Literature DB >> 27113968

Characterization of the Protein Components of Matrix Stones Sheds Light on S100-A8 and S100-A9 Relevance in the Inflammatory Pathogenesis of These Rare Renal Calculi.

Claudia Martelli1, Valeria Marzano1, Federica Iavarone1, Liling Huang1, Federica Vincenzoni1, Claudia Desiderio2, Irene Messana3, Paolo Beltrami4, Filiberto Zattoni4, Pietro Manuel Ferraro5, Noor Buchholz6, Giorgia Locci7, Gavino Faa7, Massimo Castagnola8, Giovanni Gambaro9.   

Abstract

PURPOSE: Among the different types of kidney stones, matrix stones are uncommon urinary calculi composed of a soft, pliable, amorphous substance with little crystalline content. To gain insight into the pathogenesis we investigated the protein component by analyzing the proteomic profiles of surgically removed matrix stones.
MATERIALS AND METHODS: A total of 5 stones were harvested from 4 patients who underwent surgery for medical reasons at 3 clinical centers during a 7-year period. Matrix stone proteome characterization was performed by mass spectrometry based techniques using an integrated top-down/bottom-up proteomic platform.
RESULTS: We identified 142 nonredundant proteins and peptides across all samples. Neutrophil defensin 1, and proteins S100-A8 and S100-A9 were the main components of these renal calculi.
CONCLUSIONS: The abundance of identified inflammatory molecules points to an inflammatory process as the event that initializes soft calculi formation rather than as a consequence of such formation. The post-translational oxidative changes in S100-A8 and A9, and the presence of thymosin β-4, granulins and ubiquitin also suggest the intervention of host defenses through a superimposed, vigorous counter inflammatory process. The post-translational changes seen in the proteins and peptides, and the known self-assembling capability of S100-A8 and S100-A9 probably explain the gelatinous consistency of these stones.
Copyright © 2016 American Urological Association Education and Research, Inc. Published by Elsevier Inc. All rights reserved.

Entities:  

Keywords:  inflammation; kidney calculi; proteomics

Mesh:

Substances:

Year:  2016        PMID: 27113968     DOI: 10.1016/j.juro.2016.04.064

Source DB:  PubMed          Journal:  J Urol        ISSN: 0022-5347            Impact factor:   7.450


  5 in total

Review 1.  Metal sequestration by S100 proteins in chemically diverse environments.

Authors:  Tomer Rosen; Kwo-Kwang A Wang; Elizabeth M Nolan
Journal:  Trends Microbiol       Date:  2022-01-24       Impact factor: 18.230

2.  Oxidative Post-translational Modifications Accelerate Proteolytic Degradation of Calprotectin.

Authors:  Jules R Stephan; Fangting Yu; Rebekah M Costello; Benjamin S Bleier; Elizabeth M Nolan
Journal:  J Am Chem Soc       Date:  2018-12-05       Impact factor: 15.419

3.  Quantitative proteomic analysis of urinary exosomes in kidney stone patients.

Authors:  Qing Wang; Yi Sun; Yuanyuan Yang; Cong Li; Jiaqiao Zhang; Shaogang Wang
Journal:  Transl Androl Urol       Date:  2020-08

4.  Proteomic analysis reveals some common proteins in the kidney stone matrix.

Authors:  Yuanyuan Yang; Senyuan Hong; Cong Li; Jiaqiao Zhang; Henglong Hu; Xiaolong Chen; Kehua Jiang; Fa Sun; Qing Wang; Shaogang Wang
Journal:  PeerJ       Date:  2021-07-27       Impact factor: 2.984

5.  Comprehensive study of altered proteomic landscape in proximal renal tubular epithelial cells in response to calcium oxalate monohydrate crystals.

Authors:  Zhu Wang; Ming-Xing Li; Chang-Zhi Xu; Ying Zhang; Qiong Deng; Rui Sun; Qi-Yi Hu; Sheng-Ping Zhang; Jian-Wen Zhang; Hui Liang
Journal:  BMC Urol       Date:  2020-08-31       Impact factor: 2.264

  5 in total

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