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Mitochondrial ATP synthase is a target for TNBS‐induced protein carbonylation in XS‐106 dendritic cells
Author(s) -
Je Jeong Hwan,
Lee Tae Hyung,
Kim Dong Hyun,
Cho Young Hun,
Lee Ju Hee,
Kim Soo Chan,
Lee SangKyou,
Lee Jaewon,
Lee MinGeol
Publication year - 2008
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200700962
Subject(s) - protein carbonylation , carbonylation , chemistry , oxidative stress , glutathione , atp synthase , reactive oxygen species , biochemistry , oxidative phosphorylation , myeloperoxidase , mitochondrial ros , immunology , biology , enzyme , inflammation , catalysis , carbon monoxide
ROS are produced in dendritic cells (DCs) during antigen presentation in contact hypersensitivity (CHS). As a result, ROS cause a number of nonenzymatic protein modifications, including carbonylation, which is the most widely used marker of oxidative stress. 2,4,6‐Trinitrobenzene sulfonic acid (TNBS) is a well‐characterized contact allergen that results in the formation of ROS. However, proteins that are carbonylated in DCs in response to TNBS have not been identified. To study ROS‐dependent protein carbonylation in response to TNBS, we used the well‐established mouse DC line, XS‐106. We focused on the effects of TNBS on oxidation by examining selected oxidative markers. We identified TNBS‐induced ROS and myeloperoxidase (MPO) proteins and demonstrated that the increase in ROS resulted in IL‐12 production. The increase in oxidation was further confirmed by an oxidation‐dependent increase in protein modifications, such as carbonylation. In fact, TNBS strongly induced carbonylation of mitochondrial adenosine triphosphate (ATP) synthase in XS‐106 DCs, as determined by MALDI‐TOF analysis and 2‐D Western blotting. ROS production and protein carbonylation were confirmed in human monocyte‐derived DCs (Mo‐DCs). Furthermore, glutathione (GSH) decreased ROS and protein carbonylation in Mo‐DCs. Carbonylation of ATP synthase in DCs may contribute to the pathophysiology of CHS.