Characterization and Functional Analysis of Voltage‐Dependent Anion Channel 1 (VDAC1) from Orange‐Spotted Grouper (Epinephelus coioides). Issue 7 (30th May 2014)
- Record Type:
- Journal Article
- Title:
- Characterization and Functional Analysis of Voltage‐Dependent Anion Channel 1 (VDAC1) from Orange‐Spotted Grouper (Epinephelus coioides). Issue 7 (30th May 2014)
- Main Title:
- Characterization and Functional Analysis of Voltage‐Dependent Anion Channel 1 (VDAC1) from Orange‐Spotted Grouper (Epinephelus coioides)
- Authors:
- Shi, Yan
Zhao, Zhe
Hong, Xiaoyou
Chen, Kunci
Zhu, Xinping - Abstract:
- <abstract abstract-type="main"> <title>ABSTRACT</title> <p>The voltage‐dependent anion channel (VDAC) is a highly conserved integral protein of mitochondria in different eukaryotic species. It forms a selective channel in the mitochondrial outer membrane that serves as the controlled pathway for small metabolites and ions. In this study, a <italic>VDAC</italic> gene, <italic>EcVDAC1</italic>, was isolated from orange‐spotted grouper (<italic>Epinephelus coioides</italic>). The <italic>EcVDAC1</italic> exhibits ubiquitous expression in various tissues of orange‐spotted grouper and is upregulated in liver, gill, and spleen after stimulation with lipopolysaccharides (LPS). Subcellular localization analysis shows that the <italic>Ec</italic>VDAC1 protein colocalized with the mitochondria. A caspase‐3 assay demonstrates that overexpression of the <italic>EcVDAC1</italic> induced apoptotic cell death in fathead minnow cells. The data presented in this study provide new information regarding the relationship between LPS and the <italic>EcVDAC1</italic> gene, suggesting that the fish <italic>VDAC1</italic> gene may play an important role in antibacterial immune response.</p> </abstract>
- Is Part Of:
- Journal of biochemical and molecular toxicology. Volume 28:Issue 7(2014:Jul.)
- Journal:
- Journal of biochemical and molecular toxicology
- Issue:
- Volume 28:Issue 7(2014:Jul.)
- Issue Display:
- Volume 28, Issue 7 (2014)
- Year:
- 2014
- Volume:
- 28
- Issue:
- 7
- Issue Sort Value:
- 2014-0028-0007-0000
- Page Start:
- 292
- Page End:
- 301
- Publication Date:
- 2014-05-30
- Subjects:
- Biochemistry -- Periodicals
Molecular biology -- Periodicals
Toxicology -- Periodicals
574 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1099-0461 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/jbt.21565 ↗
- Languages:
- English
- ISSNs:
- 1095-6670
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 4951.650000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 3675.xml