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3 results on '"ABIN-1"'

1. ABIN‐1 protects chondrocytes from lipopolysaccharide‐induced inflammatory injury through the inactivation of NF‐κB signalling.

Author

Peng, Kan, Li, Yanqi, Lu, Chao, and Hu, Shouye

Subjects
*LIPOPOLYSACCHARIDES, *APOPTOSIS, *WOUNDS & injuries, *CARTILAGE cells, *INFLAMMATION
Abstract

The A20‐binding inhibitor of nuclear factor (NF)‐κB‐1 (ABIN‐1) protein has recently been implicated as a key regulator of inflammation with involvement in multiple inflammatory diseases. However, the function of ABIN‐1 in osteoarthritis (OA) remains unclear. In the current study, we explored the role of ABIN‐1 in the regulation of lipopolysaccharide (LPS)‐induced inflammatory injury of chondrocytes, which served as an in vitro model of OA. Results revealed that ABIN‐1 expression was induced by chondrocyte exposure to LPS. ABN‐1 silencing exacerbated LPS‐induced apoptosis and the inflammatory response, while ABIN‐1 overexpression alleviated the inflammatory response and LPS‐induced apoptosis in chondrocytes. Moreover, ABIN‐1 overexpression resulted in significantly decreased LPS‐induced NF‐κB activation. Notably, activation of NF‐κB signalling significantly reversed ABIN‐1‐mediated inhibitory effects on LPS‐induced inflammatory injury in chondrocytes. Taken together, these results demonstrate that ABIN‐1 protects chondrocytes against LPS‐induced inflammatory injury through the suppression of NF‐κB signalling. Our study suggests a potential role for ABIN‐1 in OA. Further, we show that ABIN‐1 may serve as a potential target for controlling joint inflammation. [ABSTRACT FROM AUTHOR]

Published
2020
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2. LUBAC and ABIN-1 Modulate TRAIL-Based NF-κB Induction in Human Embryonic Kidney 293 Cells

Author

Sebastian Dorn, Christian Schoergenhofer, Markus Müller, Michael Krainer, and Bernd Jilma

Subjects
0301 basic medicine, lcsh:Medicine, TRAIL, General Biochemistry, Genetics and Molecular Biology, Deubiquitinating enzyme, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Ubiquitin, Downregulation and upregulation, LUBAC, Original Research Article, lcsh:QH301-705.5, Gene knockdown, biology, lcsh:R, HEK 293 cells, NF-κB, Cell biology, 030104 developmental biology, lcsh:Biology (General), chemistry, Cell culture, ABIN-1, biology.protein, Tumor necrosis factor alpha, NF-κB regulation, 030217 neurology & neurosurgery
Abstract

Tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) is known to activate the canonical NF-κB pathway similar to TNF. The exact mechanism of the entire signaling cascade is still under investigation. The involvement of linear ubiquitylation as upregulating component has already been shown recently in some cell lines, but not in human embryonic kidney 293 (HEK293) cells. The downregulating function of the ABIN-1 (A20 binding and inhibitor of NF-κB) as linear ubiquitylation antagonist has been shown in combination with some NF-κB-inducing pathways, but not with TRAIL. We performed luciferase and western blot assays using HEK293 cells stimulated with either TRAIL (or TNF as a control) to analyze the involvement of linear ubiquitin chain assembly complex (LUBAC) components and the impact of ABIN-1 and ABIN-1-MAD (truncated form without A20 binding site) on NF-κB signaling. For overexpression experiments, we added plasmids of ABIN-1 and ABIN-1-MAD or LUBAC components HOIP, HOIL-1, or SHARPIN (single and combinations). For downregulation experiments five pairs of either SHARPIN, HOIL-1, or HOIP targeting miRNAs or one miRNA for ABIN-1 were designed and added. ABIN-1 and its truncated form ABIN-1-MAD reduced the NF-κB induction significantly indicating its involvement as antagonist (independent of deubiquitinase A20) of linear ubiquitylation in TRAIL-induced NF-κB signaling. In opposition, knockdown of ABIN-1 using a specific ABIN-1 miRNA led a clear increase of NF-κB signaling. Addition of single LUBAC components or combinations (except for SHARPIN with HOIL-1) resulted in clearly stronger NF-κB inductions. MiRNAs targeting LUBAC components significantly reduced NF-κB activation. Thus, in HEK293 cells linear ubiquitylation by LUBAC critically upregulates and ABIN-1 downregulates TRAIL-induced NF-κB signaling and may be interesting targets for future pathological therapies.

Published
2018
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3. ABIN-1 negatively regulates NF-κB by inhibiting processing of the p105 precursor

Author

Cohen, Shai, Ciechanover, Aaron, Kravtsova-Ivantsiv, Yelena, Lapid, Dana, and Lahav-Baratz, Shirly

Subjects
*CHEMICAL inhibitors, *NF-kappa B, *PROTEIN precursors, *CELLULAR signal transduction, *UBIQUITIN, *CARRIER proteins, *HOMOLOGY (Biology)
Abstract

Abstract: p105 plays dual roles in NF-κB signaling: in its precursor form it inhibits NF-κB activation, but limited processing by the ubiquitin system generates the p50 active subunit of the transcription factor. Here we show that ABIN-1, an A20-binding protein that is also known to attenuate NF-κB activation, inhibits p105 processing. p105 and ABIN-1 physically interact with one another, but the binding is not necessary for inhibition of processing. Rather, it appears to stabilize ABIN-1 and to increase its level, which further augments its inhibitory effect. Deletion of the processing inhibitory domain (PID) of p105 abrogates the inhibition which also requires the ABIN homology domain (AHD)-2 of ABIN-1. Together, the effects of ABIN-1 on p105 processing and of p105 on stabilizing ABIN-1 act to potentiate the NF-κB inhibitory activity of ABIN-1. [Copyright &y& Elsevier]

Published
2009
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