Exploring mechanisms of protein influence on calcium oxalate kidney stone formation

Urolithiasis - Tập 49 - Trang 281-290 - 2021
Garrett K. Berger1, Jessica Eisenhauer1, Andrew Vallejos2,3, Brian Hoffmann3,4,5, Jeffrey A. Wesson1,6
1Division of Nephrology, Department of Medicine, Medical College of Wisconsin, Milwaukee, USA
2Department of Biomedical Engineering, Max McGee National Research Center, Cardiovascular Center, Center for Advancing Population Science, Medical College of Wisconsin and Marquette University, Milwaukee, USA
3Clinical Science and Translational Institute, Medical College of Wisconsin, Milwaukee, USA
4Department of Physiology, Max McGee National Research Center, Cardiovascular Center, Center for Advancing Population Science, Medical College of Wisconsin, Milwaukee, USA
5The Jackson Laboratory, Mass Spectrometry and Protein Chemistry, Protein Sciences, Bar Harbor, USA
6Consultant Care Division/Nephrology Section, Clement J. Zablocki Department of Veterans Affairs Medical Center, Milwaukee, USA

Tóm tắt

Calcium oxalate monohydrate (COM) crystals are the primary constituent of most kidney stones, but urine proteins in stone matrix are believed to be critical elements for stone formation from these crystals. Recent data have shown that hundreds of proteins appear in the stone matrix with no explanation for inclusion of so many proteins. We have proposed a stone formation model with protein stimulated COM aggregation based on polyanion–polycation aggregation, which is supported by finding that matrix is highly enriched in strongly anionic and strongly cationic proteins. Many other proteins may be drawn to such aggregates due to their limited solubility in water or charge effects. Finding similar protein enrichment in both polyarginine (pR) induced aggregates of urine proteins and COM stone matrix would support this hypothesis. Purified proteins (PP) were obtained from random urine samples of six healthy adults by ultradiafiltration. Protein aggregation was induced by adding pR to PP solutions at two concentrations; 0.25 and 0.5 µg pR/µg of PP. Samples of each fraction and the original PP mixture were lyophilized and analyzed by tandem mass spectrometry. Aggregates induced by pR addition to PP samples collected a protein mixture that mimicked the protein distribution observed in COM matrix, supporting our hypothesis. The apparently discordant behavior of certain abundant anionic proteins preferentially joining the pR aggregate, when they had demonstrated reduced abundance in COM stone matrix, suggests that this model was overdriven to aggregate. The reversal of aggregate preference of albumin at low pR addition supports this interpretation.

Tài liệu tham khảo

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