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Int. J. Mol. Sci. 2015, 16(11), 26871-26879; doi:10.3390/ijms161125994

Identification of Arsenic Direct-Binding Proteins in Acute Promyelocytic Leukaemia Cells

1,†
,
2,†
,
3
,
3,4,* and 5,*
1
Department of Laboratory Medicine, Huashan Hospital, Fudan University, 12 Central Urumqi Road, Shanghai 200040, China
2
Shanghai Cancer Center and Key Laboratory of Glycoconjugates Research Ministry of Public Health, Fudan University, Shanghai 200032, China
3
State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, University of Chinese Academy of Sciences, 320 Yueyang Road, Shanghai 200031, China
4
Cancer Research Center, SIBS-Xuhui Central Hospital, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, 320 Yueyang Road, Shanghai 200031, China
5
Department of Hematology, Huashan Hospital, Fudan University, Shanghai 200040, China
These authors contributed equally to this work.
*
Authors to whom correspondence should be addressed.
Academic Editor: Kaixun Huang
Received: 7 July 2015 / Revised: 23 October 2015 / Accepted: 30 October 2015 / Published: 10 November 2015
(This article belongs to the Special Issue Applied Bioinorganic Chemistry and Selected Papers from 13th ISABC)
View Full-Text   |   Download PDF [1265 KB, uploaded 10 November 2015]   |  

Abstract

The identification of arsenic direct-binding proteins is essential for determining the mechanism by which arsenic trioxide achieves its chemotherapeutic effects. At least two cysteines close together in the amino acid sequence are crucial to the binding of arsenic and essential to the identification of arsenic-binding proteins. In the present study, arsenic binding proteins were pulled down with streptavidin and identified using a liquid chromatograph-mass spectrometer (LC-MS/MS). More than 40 arsenic-binding proteins were separated, and redox-related proteins, glutathione S-transferase P1 (GSTP1), heat shock 70 kDa protein 9 (HSPA9) and pyruvate kinase M2 (PKM2), were further studied using binding assays in vitro. Notably, PKM2 has a high affinity for arsenic. In contrast to PKM2, GSTP1and HSPA9 did not combine with arsenic directly in vitro. These observations suggest that arsenic-mediated acute promyelocytic leukaemia (APL) suppressive effects involve PKM2. In summary, we identified several arsenic binding proteins in APL cells and investigated the therapeutic mechanisms of arsenic trioxide for APL. Further investigation into specific signal pathways by which PKM2 mediates APL developments may lead to a better understanding of arsenic effects on APL. View Full-Text
Keywords: arsenic-binding protein; arsenic-biotin; acute promyelocytic leukaemia; LC-MS/MS; pyruvate kinase M2 arsenic-binding protein; arsenic-biotin; acute promyelocytic leukaemia; LC-MS/MS; pyruvate kinase M2
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Zhang, T.; Lu, H.; Li, W.; Hu, R.; Chen, Z. Identification of Arsenic Direct-Binding Proteins in Acute Promyelocytic Leukaemia Cells. Int. J. Mol. Sci. 2015, 16, 26871-26879.

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