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BioMed Research International
Volume 2017 (2017), Article ID 3982906, 9 pages
Research Article

CYLD Deubiquitinase Negatively Regulates High Glucose-Induced NF-κB Inflammatory Signaling in Mesangial Cells

1Department of Endocrinology, The Affiliated Hospital of Southwest Medical University, Luzhou, Sichuan 646000, China
2Department of Kidney Endocrinology, The People’s Hospital of Qingbaijiang, Qingbaijiang, Sichuan 610300, China
3Faculty of Chinese Medicine, Macau University of Science and Technology, Avenida Wai Long, Taipa, Macau
4State Key Laboratory of Quality Research in Chinese Medicine, Macau University of Science and Technology, Avenida Wai Long, Taipa, Macau
5Collaborative Innovation Center for Prevention and Treatment of Cardiovascular Disease of Sichuan Province, Southwest Medical University, Luzhou, Sichuan 646000, China

Correspondence should be addressed to Yang Long; moc.361@yl5230gnoloaix and Yong Xu; moc.nuyila@llywyx

Received 30 July 2017; Revised 12 October 2017; Accepted 22 October 2017; Published 12 November 2017

Academic Editor: Massimo Collino

Copyright © 2017 Yanhui Li et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Nuclear factor-kappa B (NF-κB) is the key part of multiple signal transduction of inflammation in the pathogenesis of diabetic nephropathy (DN). The ubiquitin-proteasome system is extensively involved in the regulation of the NF-κB pathway. Cylindromatosis (CYLD) has deubiquitinase activity and acts as a negative regulator of the NF-κB signaling pathway. However, the association between CYLD and NF-κB inflammatory signaling in DN is unclear. In the present study, mouse glomerular mesangial cells (GMCs) and rat GMCs were stimulated by elevated concentrations of glucose (10, 20, and 30 mmol/L high glucose) or mannitol as the osmotic pressure control. CYLD was overexpressed or suppressed by transfection with a CYLD expressing vector or CYLD-specific siRNA, respectively. Our data showed that high glucose significantly inhibited the protein and mRNA expression of CYLD in a dose- and time-dependent manner (both ). siRNA-mediated knockdown CYLD facilitated the high glucose-induced activation of NF-κB signaling and triggered the release of MCP-1, IL-6, and IL-8 (all ). However, these high glucose-mediated effects were blunted by overexpression of CYLD (). The present results support the involvement of CYLD in the regulation of NF-κB inflammatory signaling induced by elevated glucose, implicating CYLD as a potential therapeutic target of DN.