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KMID : 0578320130360050439
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Molecules and Cells
2013 Volume.36 No. 5 p.439 ~ p.445
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Cytoplasmic Localization and Redox Cysteine Residue of APE1/Ref-1 Is Associated with Anti-Inflammatory Activity in Cultured Endothelial Cells
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Park Myoung-Soo
Kim Cuk-Seong
Joo Hee-Kyoung
Lee Yu-Ran
Kang Gun
Kim Soo-Jin
Choi Sun-Ga
Lee Sang-Do
Park Jin-Bong
Jeon Byeong-Hwa
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Abstract
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Apurinic/apyrimidinic endonuclease1/redox factor-1 (APE1/Ref-1) is a multifunctional protein involved in base excision DNA repair and transcriptional regulation of gene expression. APE1/Ref-1 is mainly localized in the nucleus, but cytoplasmic localization has also been reported. However, the functional role of cytoplasmic APE1/Ref-1 and its redox cysteine residue are still unknown. We investigated the role of cytoplasmic APE1/Ref-1 on tumor necrosis factor-α (TNF-α)-induced vascular cell adhesion molecule-1 (VCAM-1) expressions in endothelial cells. Endogenous APE1/Ref-1 was mainly observed in the nucleus, however, cytoplasmic APE1/Ref-1 was increased by TNF-α. Cytoplasmic APE1/Ref-1 expression was not blunted by cycloheximide, a protein synthesis inhibitor, suggesting cytoplasmic translocation of APE1/Ref-1. Transfection of an N-terminus deletion mutant APE1/Ref-1(29-318) inhibited TNF-α-induced VCAM-1 expression, indicating an anti-inflammatory role for APE1/Ref-1 in the cytoplasm. In contrast, redox mutant of APE1/Ref-1 (C65A/C93A) transfection led to increased TNF-α-induced VCAM-1 expression. Our findings suggest cytoplasmic APE1/Ref-1 localization and redox cysteine residues of APE1/Ref-1 are associated with its anti-inflammatory activity in endothelial cells.
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KEYWORD
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APE1/Ref-1, endothelial cells, TNF-α, VCAM-1
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