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Last update 08 May 2025

BRIX1

Last update 08 May 2025

Basic Info

Synonyms

biogenesis of ribosomes BRX1, BRIX, Brix domain-containing protein 2

+ [4]

Introduction

Required for biogenesis of the 60S ribosomal subunit.

Drugs associated with BRIX1

iRGD-Exo-siBRIX1

Target

BRIX1

Mechanism

BRIX1 inhibitors

Active Org.

Nanchang University [+1]

Originator Org.

Nanchang University [+1]

Active Indication

Colorectal Cancer

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with BRIX1

100 Translational Medicine associated with BRIX1

0 Patents (Medical) associated with BRIX1

Literatures (Medical) associated with BRIX1

01 Jun 2025·Journal of Equine Veterinary Science

The diagnostic accuracy of the Brix refractometer in determining mare colostrum with high and low immunoglobulin G concentrations

Article

Author: Akköse, Mehmet

BACKGROUNDFoals, that receive poor-quality colostrum, are exposed to a risk of failure of transfer of passive immunity. The Brix refractometer can be used for the estimation of the immunoglobulin (IgG) concentration of mare colostrum, yet there is a scarce literature available on Brix refractometer thresholds for use in the detection of mare colostra with high and low IgG concentrations.AIMThis study aimed to assess the diagnostic accuracy of the Brix refractometer in determining mare colostra with IgG concentrations of <50g/L, <60g/L, ≥80g/L, ≥100g/L and ≥125g/L.MATERIALS AND METHODSTwo hundred and seventeen Arabian mares had colostral IgG concentrations measured with the radial immunodiffusion assay and estimated with the Brix refractometer. Brix thresholds were determined by performing a receiver operating characteristics analysis.RESULTSThe mean colostral IgG concentration was 83.73 ± 2.46 g/L and colostral IgG concentrations had a high correlation (Pearson's r=0.78) with Brix percentages. The optimal refractometer thresholds for the determination of colostral IgG concentrations of <50, <60, ≥80, ≥100 and ≥125 g/L were ascertained to be ≤19.6 %, ≤20.1 %, >21.6 %, >23.6 % and >27.3 %, respectively. The sensitivity and specificity of the Brix refractometer for the determination of colostral IgG concentrations of <50, <60, ≥80, ≥100 and ≥125 g/L were found to be 89.3 % (95 % CI: 71.8-97.7 %) and 83.8 % (95 % CI: 77.5-89.0 %); 82.0 % (95 % CI: 68.6-91.4 %) and 88.1 % (95 % CI: 81.8-92.8 %); 85.3 % (95 % CI: 76.9-91.5 %) and 73.7 % (95 % CI: 63.9-82.1 %); 84.8 % (95 % CI: 73.0-92.8 %) and 76.1 % (95 % CI: 68.2-82.8 %); and 75.0 % (95 % CI: 53.3-90.2 %) and 90.4 % (95 % CI: 85.1-94.3 %), respectively.CONCLUSIONThe digital Brix refractometer showed a good performance in determining mare colostra with low and high IgG concentrations.

01 Dec 2024·Advanced Science

Targeting BRIX1 via Engineered Exosomes Induces Nucleolar Stress to Suppress Cancer Progression

Article

Author: Shao, Zhi‐Ming ; Li, Pengfei ; Hao, Qian ; Li, Yanan ; Gao, Bo ; Zhou, Xiang ; Tong, Jing ; Han, Tao ; Gan, Yu ; Xu, Yingying ; Xuan, Zhisheng ; Yan, Qingya ; Chen, Jiaxiang ; Jiang, Yi‐Zhou ; Zhong, Hongguang ; Yao, Litong ; Deng, Jun

AbstractElevated ribosome biogenesis correlates with the rapid growth and progression of cancer. Targeted blockade of ribosome biogenesis induces nucleolar stress, which preferentially leads to the elimination of malignant cells. In this study, it is reported that the nucleolar protein BRIX1 is a critical regulator for the homeostasis between ribosome biogenesis and p53 activation. BRIX1 facilitated the processing of pre‐rRNA by supporting the formation of the PeBoW complex. In addition, BRIX1 prevented p53 activation in response to nucleolar stress by impairing the interactions between MDM2 and the ribosomal proteins, RPL5, and RPL11, thereby triggering the resistance of cancer cells to chemotherapy. Conversely, depletion of BRIX1 induced nucleolar stress, which in turn activated p53 through RPL5 and RPL11, consequently inhibiting the growth of tumors. Moreover, engineered exosomes are developed, which are surface‐decorated with iRGD, a tumor‐homing peptide, and loaded with siRNAs specific to BRIX1, for the treatment of cancer. iRGD‐Exo‐siBRIX1 significantly suppressed the growth of colorectal cancer and enhanced the efficacy of 5‐FU chemotherapy in vivo. Overall, the study uncovers that BRIX1 functions as an oncoprotein to promote rRNA synthesis and dampen p53 activity, and also implies that targeted inhibition of BRIX1 via engineered exosomes can be a potent approach for cancer therapy.

01 Mar 2024·Clinics and Research in Hepatology and Gastroenterology

Clinical significance of ribosome production factor 2 homolog in hepatocellular carcinoma

Article

Author: Wang, Zhengyang ; Jin, Guang-Zhi ; An, Yan ; Xia, Yechen ; Shang, Mingyi

Hepatocellular carcinoma (HCC) is the third leading cause of cancer deaths worldwide. Dysregulation of ribosome biogenesis increases the risk of cancer. RPF2 (ribosome production factor 2 homolog), a member of the BRIX family, is involved in ribosome biogenesis. However, the biological functions of RPF2 in HCC remain unclear. This study aims to evaluate the function of RPF2 and its clinical significance in HCC. We collected 45 pairs of HCC/adjacent samples and 291 HCC samples. These samples were used to perform immunohistochemical analysis and western blot. Six cell lines were used to perform western blot, and two of cell lines, SMCC-7721 and SNU449, were subjected to CCK-8, wound healing and transwell assays. Immunofluorescence staining was executed in SMCC-7721 cells. The protein levels of RPF2 were higher in HCC tissues than in adjacent tissues. Immunofluorescence staining showed that the RPF2 protein was located in the nucleuses, especially the nucleolus. Furthermore, the immunohistochemical analysis showed that high expression levels of nuclear RPF2 correlated with poor prognosis, vascular invasion, liver cirrhosis and tumor size. Cell experiments showed that overexpression of RPF2 promoted cell proliferation, migration and invasion, while knockdown of RPF2 tended to show the opposite effect. This is the first report that RPF2 is involved in HCC progression. The levels of RPF2 were significantly high in HCC tumors and had a side effect on prognosis in HCC patients. RPF2 has the potential to be a useful marker for HCC.

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BRIX1

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