Hepatitis B virus X protein disrupts stress fiber formation and triggers apoptosis.

THUIR > College of Science > Department of Life Sciences > Periodical Articles > Item 310901/27890

Please use this identifier to cite or link to this item: http://140.128.103.80:8080/handle/310901/27890

Title:	Hepatitis B virus X protein disrupts stress fiber formation and triggers apoptosis.
Authors:	黃光裕 Kuo, Chan-Yen Chou, Tzu-Yu Chen, Chun-Ming Tsai, Yung-Fong Hwang, Guang-Yuh Hwang, Tsong-Long
Contributors:	Chang Gung University Department of Life Science, Tunghai University Department of Anesthesiology, Chang Gung Memorial Hospital
Keywords:	HBx MLCK PTEN Stress-fiber formation Apoptosis
Date:	2013-07
Issue Date:	2016-08-16
Publisher:	荷蘭:Elsevier
Abstract:	Cytoskeletal proteins are key participants in the cellular progression to apoptosis. In a previous study we injected nude mice with CCL13-HBx cells and identified in contrast to non-HBx transfected cells a differentially phosphorylated myosin light chain (p-MLC) by two-dimensional PAGE and mass spectrometry of the tumor material. To investigate the role of HBx in myosin light chain kinase (MLCK) signaling pathways, we analyzed the key molecules, p-MLC and MLCK, by western blotting. Immunofluorescence staining analysis showed that HBx disrupted stress fiber formation and that focal adhesion kinase (FAK) and integrin-linked kinase (ILK) were regulated by HBx-mediated phosphatase and tensin homolog (PTEN). We also used pharmacological inhibitors to explore the correlation between cytoskeletal rearrangements and HBx-mediated cell apoptosis via an MLCK and a PTEN-dependent pathway. The results showed that both ML9 and bvp restored the effects caused by HBx induction. Our findings suggest that HBx disrupts stress fiber formation and triggers apoptosis via an MLCK and a PTEN-dependent pathway.
Relation:	Virus Research, 175(1), 20-29
Appears in Collections:	[Department of Life Sciences ] Periodical Articles

Files in This Item:

File	Description	Size	Format
index.html		0Kb	HTML	168	View/Open

View Licence

Loading...