HSP90β interacts with Rac1 to activate NADPH oxidase in Helicobacter pylori-infected gastric epithelial cells

Boram Cha; Joo Weon Lim; Kyung Hwan Kim; Hyeyong Kim

doi:10.1016/j.biocel.2010.04.015

HSP90β interacts with Rac1 to activate NADPH oxidase in Helicobacter pylori-infected gastric epithelial cells

Boram Cha, Joo Weon Lim, Kyung Hwan Kim, Hyeyong Kim

Department of Food and Nutrition

Research output: Contribution to journal › Article › peer-review

29 Citations (Scopus)

Abstract

Reactive oxygen species (ROS) are involved in the pathogenesis of Helicobacter pylori (H. pylori)-induced gastric disorders including inflammation. NADPH oxidase has been considered as a major source of ROS in phagocytic and non-phagocytic cells. Small G protein Rac1 is one components of NADPH oxidase complex. Heat shock protein 90kDa (HSP90) modulates cytokine production in H. pylori-infected gastric epithelial cells. The present study aims to investigate the relation of HSP90β and Rac1 on the activation of NADPH oxidase in H. pylori-infected gastric epithelial cells. As a result, H. pylori-induced translocation of HSP90β from the cytosol to the membrane and activated Rac1 in gastric epithelial AGS cells. HSP90β physically interacted with Rac1, which resulted in the activation of NADPH oxidase in H. pylori-infected AGS cells. Down-regulation of HSP90β by transfection of HSP90β siRNA suppressed the activation of Rac1, activity of NADPH oxidase and the production of H₂O₂ in H. pylori-infected AGS cells. In conclusion, H. pylori induces the translocation of HSP90β from the cytosol to the membrane and interaction of HSP90β and Rac1, which leads to the activation of NADPH oxidase and production of ROS in gastric epithelial cells. HSP90β may be the target molecule for treatment of H. pylori-induced gastric injury.

Original language	English
Pages (from-to)	1455-1461
Number of pages	7
Journal	International Journal of Biochemistry and Cell Biology
Volume	42
Issue number	9
DOIs	https://doi.org/10.1016/j.biocel.2010.04.015
Publication status	Published - 2010 Sept

Bibliographical note

Funding Information:
This study was supported by Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education, Science and Technology (R11-2007-040-01002-0) and a grant (Joint Research Project under the Korea-Japan Basic Scientific Cooperation Program) from NRF (F01-2009-000-10101-0). H. Kim is grateful to the Brain Korea 21 Project, college of Human Ecology, Yonsei University.

All Science Journal Classification (ASJC) codes

Biochemistry
Cell Biology

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10.1016/j.biocel.2010.04.015

Cite this

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title = "HSP90β interacts with Rac1 to activate NADPH oxidase in Helicobacter pylori-infected gastric epithelial cells",

abstract = "Reactive oxygen species (ROS) are involved in the pathogenesis of Helicobacter pylori (H. pylori)-induced gastric disorders including inflammation. NADPH oxidase has been considered as a major source of ROS in phagocytic and non-phagocytic cells. Small G protein Rac1 is one components of NADPH oxidase complex. Heat shock protein 90kDa (HSP90) modulates cytokine production in H. pylori-infected gastric epithelial cells. The present study aims to investigate the relation of HSP90β and Rac1 on the activation of NADPH oxidase in H. pylori-infected gastric epithelial cells. As a result, H. pylori-induced translocation of HSP90β from the cytosol to the membrane and activated Rac1 in gastric epithelial AGS cells. HSP90β physically interacted with Rac1, which resulted in the activation of NADPH oxidase in H. pylori-infected AGS cells. Down-regulation of HSP90β by transfection of HSP90β siRNA suppressed the activation of Rac1, activity of NADPH oxidase and the production of H2O2 in H. pylori-infected AGS cells. In conclusion, H. pylori induces the translocation of HSP90β from the cytosol to the membrane and interaction of HSP90β and Rac1, which leads to the activation of NADPH oxidase and production of ROS in gastric epithelial cells. HSP90β may be the target molecule for treatment of H. pylori-induced gastric injury.",

