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- Title
Activation of p38 MAPK Pathway by Hepatitis C Virus E2 in Cells Transiently Expressing DC-SIGN.
- Authors
Qiu-Li Chen; Shi-Ying Zhu; Zhong-Qi Bian; Lan-Juan Zhao; Jie Cao; Wei Pan; Zhong-Tian Qi
- Abstract
Abstract Dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN) is a cellular receptor for hepatitis C virus for the binding of viral envelope glycoprotein E2. Interaction of DC-SIGN with the E2 may evoke cellular signal transduction implicated in viral pathogenesis. We developed a cell model with DC-SIGN transient transfection to study p38 mitogen-activated protein kinase (MAPK) signaling pathway in response to the E2 treatment. HEK293T and HeLa were DC-SIGN-deficient cell lines. DC-SIGN was detectable at the surface of HEK293T and HeLa transfected with DC-SIGN, and the levels of DC-SIGN were high in transfected-HEK293T as compared with HeLa. The transfected-HEK293T displayed ability for the E2 binding. In the transfected-HEK293T, level of p38 MAPK phosphorylation was increased upon the E2 treatment and reduced following blockage of DC-SIGN with an antibody against DC-SIGN. Phosphorylation of downstream transcription factor activating transcription factor (ATF)-2 was also up-regulated by the E2 via DC-SIGN. Similar results were obtained with NIH3T3 cells stably expressing DC-SIGN and Huh7 cells. Our results indicate that DC-SIGN transient expression in HEK293T is a useful cell model for investigating p38 MAPK pathway triggered by the E2, which may provide information for understanding cellular receptors-mediated signaling events and the viral pathogenesis.
- Subjects
MITOGEN-activated protein kinases; ENZYME activation; HEPATITIS C virus; GENE transfection; CELL adhesion molecules; GLYCOPROTEINS; CELLULAR signal transduction; GENE expression
- Publication
Cell Biochemistry & Biophysics, 2010, Vol 56, Issue 1, p49
- ISSN
1085-9195
- Publication type
Article
- DOI
10.1007/s12013-009-9069-0