BIX - CAS 101714-41-4
Category: Inhibitor
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BIX is a BiP (Hsp70-5) ER chaperone inducer that induces BiP expression in vitro and in vivo. BIX protects against ER-stress induced cell death in neuronal and retinal cell lines, and also protects against ischaemia-induced hippocampal cell death in vivo.
≥98% by HPLC
2-(3,4-Dihydroxyphenyl)-2-oxoethyl ester thiocyanic acid; Thiocyanic acid,2-(3,4-dihydroxyphenyl)-2-oxoethyl ester
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1.Effect of an inducer of BiP, a molecular chaperone, on endoplasmic reticulum (ER) stress-induced retinal cell death.
Inokuchi Y;Nakajima Y;Shimazawa M;Kurita T;Kubo M;Saito A;Sajiki H;Kudo T;Aihara M;Imaizumi K;Araie M;Hara H Invest Ophthalmol Vis Sci. 2009 Jan;50(1):334-44. doi: 10.1167/iovs.08-2123. Epub 2008 Aug 29.
PURPOSE: ;The effect of a preferential inducer of 78 kDa glucose-regulated protein (GRP78)/immunoglobulin heavy-chain binding protein (BiP; BiP inducer X, BIX) against tunicamycin-induced cell death in RGC-5 (a rat ganglion cell line), and also against tunicamycin- or N-methyl-D-aspartate (NMDA)-induced retinal damage in mice was evaluated.;METHODS: ;In vitro, BiP mRNA was measured after BIX treatment using semi-quantitative RT-PCR or real-time PCR. The effect of BIX on tunicamycin (at 2 microg/mL)-induced damage was evaluated by measuring the cell-death rate and CHOP protein expression. In vivo, BiP protein induction was examined by immunostaining. The retinal cell damage induced by tunicamycin (1 microg) or NMDA (40 nmol) was assessed by examining ganglion cell layer (GCL) cell loss, terminal deoxyribonucleotidyl transferase (TdT)-mediated dUTP nick-end labeling (TUNEL) staining, and CHOP protein expression.;RESULTS: ;In vitro, BIX preferentially induced BiP mRNA expression both time- and concentration-dependently in RGC-5 cells. BIX (1 and 5 microM) significantly reduced tunicamycin-induced cell death, and BIX (5 microM) significantly reduced tunicamycin-induced CHOP protein expression.
2.A novel role for bone-derived cells in ankylosing spondylitis: Focus on IL-23.
Jo S;Koo BS;Lee B;Kwon E;Lee YL;Chung H;Sung IH;Park YS;Kim TH Biochem Biophys Res Commun. 2017 Sep 23;491(3):787-793. doi: 10.1016/j.bbrc.2017.07.079. Epub 2017 Jul 18.
The main aim of this study are to explore the role of bone-derived cells (BdCs) in ankylosing spondylitis (AS) and determine the underlying molecular mechanisms of IL-23 production. Primary BdCs were isolated from diced bone of facet joints obtained during surgery from seven AS patients and seven disease control (Ct) patients. Osteoblastic activity of BdCs was assessed by measuring their alkaline phosphatase activity and by alizarin red staining. Osteoblast and endoplasmic reticulum (ER) stress-related genes were assessed by quantitative PCR, immunoblotting, immunofluorescence, and immunohistochemistry. In addition, expression of IL-23 in response to BIX (selective BIP inducer X)-induced ER stress was evaluated by qPCR and ELISA. Protein interaction and binding to IL-23 promoter were confirmed by Immunoprecipitation and Chromatin immunoprecipitation, respectively. Transcript levels of genes involved in osteoblast function, as well as of the ER stress marker were higher in the AS group than the Ct group, and elevated RUNX2, BiP and IL-23 expression were observed in the BdCs, serum, and bone biopsies from the AS group. BIX-induced ER stress stimulated osteoblastic activity and IL-23 secretion by upregulating RUNX2 expression.
3.A molecular chaperone inducer protects neurons from ER stress.
Kudo T;Kanemoto S;Hara H;Morimoto N;Morihara T;Kimura R;Tabira T;Imaizumi K;Takeda M Cell Death Differ. 2008 Feb;15(2):364-75. Epub 2007 Nov 30.
The endoplasmic reticulum (ER) stress response is a defense system for dealing with the accumulation of unfolded proteins in the ER lumen. Recent reports have shown that ER stress is involved in the pathology of some neurodegenerative diseases and cerebral ischemia. In a screen for compounds that induce the ER-mediated chaperone BiP (immunoglobulin heavy-chain binding protein)/GRP78 (78 kDa glucose-regulated protein), we identified BiP inducer X (BIX). BIX preferentially induced BiP with slight inductions of GRP94 (94 kDa glucose-regulated protein), calreticulin, and C/EBP homologous protein. The induction of BiP mRNA by BIX was mediated by activation of ER stress response elements upstream of the BiP gene, through the ATF6 (activating transcription factor 6) pathway. Pretreatment of neuroblastoma cells with BIX reduced cell death induced by ER stress. Intracerebroventricular pretreatment with BIX reduced the area of infarction due to focal cerebral ischemia in mice. In the penumbra of BIX-treated mice, ER stress-induced apoptosis was suppressed, leading to a reduction in the number of apoptotic cells. Considering these results together, it appears that BIX induces BiP to prevent neuronal death by ER stress, suggesting that it may be a potential therapeutic agent for cerebral diseases caused by ER stress.
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CAS 101714-41-4 BIX

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