A genetic analysis of the porin gene encoding a voltage-dependent anion channel protein in Drosophila melanogaster

2002 ◽  
Vol 267 (6) ◽  
pp. 746-756 ◽  
Author(s):  
M. Oliva ◽  
V. De Pinto ◽  
P. Barsanti ◽  
C. Caggese
Keyword(s):  
Drosophila Melanogaster ◽  
Genetic Analysis ◽  
Anion Channel ◽  
Voltage Dependent Anion Channel ◽  
Gene Encoding ◽  
Channel Protein ◽  
Voltage Dependent

A comparative study of the porin genes encoding VDAC, a voltage-dependent anion channel protein, in Anopheles gambiae and Drosophila melanogaster

Gene ◽  
2003 ◽  
Vol 317 ◽  
pp. 111-115 ◽  
Author(s):  
Marco Sardiello ◽  
Gaetano Tripoli ◽  
Marta Oliva ◽  
Federica Santolamazza ◽  
Roberta Moschetti ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Comparative Study ◽  
Anopheles Gambiae ◽  
Anion Channel ◽  
Voltage Dependent Anion Channel ◽  
Channel Protein ◽  
Voltage Dependent ◽  
Genes Encoding

Effects of a mutation in theDrosophila porin gene encoding mitochondrial voltage-dependent anion channel protein on phototransduction

2007 ◽  
Vol 67 (11) ◽  
pp. 1533-1545 ◽  
Author(s):  
Sunji Lee ◽  
Hung-Tat Leung ◽  
Eunju Kim ◽  
Jeyoun Jang ◽  
Eunsung Lee ◽  
...  
Keyword(s):  
Anion Channel ◽  
Voltage Dependent Anion Channel ◽  
Gene Encoding ◽  
Channel Protein ◽  
Voltage Dependent

scholarly journals Effects of a mutation in theDrosophila porin gene encoding mitochondrial voltage-dependent anion channel protein on phototransduction

2007 ◽  
Vol 67 (12) ◽  
pp. 1686-1686
Author(s):  
Sunji Lee ◽  
Hung-Tat Leung ◽  
Eunju Kim ◽  
Jeyoun Jang ◽  
Eunsung Lee ◽  
...  
Keyword(s):  
Anion Channel ◽  
Voltage Dependent Anion Channel ◽  
Gene Encoding ◽  
Channel Protein ◽  
Voltage Dependent

Proteomic approach to the identification of voltage-dependent anion channel protein isoforms in guinea pig brain synaptosomes

PROTEOMICS ◽  
2004 ◽  
Vol 4 (5) ◽  
pp. 1335-1340 ◽  
Author(s):  
Sabrina Liberatori ◽  
Benito Canas ◽  
Chiara Tani ◽  
Luca Bini ◽  
Giuseppe Buonocore ◽  
...  
Keyword(s):  
Guinea Pig ◽  
Anion Channel ◽  
Protein Isoforms ◽  
Voltage Dependent Anion Channel ◽  
Channel Protein ◽  
Pig Brain ◽  
Proteomic Approach ◽  
Brain Synaptosomes ◽  
Voltage Dependent ◽  
Guinea Pig Brain

scholarly journals Voltage-Dependent Anion Channel Protein 2 (VDAC2) and Receptor of Activated Protein C Kinase 1 (RACK1) Act as Functional Receptors for Lymphocystis Disease Virus Infection

2019 ◽  
Vol 93 (12) ◽  
Author(s):  
Ying Zhong ◽  
Xiaoqian Tang ◽  
Xiuzhen Sheng ◽  
Jing Xing ◽  
Wenbin Zhan
Keyword(s):  
Disease Virus ◽  
Protein C ◽  
Polyclonal Antibodies ◽  
Activated Protein C ◽  
Anion Channel ◽  
Voltage Dependent Anion Channel ◽  
Lymphocystis Disease Virus ◽  
Channel Protein ◽  
Lymphocystis Disease ◽  
Voltage Dependent

