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ARTICLE
The function of ubiquitin-specific protease 31 in intracerebral hemorrhage
1 Department of Neurology, Shanghai Xuhui District Dahua Hospital, Shanghai, 200237, China
2 Department of Endocrinology and Metabolism, Minhang Hospital, Fudan University, Shanghai, 201199, China
* Address correspondence to: Shunjun Li,
# These authors have contributed equally to this work
BIOCELL 2022, 46(6), 1545-1555. https://doi.org/10.32604/biocell.2022.017544
Received 19 May 2021; Accepted 04 August 2021; Issue published 07 February 2022
Abstract
Intracerebral hemorrhage (ICH) is the most serious type of stroke. High level of thrombin is found in the ICH. Ubiquitin-specific protease (USP) 31, a member of deubiquitinating enzymes family, has been found to negatively regulate the NF-κB pathway. However, the function of USP31 in ICH remains largely unknown. In the present study, the mRNA and protein expression levels of USP31 were measured by real-time PCR and western blot. Flow cytometry was used to measure cell apoptosis and the level of reactive oxygen species (ROS). In the current study, we found the mRNA level of USP31 was decreased in peripheral blood mononuclear cells (PBMCs) from the patients with ICH. Thrombin stimulated cell apoptosis, and increased the ROS level, the productions of interleukin-1β (IL-1β), tumor necrosis factor-α (TNF-α), and monocyte chemoattractant protein-1 (MCP-1), but it decreased the expression level of USP31 in BV-2 cells. In agreement, USP31 overexpressing could alleviate these effects caused by thrombin. USP31 partially reversed the thrombin induced increase of nuclear factor kappa B (NF-κB) localization. Further, NF-κB inhibitor could alleviate the effects induced by USP31 knockdown. In addition, USP31 decreased the ubiquitination level of IκBα, which might contribute to the depression of NF-κB activation. In conclusions, USP31 played a role in the ICH might via regulating NF-κB signaling pathway.Keywords
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