Abstract
BackgroundAlthough deubiquitinating enzymes (DUBs) such as CYLD, A20 and OTULIN are expressed in multiple tissues and thought to be linked with inflammatory diseases, their expression in periodontal tissues remains to be determined. This research was designed to assess the expression of CYLD, A20 and OTULIN in human gingiva, and to evaluate the regulation of these DUBs in human gingival fibroblasts (HGFs) upon different stimuli.MethodsImmunohistochemistry assay was conducted to determine the expression of CYLD, A20 and OTULIN in human gingiva. Immunofluorescence assay was employed to observe the protein expression of CYLD, A20 and OTULIN in HGFs. RT-PCR and western blots were carried out to assess gene and protein expression changes of these DUBs in HGFs upon LPS or TNF-α.ResultsCYLD, A20 and OTULIN were found to be expressed in human gingiva and HGFs. The expression of CYLD, A20 and OTULIN was lower in the inflamed gingival tissue samples compared with the healthy gingival tissue samples. Further, the expression of CYLD, A20 and OTULIN in HGFs exhibited distinct regulation by different stimuli. TNF-α treatment markedly increased NF-κB activation in HGFsConclusionsOur findings suggest that CYLD, A20 and OTULIN might play a role in the progression of periodontitis.
Highlights
Deubiquitinating enzymes (DUBs) such as CYLD, A20 and OTULIN are expressed in multiple tissues and thought to be linked with inflammatory diseases, their expression in periodontal tissues remains to be determined
Expression of deubiquitinases in human gingival tissues To determine the expression of CYLD, A20 and OTULIN in human gingiva, we performed immunohistochemistry staining on healthy and inflamed gingival tissue samples
The expression of CYLD, A20 and OTULIN was lower in the inflamed gingival tissue samples compared with the healthy gingival tissue samples (Fig. 1)
Summary
Deubiquitinating enzymes (DUBs) such as CYLD, A20 and OTULIN are expressed in multiple tissues and thought to be linked with inflammatory diseases, their expression in periodontal tissues remains to be determined. A protein containing 76 amino acids, has an essential role in variety of biological processes [1,2,3]. Ubiquitination is a critical post-translational protein modification, performed by specific ubiquitin enzymes [4, 5]. The ubiquitin enzymes attach ubiquitin to target proteins and modulate the function of the target proteins. Attached ubiquitins can be removed by deubiquitinating enzymes (DUBs). Several DUBs including CYLD, A20 and OTULIN are reported to inhibit NF-κB activation and play an important role in modulating immunity and inflammation [6,7,8].
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
