Publication: Isolation and characterizations of oxalate-binding proteins in the kidney
Issued Date
2012-08-03
Resource Type
ISSN
10902104
0006291X
0006291X
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2-s2.0-84864760793
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Mahidol University
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SCOPUS
Bibliographic Citation
Biochemical and Biophysical Research Communications. Vol.424, No.3 (2012), 629-634
Suggested Citation
Piyachat Roop-ngam, Sakdithep Chaiyarit, Nutkridta Pongsakul, Visith Thongboonkerd Isolation and characterizations of oxalate-binding proteins in the kidney. Biochemical and Biophysical Research Communications. Vol.424, No.3 (2012), 629-634. doi:10.1016/j.bbrc.2012.07.015 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/13642
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Title
Isolation and characterizations of oxalate-binding proteins in the kidney
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Abstract
Oxalate-binding proteins are thought to serve as potential modulators of kidney stone formation. However, only few oxalate-binding proteins have been identified from previous studies. Our present study, therefore, aimed for large-scale identification of oxalate-binding proteins in porcine kidney using an oxalate-affinity column containing oxalate-conjugated EAH Sepharose 4B beads for purification followed by two-dimensional gel electrophoresis (2-DE) to resolve the recovered proteins. Comparing with those obtained from the controlled column containing uncoupled EAH-Sepharose 4B (to subtract the background of non-specific bindings), a total of 38 protein spots were defined as oxalate-binding proteins. These protein spots were successfully identified by quadrupole time-of-flight mass spectrometry (MS) and/or tandem MS (MS/MS) as 26 unique proteins, including several nuclear proteins, mitochondrial proteins, oxidative stress regulatory proteins, metabolic enzymes and others. Identification of oxalate-binding domain using the PRATT tool revealed "L- x(3,. 5)- R- x(2)-[. AGILPV]" as a functional domain responsible for oxalate-binding in 25 of 26 (96%) unique identified proteins. We report herein, for the first time, large-scale identification and characterizations of oxalate-binding proteins in the kidney. The presence of positively charged arginine residue in the middle of this functional domain suggested its significance for binding to the negatively charged oxalate. These data will enhance future stone research, particularly on stone modulators. © 2012 Elsevier Inc.