Proteomic Study of Renal Uric Acid Stone

The precise mechanisms of kidney stone formation and growth are not completely known, even though human stone disease appears to be one of the oldest diseases known to medicine. With the advent of the new digital endoscope and detailed renal physiological studies performed on well phenotyped stone formers, substantial advances have been made in our knowledge of the pathogenesis of the most common type of stone former, the idiopathic calcium oxalate stone former (ICSF) as well as nine other stone forming groups. The observations from our group on human stone formers and those of others on model systems have suggested four entirely different pathways for kidney stone formation. Calcium oxalate stone growth over sites of Randall’s plaque appear to be the primary mode of stone formation for those patients with hypercalciuria. Overgrowths off the ends of Bellini duct plugs have been noted in most stone phenotypes, do they result in a clinical stone? Micro-lith formation does occur within the lumens of dilated inner medullary collecting ducts of cystinuric stone formers and appear to be confined to this space. Lastly, cystinuric stone formers also have numerous small, oval, smooth yellow appearing calyceal stones suggestive of formation in free solution. The scientific basis for each of these four modes of stone formation are reviewed and used to explore novel research opportunities.

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“…We are aware of proteomic studies of materials eluted from kidney stones (40–47). These are of value in themselves.…”

Section: Growth On Plaquementioning

confidence: 99%

Mechanisms of human kidney stone formation

et al. 2014

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“…Between 2010 and today, a number of papers have been published that add to the total number of proteins known to have been identified in kidney stones matrices. 5,6,8,9,14,18,19 These papers point to the large proportion of inflammatory proteins found within kidney stone matrices. They also highlight the diversity in kidney stone matrix protein composition between individuals.…”

Section: Discussionmentioning

confidence: 99%

“…A number of studies have used mass spectrometry to identify the proteins within kidney stone matrices. [5][6][7][8][9][10][11][12][13][14][15] These studies have employed a range of techniques to extract proteins from the crystalline structure. Most of these studies have assessed relatively small cohorts of samples and inadequate extraction techniques have necessitated the use of pooled samples.…”

Section: Introductionmentioning

confidence: 99%

Analysis of Methods for Extracting Matrix Proteins from Human Kidney Stones

Stock¹

2017

UNOAJ

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Five techniques for the extraction of proteins from kidney stones were compared for the purpose of maximizing yield for mass spec analysis. The proteomics of kidney stones may provide insight into the underlying mechanisms of stone formation and why some people are more prone to developing kidney stones than others. Kidney stones contain proteins that may serve as markers for a wide variety of disease states. Mass spectrometry offers the ability to identify and quantify the complete proteome of a kidney stone. To date, there have been only a limited number of research projects aimed at studying the protein composition of kidney stones, possibly due to the difficulty in extracting these proteins while preserving the ability to subject the samples to mass spectrometry. We compared five methods for extracting kidney stone matrix proteins, three from previously published studies and two methods we designed based on previous studies. We were able to establish which methods produced the highest yield of protein for both calcium oxalate and uric acid stones.

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“…The proteins were identified using the Mascot Distiller 2.0 software (Matrix Science Ltd., London, UK). The mass spectra collected in the experiment were analyzed using the Swiss-Prot protein database (19). Protein scores >56 were regarded as significant.…”

Section: Methodsmentioning

confidence: 99%

Proteomic analysis of differentially expressed proteins in kidneys of brain dead rabbits

et al. 2017

Molecular Medicine Reports

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A large number of previous clinical studies have reported a delayed graft function for brain dead donors, when compared with living relatives or cadaveric organ transplantations. However, there is no accurate method for the quality evaluation of kidneys from brain-dead donors. In the present study, two-dimensional gel electrophoresis and MALDI-TOF MS-based comparative proteomic analysis were conducted to profile the differentially-expressed proteins between brain death and the control group renal tissues. A total of 40 age- and sex-matched rabbits were randomly divided into donation following brain death (DBD) and control groups. Following the induction of brain death via intracranial progressive pressure, the renal function and the morphological alterations were measured 2, 6 and 8 h afterwards. The differentially expressed proteins were detected from renal histological evidence at 6 h following brain death. Although 904±19 protein spots in control groups and 916±25 in DBD groups were identified in the two-dimensional gel electrophoresis, >2-fold alterations were identified by MALDI-TOF MS and searched by NCBI database. The authors successfully acquired five downregulated proteins, these were: Prohibitin (isoform CRA_b), beta-1,3-N-acetylgalactosaminyltransferase 1, Annexin A5, superoxide dismutase (mitochondrial) and cytochrome b-c1 complex subunit 1 (mitochondrial precursor). Conversely, the other five upregulated proteins were: PRP38 pre-mRNA processing factor 38 (yeast) domain containing A, calcineurin subunit B type 1, V-type proton ATPase subunit G 1, NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10 and peroxiredoxin-3 (mitochondrial). Immunohistochemical results revealed that the expressions of prohibitin (PHB) were gradually increased in a time-dependent manner. The results indicated that there were alterations in levels of several proteins in the kidneys of those with brain death, even if the primary function and the morphological changes were not obvious. PHB may therefore be a novel biomarker for primary quality evaluation of kidneys from brain-dead donors.

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Proteomic Study of Renal Uric Acid Stone

Cited by 23 publications

References 26 publications

Mechanisms of human kidney stone formation

Mechanisms of human kidney stone formation

Analysis of Methods for Extracting Matrix Proteins from Human Kidney Stones

Proteomic analysis of differentially expressed proteins in kidneys of brain dead rabbits

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