Abstract
BackgroundKidney stone matrix protein composition is an important yet poorly understood aspect of nephrolithiasis. We hypothesized that this proteome is considerably more complex than previous reports have indicated and that comprehensive proteomic profiling of the kidney stone matrix may demonstrate relevant constitutive differences between stones. We have analyzed the matrices of two unique human calcium oxalate stones (CaOx-Ia and CaOx-Id) using a simple but effective chaotropic reducing solution for extraction/solubilization combined with label-free quantitative mass spectrometry to generate a comprehensive profile of their proteomes, including physicochemical and bioinformatic analysis.`ResultsWe identified and quantified 1,059 unique protein database entries in the two human kidney stone samples, revealing a more complex proteome than previously reported. Protein composition reflects a common range of proteins related to immune response, inflammation, injury, and tissue repair, along with a more diverse set of proteins unique to each stone.ConclusionThe use of a simple chaotropic reducing solution and moderate sonication for extraction and solubilization of kidney stone powders combined with label-free quantitative mass spectrometry has yielded the most comprehensive list to date of the proteins that constitute the human kidney stone proteome.Electronic supplementary materialThe online version of this article (doi:10.1186/s12953-016-0093-x) contains supplementary material, which is available to authorized users.
Highlights
Kidney stone matrix protein composition is an important yet poorly understood aspect of nephrolithiasis
Stone extracts It is not exactly clear what fraction of the total stone protein can be extracted in a form usable for proteomic analysis
The larger value is 3 times the average extraction yield that we have previously reported for calcium oxalate monohydrate (COM) stones using 9 M urea/1 mM DTT [5]
Summary
Kidney stone matrix protein composition is an important yet poorly understood aspect of nephrolithiasis. Recent studies of human stone matrix have begun to exploit the power of modern proteomic methods, with some patterns beginning to emerge in the kinds of proteins found [6,7,8,9,10,11,12,13,14,15,16,17]. Nine of these recent stone proteomic studies contain profiles of CaOx stone-
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