ABSTRACTIn previous research, a 27.8-kDa protein in flounderParalichthys olivaceusgill (FG) cells was identified as a putative cellular receptor (27.8R), which mediated lymphocystis disease virus (LCDV) infection via interaction with a 32-kDa viral attachment protein (VAP) of LCDV, and monoclonal antibodies (MAbs) against 27.8R and 32-kDa VAP were developed. In this study, the 27.8R was identified as voltage-dependent anion channel protein 2 (VDAC2) and receptor of activated protein C kinase 1 (RACK1) of flounder. Recombinant VDAC2 (rVDAC2) and RACK1 (rRACK1) were obtained by prokaryotic expression, and rabbit anti-VDAC2/RACK1 polyclonal antibodies were prepared. The rVDAC2, rRACK1, and 27.8-kDa proteins in FG cells were recognized by anti-27.8R MAbs and anti-VDAC2/RACK1 polyclonal antibodies simultaneously. Preincubation of FG cells with anti-VDAC2/RACK1 polyclonal antibodies significantly decreased the percentages of LCDV-infected cells and LCDV copy numbers, blocked virus infection, and delayed the development of cytopathic effect. The mRNA expressions of VDAC2 and RACK1 in FG cells were upregulated to maximum levels 12 h and 48 h after LCDV infection, respectively. VDAC2/RACK1 knockdown through short interfering RNA (siRNA) significantly reduced VDAC2/RACK1 expression and LCDV copy numbers in FG cells compared with negative controls, while VDAC2/RACK1 expression on LCDV-nonpermissive epithelial papillosum cells (EPCs) conferred susceptibility to LCDV infection, indicating the VDAC2 and RACK1 were sufficient to allow LCDV entry and infection. All these results collectively showed that VDAC2 and RACK1 function as receptors for LCDV entry and infection.IMPORTANCELymphocystis disease virus (LCDV) is the causative agent of lymphocystis disease in fish, which has caused huge economic losses to the aquaculture industry worldwide, but the molecular mechanism underlying the LCDV-host interaction remains unclear. Here, the 27.8-kDa putative cellular receptor for LCDV was identified as voltage-dependent anion channel protein 2 (VDAC2) and receptor of activated protein C kinase 1 (RACK1), and our results revealed that VDAC2 and RACK1 expression was sufficient to allow LCDV entry and that they are functional receptors that initiate LCDV infection for the first time, which leads to a better understanding of the molecular mechanism underlying LCDV infection and virus-host interactions.

scholarly journals VDAC1 in the diseased myocardium and the effect of VDAC1-interacting compound on atrial fibrosis induced by hyperaldosteronism

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Hadar Klapper-Goldstein ◽  
Ankit Verma ◽  
Sigal Elyagon ◽  
Roni Gillis ◽  
Michael Murninkas ◽  
...  
Keyword(s):  
Myocardial Infarction ◽  
Apoptotic Cell ◽  
Anion Channel ◽  
Immunohistochemical Analysis ◽  
Voltage Dependent Anion Channel ◽  
Cardiac Tissues ◽  
Therapeutic Implications ◽  
Voltage Dependent ◽  
Models Of Lupus

AbstractThe voltage-dependent anion channel 1 (VDAC1) is a key player in mitochondrial function. VDAC1 serves as a gatekeeper mediating the fluxes of ions, nucleotides, and other metabolites across the outer mitochondrial membrane, as well as the release of apoptogenic proteins initiating apoptotic cell death. VBIT-4, a VDAC1 oligomerization inhibitor, was recently shown to prevent mitochondrial dysfunction and apoptosis, as validated in mouse models of lupus and type-2 diabetes. In the present study, we explored the expression of VDAC1 in the diseased myocardium of humans and rats. In addition, we evaluated the effect of VBIT-4 treatment on the atrial structural and electrical remodeling of rats exposed to excessive aldosterone levels. Immunohistochemical analysis of commercially available human cardiac tissues revealed marked overexpression of VDAC1 in post-myocardial infarction patients, as well as in patients with chronic ventricular dilatation\dysfunction. In agreement, rats exposed to myocardial infarction or to excessive aldosterone had a marked increase of VDAC1 in both ventricular and atrial tissues. Immunofluorescence staining indicated a punctuated appearance typical for mitochondrial-localized VDAC1. Finally, VBIT-4 treatment attenuated the atrial fibrotic load of rats exposed to excessive aldosterone without a notable effect on the susceptibility to atrial fibrillation episodes induced by burst pacing. Our results indicate that VDAC1 overexpression is associated with myocardial abnormalities in common pathological settings. Our data also indicate that inhibition of the VDAC1 can reduce excessive fibrosis in the atrial myocardium, a finding which may have important therapeutic implications. The exact mechanism\s of this beneficial effect need further studies.

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