author = "Boram Cha and Lim, {Joo Weon} and Kim, {Kyung Hwan} and Hyeyong Kim",

note = "Funding Information: This study was supported by Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education, Science and Technology (R11-2007-040-01002-0) and a grant (Joint Research Project under the Korea-Japan Basic Scientific Cooperation Program) from NRF (F01-2009-000-10101-0). H. Kim is grateful to the Brain Korea 21 Project, college of Human Ecology, Yonsei University.",

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AU - Cha, Boram

AU - Lim, Joo Weon

AU - Kim, Kyung Hwan

AU - Kim, Hyeyong

N1 - Funding Information: This study was supported by Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education, Science and Technology (R11-2007-040-01002-0) and a grant (Joint Research Project under the Korea-Japan Basic Scientific Cooperation Program) from NRF (F01-2009-000-10101-0). H. Kim is grateful to the Brain Korea 21 Project, college of Human Ecology, Yonsei University.

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N2 - Reactive oxygen species (ROS) are involved in the pathogenesis of Helicobacter pylori (H. pylori)-induced gastric disorders including inflammation. NADPH oxidase has been considered as a major source of ROS in phagocytic and non-phagocytic cells. Small G protein Rac1 is one components of NADPH oxidase complex. Heat shock protein 90kDa (HSP90) modulates cytokine production in H. pylori-infected gastric epithelial cells. The present study aims to investigate the relation of HSP90β and Rac1 on the activation of NADPH oxidase in H. pylori-infected gastric epithelial cells. As a result, H. pylori-induced translocation of HSP90β from the cytosol to the membrane and activated Rac1 in gastric epithelial AGS cells. HSP90β physically interacted with Rac1, which resulted in the activation of NADPH oxidase in H. pylori-infected AGS cells. Down-regulation of HSP90β by transfection of HSP90β siRNA suppressed the activation of Rac1, activity of NADPH oxidase and the production of H2O2 in H. pylori-infected AGS cells. In conclusion, H. pylori induces the translocation of HSP90β from the cytosol to the membrane and interaction of HSP90β and Rac1, which leads to the activation of NADPH oxidase and production of ROS in gastric epithelial cells. HSP90β may be the target molecule for treatment of H. pylori-induced gastric injury.

AB - Reactive oxygen species (ROS) are involved in the pathogenesis of Helicobacter pylori (H. pylori)-induced gastric disorders including inflammation. NADPH oxidase has been considered as a major source of ROS in phagocytic and non-phagocytic cells. Small G protein Rac1 is one components of NADPH oxidase complex. Heat shock protein 90kDa (HSP90) modulates cytokine production in H. pylori-infected gastric epithelial cells. The present study aims to investigate the relation of HSP90β and Rac1 on the activation of NADPH oxidase in H. pylori-infected gastric epithelial cells. As a result, H. pylori-induced translocation of HSP90β from the cytosol to the membrane and activated Rac1 in gastric epithelial AGS cells. HSP90β physically interacted with Rac1, which resulted in the activation of NADPH oxidase in H. pylori-infected AGS cells. Down-regulation of HSP90β by transfection of HSP90β siRNA suppressed the activation of Rac1, activity of NADPH oxidase and the production of H2O2 in H. pylori-infected AGS cells. In conclusion, H. pylori induces the translocation of HSP90β from the cytosol to the membrane and interaction of HSP90β and Rac1, which leads to the activation of NADPH oxidase and production of ROS in gastric epithelial cells. HSP90β may be the target molecule for treatment of H. pylori-induced gastric injury.

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HSP90β interacts with Rac1 to activate NADPH oxidase in Helicobacter pylori-infected gastric epithelial cells

Abstract

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