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박명수,전병화,김척승,주희경,이유란,강건,김수진,최성아,이상도,박진봉,김국성 한국분자세포생물학회 2013 Molecules and cells Vol.36 No.5
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 un-known. We investigated the role of cytoplasmic APE1/Ref-1 on tumor necrosis factor-alpha (TNF-alpha)-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-alpha. Cytoplasmic APE1/ Ref-1 expression was not blunted by cycloheximide, a protein synthesis inhibitor, suggesting cytoplasmic trans-location of APE1/Ref-1. Transfection of an N-terminus deletion mutant APE1/Ref-1(29-318) inhibited TNF-alpha-induced VCAM-1 expression, indicating an anti-inflam- matory role for APE1/Ref-1 in the cytoplasm. In contrast, redox mutant of APE1/Ref-1 (C65A/C93A) transfection led to increased TNF-alpha-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-inflam-matory activity in endothelial cells.
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