Characterization of the role of protein-cysteine residues in the binding with sodium arsenite

Please use this identifier to cite or link to this item: https://ir.lib.ncu.edu.tw/handle/987654321/100274

Title:	Characterization of the role of protein-cysteine residues in the binding with sodium arsenite
Authors:	侯敦仁;Chang, Yu-Ying;Kuo, Tai-Chih;Hsu, Chun-Hua;Hou, Duen-Ren;Kao, Yung-Hsi;Huang, Rong-Nan
Contributors:	理學院化學學系
Keywords:	Animals;Arsenic;Arsenic - metabolism;Arsenic - toxicity;Arsenites - metabolism;Binding sites;Biomedical and Life Sciences;Biomedicine;Calcium-Binding Proteins - metabolism;Carrier Proteins - metabolism;Cell Line - metabolism;Cellular biology;Chemical compounds;Cricetinae;Cricetulus;Cysteine - metabolism;Environmental Health;Escherichia coli;Female;Heat shock proteins;Heat-Shock Proteins - drug effects;Heat-Shock Proteins - metabolism;Inorganic Compounds;Occupational Medicine/Industrial Medicine;Ovary - cytology;Ovary - metabolism;Pharmacology/Toxicology;Protein Binding - drug effects;Sodium Compounds - metabolism;Toxicity
Date:	2012-06-01
Issue Date:	2026-04-21 13:56:03 (UTC+8)
Publisher:	Springer Verlag;Berlin/Heidelberg: Springer-Verlag
Abstract:	摘要： To better characterize the interaction of protein–cysteines with sodium arsenite, arsenic-binding proteins were identified from the arsenic-resistant Chinese hamster ovary cell line SA7 using a p -aminophenylarsine oxide (PAO)-agarose matrix in combination with proteomic techniques. Twenty of the isolated arsenic-binding proteins were further peptide-mapped by MALDI-Q-TOF-MS. The binding capacity of PAO-agarose-retained proteins was then verified by re-applying Escherichia coli overexpressed recombinant proteins with various numbers of cysteine residues onto the PAO-agarose matrix. The results showed that recombinant heat shock protein 27 (HSP27, with one cysteine residue), reticulocalbin-3 (RCN3, with no cysteine residue), galectin-1 (GAL1, with six cysteine residues), but not peroxiredoxin 6 (Prdx6, with one cysteine residue but not retained by the PAO-agarose matrix), were bound to the PAO-agarose matrix. The six free cysteine residues in GAL1 were individually or double-mutated to alanine by means of site-directed mutagenesis and subjected to CD and ICP-MS analysis. The binding capacity of GAL1 for sodium arsenite was significantly attenuated in C16A, C88A and all double mutant clones. Taken together, our current data suggest that the cysteine residues in GAL1 may play a critical role in the binding of arsenic, but that in the case of RCN3 and Prdx6, this interaction may be mediated by other factors. 其他題名： Arch Toxicol 出版者： Berlin/Heidelberg: Springer-Verlag 出版日期： 2012-06 出處： Archives of toxicology, 2012-06, Vol.86 (6), p.911-922 資源來源： Agricultural & Environmental Science Collection 版權： Springer-Verlag 2012 識別號： ISSN: 0340-5761 識別號： ISSN: 1432-0738 識別號： EISSN: 1432-0738 識別號： DOI: 10.1007/s00204-012-0828-0 識別號： PMID: 22422341
Appears in Collections:	[Department of Chemistry] journal & Dissertation

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