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Last update 23 Jan 2025

VDAC2

Last update 23 Jan 2025

Basic Info

Synonyms

hVDAC2, Outer mitochondrial membrane protein porin 2, VDAC-2

+ [3]

Introduction

Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules (By similarity). The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV (By similarity). The open state has a weak anion selectivity whereas the closed state is cation-selective (By similarity). Binds various lipids, including the sphingolipid ceramide, the phospholipid phosphatidylcholine, and the sterol cholesterol (PubMed:31015432). Binding of ceramide promotes the mitochondrial outer membrane permeabilization (MOMP) apoptotic pathway (PubMed:31015432).

Drugs associated with VDAC2

Erastin

Target

SLC7A11 x VDAC1 x VDAC2 x VDAC3 x p53

Mechanism

SLC7A11 modulators [+4]

Active Org.

Prolexys Pharmaceuticals, Inc. [+1]

Originator Org.-

Active Indication

Mutation related cancer [+1]

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

WEHI-9625

Target

VDAC2

Mechanism

VDAC2 agonists

Active Org.

The Walter & Eliza Hall Institute of Medical Research

Originator Org.

The Walter & Eliza Hall Institute of Medical Research

Active Indication

Neoplasms

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with VDAC2

100 Translational Medicine associated with VDAC2

0 Patents (Medical) associated with VDAC2

368

Literatures (Medical) associated with VDAC2

01 Mar 2025·Theriogenology

Isoglycyrrhizin supplementation of frozen goat semen-extender improves post-thaw sperm quality and in vitro fertilization rates

Article

Author: Wu, Caifeng ; Gao, Jun ; Xu, Jiehuan ; Liu, Fuqin ; Shen, Haoxing ; Dai, Jianjun ; He, Mengqian ; Zhu, Huibin ; Luo, Feng ; Sun, Lingwei

This study examined the effect of supplementation of freezing extender with isoglycyrrhizin (ISL), a natural antioxidant agent, on the quality and fertility potential of goat spermatozoa after cryopreservation. Forty ejaculates were collected from eight Chongming White rams and diluted with five concentrations of ISL: 0 (control group), 50, 100, 150, and 200 μg/mL. The quality, motility parameters, antioxidant properties, mRNA expression of antioxidant and ferroptosis genes, and ability to induce fertilization, were evaluated following freezing/thawing. Total motility and progressive motility were significantly increased in spermatozoa following the addition of 150 and 200 μg/mL ISL. Superoxide dismutase (SOD), glutathione peroxidase (GSH-Px), and catalase (CAT) activities were enhanced in all ISL-supplemented groups compared to controls. Adding ISL decreased the levels of reactive oxygen species (ROS), malondialdehyde (MDA) and nitric oxide (NO). mRNA levels of ferroptosis-related genes, voltage-dependent anion channel protein 2 (VDAC2), voltage-dependent anion channel protein 3 (VDAC3), protein 53 (P53), and nuclear factor erythroid 2-related factor 2 (NRF2) tended to decrease after adding ISL, whereas the levels of antioxidant genes glutathione peroxidase 4 (GPX4) and glutathione peroxidase 4 (GPX5), tended to increase. The best spermatozoa quality and the strongest antioxidant properties were obtained after adding 150 μg/mL ISL. Therefore, fresh semen, frozen semen, and frozen semen with 150 μg/mL ISL was used for in vitro fertilization of oocytes. The cleavage and blastocyst rates were significantly lower in frozen semen compared with fresh semen, whereas frozen semen containing 150 μg/mL ISL showed a significant increase in cleavage and blastocyst rates compared with frozen semen. In conclusion, ISL can be used as an antioxidant in goat semen cryodilution, and the addition of ISL can improve the quality and antioxidant properties of frozen and thawed spermatozoa. ISL can also protect the ability of spermatozoa to be fertilized and develop; 150 μg/mL ISL was the optimal concentration for addition.

01 Jan 2025·International Journal of Biological Macromolecules

VRK2 inhibits the replication of infectious bursal disease virus by phosphorylating RACK1 and suppressing apoptosis

Article

Author: Han, Shichong ; Wan, Bo ; Lin, Wencheng ; Pan, Xiao-Ya ; Ma, Yu-He ; Ren, Haojie ; Shao, Han-Cheng ; Zhang, Yuhang ; Zi, Meng-Hui ; Liang, Zhi-Shan ; Shi, Lan-Fang ; He, Wen-Rui ; Yuan, Jin

Infectious bursal disease (IBD) is an acute, highly contagious, and immunosuppressive avian disease caused by the infectious bursal disease virus (IBDV). Despite significant efforts, the lack of knowledge about host proteins that counteract IBDV replication has hindered progress in preventing and controlling IBD in chickens. This study identifies the mitochondria-associated protein vaccinia virus-related kinase 2 (VRK2) as an inhibitor of IBDV. Overexpression of VRK2 significantly reduced IBDV proliferation in DF-1 cells and chicken embryo fibroblasts (CEFs). Conversely, the absence of VRK2 resulted in higher viral loads in these cells. Additionally, we found that VRK2 interacts with voltage-dependent anion channel 2 (VDAC2) and Receptor for Activated C Kinase 1 (RACK1). Mechanistic studies revealed that VRK2 inhibits IBDV-induced apoptosis by targeting RACK1 phosphorylation, leading to reduced viral growth. This study enhances our understanding of VRK2's role in host anti-apoptotic mechanisms and offers novel insights into IBDV pathogenesis and vaccine development.

01 Jan 2025·International Journal of Biological Macromolecules

GCRV-II major outer capsid protein VP4 promotes cell apoptosis by VDAC2-mediated calcium pathway facilitation

Article

Author: Hu, Chengyu ; Liu, Yulong ; Xu, Xiaowen ; Mao, Huiling ; Zhang, Qin ; Tan, Libo ; Zhao, Kaiwen ; Yin, Zijia ; Xu, Pengxia ; Juario, Ming ; Zhang, Hongying ; Wang, Shanghong ; Zhao, Guannan ; Zhang, Yansong

Grass Carp Reovirus (GCRV) is widely concerned because of its widespread prevalence and high mortality to grass carp (Ctenopharyngodon idellus). Viral protein 4 (VP4) is an important major outer capsid protein of GCRV and is involved in the regulation of cell cycle and cycle of GCRV replication. However, the elaborate function of VP4 remains to be explicated. To understand its function, we screened the transcriptome of Ctenopharyngodon idellus kidney (CIK) cells transfected with VP4 and found that VP4 may be involved in regulation of ion transmembrane transporter activity and calcium signaling pathway. It was observed through transmission electron microscopy and confocal microscopy. VP4 causes endoplasmic reticulum (ER) stress and leads to abnormal Calcium ions (Ca²⁺) concentration in cells. Also, VP4 promoted the loss of mitochondrial membrane potential, which allowed a large amount of Ca²⁺ to enter mitochondria and led to mitochondrial damage and apoptosis. In this transcriptome, we found that voltage-dependent anion channel 2 (VDAC2) was significantly upregulated. Moreover, the results also showed that the expression of C.idellus voltage-dependent anion channel 2 (CiVDAC2) and the degree of cell apoptosis were increased along with the increase of VP4 transfection. In contrast, knockdown of CiVDAC2 can reduce the concentration of Ca²⁺ and the occurrence of apoptosis caused by VP4 transfection. In conclusion, the results demonstrated that VP4 can induce cell apoptosis through VDAC2-mediated calcium pathway facilitation. This study provides some insights for the prevention and treatment of GCRV infection in grass carp.

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VDAC2

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