期刊
JOURNAL OF PROTEOMICS
卷 80, 期 -, 页码 55-65出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jprot.2013.01.001
关键词
Alpha-enolase; Crystal adhesion; Hyperoxaluria; Kidney stone; Oxalate
资金
- Thailand Research Fund (TRF) [RTA5380005, TRG5480005]
- Office of the Higher Education Commission
- Mahidol University under the National Research Universities Initiative
- Faculty of Medicine Siriraj Hospital
- Royal Golden Jubilee Ph.D. Program scholarship
- Chalermphrakiat Grant, Faculty of Medicine Siriraj Hospital
Hyperoxaluria is one of etiologic factors of calcium oxalate kidney stone disease. However, response of renal tubular cells to high-oxalate environment remained largely unknown. We applied a gel-based proteomics approach to characterize changes in cellular proteome of MDCK cells induced by 10 mM sodium oxalate. A total of 14 proteins were detected as differentially expressed proteins. The oxalate-induced up-regulation of alpha-enolase in whole cell lysate was confirmed by 2-D Western blot analysis. Interaction network analysis revealed that cellular adaptive response under high-oxalate condition involved stress response, energy production, metabolism and transcriptional regulation. Down-regulation of RhoA, which was predicted to be associated with the identified proteins, was confirmed by immunoblotting. In addition, the up-regulation of alpha-enolase on apical surface of renal tubular epithelial cells was also confirmed by immunoblotting of the isolated apical membranes and immunofluorescence study. Interestingly, blockage of alpha-enolase expressed on the cell surface by antibody neutralization significantly reduced the number of calcium oxalate monohydrate (COM) crystals adhered on the cells. These results strongly suggest that surface alpha-enolase plays an important role as the enhancer of COM crystal binding. The increase of alpha-enolase expressed on the cell surface may aggravate kidney stone formation in patients with hyperoxaluria. (C) 2013 Elsevier B.V. All rights reserved.
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