Lipopolysaccharide-Binding Protein Downregulates Fractalkine through Activation of p38 MAPK and NF-κB
Background. LBP and fractalkine are known to be involved in the pathogenesis of ARDS. This study investigated the relationship between LBP and fractalkine in LPS-induced A549 cells and rat lung tissue in an ARDS rat model. Methods. A549 cells were transfected with LBP or LBP shRNA plasmid DNA or pre...
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Wiley
2017-01-01
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Series: | Mediators of Inflammation |
Online Access: | http://dx.doi.org/10.1155/2017/9734837 |
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author | Xia Huang Yi Zeng Yujie Jiang Yueqiu Qin Weigui Luo Shulin Xiang Suren R. Sooranna Liao Pinhu |
author_facet | Xia Huang Yi Zeng Yujie Jiang Yueqiu Qin Weigui Luo Shulin Xiang Suren R. Sooranna Liao Pinhu |
author_sort | Xia Huang |
collection | DOAJ |
description | Background. LBP and fractalkine are known to be involved in the pathogenesis of ARDS. This study investigated the relationship between LBP and fractalkine in LPS-induced A549 cells and rat lung tissue in an ARDS rat model. Methods. A549 cells were transfected with LBP or LBP shRNA plasmid DNA or pretreated with SB203580 or SC-514 following LPS treatment. An ARDS rat model was established using LPS with or without LBPK95A, SB203580, or SC-514 treatment. RT-PCR, western blotting, ELISA, immunofluorescence, coimmunoprecipitation, and immunohistochemical staining were used to study the expression of fractalkine and LBP and p38 MAPK and p65 NF-κB activities. Results. LPS increased LBP and reduced fractalkine. LBP overexpression further decreased LPS-induced downregulation of fractalkine and p38 MAPK and p65 NF-κB activation; LBP gene silencing, SB203580, and SC-514 suppressed LPS-induced downregulation of fractalkine and p38 MAPK and p65 NF-κB activation in A549 cells. LBP and fractalkine in lung tissue were increased and decreased, respectively, following LPS injection. LBPK95A, SB203580, and SC-514 ameliorated LPS-induced rat lung injury and suppressed LPS-induced downregulation of fractalkine by decreasing phospho-p38 MAPK and p65 NF-κB. Conclusions. The results indicate that LBP downregulates fractalkine expression in LPS-induced A549 cells and in an ARDS rat model through activation of p38 MAPK and NF-κB. |
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id | doaj-art-30b94c9e73be480f9ab63fa7b9492009 |
institution | Kabale University |
issn | 0962-9351 1466-1861 |
language | English |
publishDate | 2017-01-01 |
publisher | Wiley |
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series | Mediators of Inflammation |
spelling | doaj-art-30b94c9e73be480f9ab63fa7b94920092025-02-03T06:05:06ZengWileyMediators of Inflammation0962-93511466-18612017-01-01201710.1155/2017/97348379734837Lipopolysaccharide-Binding Protein Downregulates Fractalkine through Activation of p38 MAPK and NF-κBXia Huang0Yi Zeng1Yujie Jiang2Yueqiu Qin3Weigui Luo4Shulin Xiang5Suren R. Sooranna6Liao Pinhu7The First Clinical Medical College of Jinan University, Guangzhou, Guangdong Province 510630, ChinaDepartment of Central Laboratory, Youjiang Medical University for Nationalities, Baise, Guangxi Zhuang Autonomous Region 533000, ChinaThe First Clinical Medical College of Jinan University, Guangzhou, Guangdong Province 510630, ChinaDepartment of Digestive Medicine, Youjiang Medical University for Nationalities, Baise, Guangxi Zhuang Autonomous Region 533000, ChinaDepartment of Respiratory Medicine, Youjiang Medical University for Nationalities, Baise, Guangxi Zhuang Autonomous Region 533000, ChinaThe First Clinical Medical College of Jinan University, Guangzhou, Guangdong Province 510630, ChinaDepartment of Surgery and Cancer, Imperial College London, Chelsea and Westminster Hospital, London SW10 9NH, UKDepartment of Intensive Care Medicine, Youjiang Medical University for Nationalities, Baise, Guangxi Zhuang Autonomous Region 533000, ChinaBackground. LBP and fractalkine are known to be involved in the pathogenesis of ARDS. This study investigated the relationship between LBP and fractalkine in LPS-induced A549 cells and rat lung tissue in an ARDS rat model. Methods. A549 cells were transfected with LBP or LBP shRNA plasmid DNA or pretreated with SB203580 or SC-514 following LPS treatment. An ARDS rat model was established using LPS with or without LBPK95A, SB203580, or SC-514 treatment. RT-PCR, western blotting, ELISA, immunofluorescence, coimmunoprecipitation, and immunohistochemical staining were used to study the expression of fractalkine and LBP and p38 MAPK and p65 NF-κB activities. Results. LPS increased LBP and reduced fractalkine. LBP overexpression further decreased LPS-induced downregulation of fractalkine and p38 MAPK and p65 NF-κB activation; LBP gene silencing, SB203580, and SC-514 suppressed LPS-induced downregulation of fractalkine and p38 MAPK and p65 NF-κB activation in A549 cells. LBP and fractalkine in lung tissue were increased and decreased, respectively, following LPS injection. LBPK95A, SB203580, and SC-514 ameliorated LPS-induced rat lung injury and suppressed LPS-induced downregulation of fractalkine by decreasing phospho-p38 MAPK and p65 NF-κB. Conclusions. The results indicate that LBP downregulates fractalkine expression in LPS-induced A549 cells and in an ARDS rat model through activation of p38 MAPK and NF-κB.http://dx.doi.org/10.1155/2017/9734837 |
spellingShingle | Xia Huang Yi Zeng Yujie Jiang Yueqiu Qin Weigui Luo Shulin Xiang Suren R. Sooranna Liao Pinhu Lipopolysaccharide-Binding Protein Downregulates Fractalkine through Activation of p38 MAPK and NF-κB Mediators of Inflammation |
title | Lipopolysaccharide-Binding Protein Downregulates Fractalkine through Activation of p38 MAPK and NF-κB |
title_full | Lipopolysaccharide-Binding Protein Downregulates Fractalkine through Activation of p38 MAPK and NF-κB |
title_fullStr | Lipopolysaccharide-Binding Protein Downregulates Fractalkine through Activation of p38 MAPK and NF-κB |
title_full_unstemmed | Lipopolysaccharide-Binding Protein Downregulates Fractalkine through Activation of p38 MAPK and NF-κB |
title_short | Lipopolysaccharide-Binding Protein Downregulates Fractalkine through Activation of p38 MAPK and NF-κB |
title_sort | lipopolysaccharide binding protein downregulates fractalkine through activation of p38 mapk and nf κb |
url | http://dx.doi.org/10.1155/2017/9734837 |
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