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Candidate Single Nucleotide Polymorphism Markers for Arsenic Responsiveness of Protein Targets
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Candidate Single Nucleotide Polymorphism Markers for Arsenic Responsiveness of Protein Targets
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Journal Article
Candidate Single Nucleotide Polymorphism Markers for Arsenic Responsiveness of Protein Targets
2010
Overview
Raphael D. Isokpehi1,2, Hari H.P. Cohly1,2, Matthew N. Anyanwu2,3, Rajendram V. Rajnarayanan4, Paul B. Tchounwou1, Udensi K. Udensi1,2 and Barbara E. Graham-Evans11RCMI-Center for Environmental Health, College of Science, Engineering and Technology, Jackson State University, Jackson, Mississippi 39217, USA. 2Center for Bioinformatics & Computational Biology, Department of Biology, Jackson State University, PO Box 18540, Jackson, Mississippi 39217, USA. 3Department of Computer Science, University of Memphis, Memphis Tennessee, USA. 4Department of Pharmacology and Toxicology, State University of New York at Buffalo, Buffalo, New York, USA. AbstractArsenic is a toxic metalloid that causes skin cancer and binds to cysteine residues-a property that could be used to infer arsenic responsiveness of a target protein. Non-synonymous Single Nucleotide Polymorphisms (nsSNPs) result in amino acid substitutions and may alter arsenic binding with cysteine residues. Thus, the objective of this investigation was to identify and analyze nsSNPs that lead to substitutions to or from cysteine residues as an indication of increased or decreased arsenic responsiveness. We hypothesize that integration of data on molecular impacts of nsSNPs and arsenic-gene relationships will identify nsSNPs that could serve as arsenic responsiveness markers. We have analyzed functional and structural impacts data for 5,811 nsSNPs linked to 1,224 arsenic-annotated genes. In addition to the identified candidate nsSNPs for increased or reduced arsenic responsiveness, we observed i) a nsSNP that results in the breakage of a disulfide bond, as candidate marker for reduced arsenic responsiveness of KLK7, a secreted serine protease participate in normal shedding of the skin; and ii) 6 pairs of vicinal cysteines in KLK7 protein that could be binding sites for arsenic. In summary, our analysis identified non-synonymous SNPs that could be used to evaluate responsiveness of a protein target to arsenic. In particular, an epidermal expressed serine protease with crucial function in normal skin physiology was prioritized on the basis of abundance of vicinal cysteines for further research on arsenic-induced keratinocyte carcinogenesis.
