work demonstrated the weak presence of the PAD2 enzyme in some normal salivary glands, although PAD2 expression was increased considerably in Sjögren's patients. The presence of citrullinated proteins was also detected in the salivary tissues of Sjögren's patients, which strongly supports the in situ posttranslational modification of proteins in this setting. Furthermore, the mutual expression of CCP and PAD2 suggests that this posttranslational modification is enzyme dependent. In conclusion, patients with Sjögren's syndrome expressed the catalytic machinery to produce posttranslational reactions that may result in autoantigen triggering.
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Registered trials
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