Renal cell carcinoma and normal kidney protein expression

Sarto, Cecilia; Marocchi, Alessandro; Sánchez, Jean Charles; Giannone, Daniela; Frutiger, Séverine; Golaz, Olivier; Wilkins, Marc R.; Doro, Giancarlo; Cappellano, Francesco; Hughes, Graham J.; Hochstrasser, Denis F.; Mocarelli, Paolo

doi:10.1002/elps.1150180343

Cited by 124 publications

(90 citation statements)

References 34 publications

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“…Since then, other studies were performed with the same goal under different conditions or different proteomics approaches (3)(4)(5)(6)(7)(8). The method that was applied in this study is based on 2DE, the most traditional technology for separation of proteins.…”

Section: Discussionmentioning

confidence: 99%

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Differencial proteome of clear-cell renal cell carcinoma (ccRCC) tissues

et al. 2013

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Purpose: We attempted to detect, for the first time in a Brazilian cohort, differences in protein expression between clear-cell renal cell carcinoma (ccRCC) and their normal adjacent tissues, aiming to identify biomarkers and/or therapeutic target candidates for this disease. Material and Methods: Twenty-four ccRCC and adjacent normal tissues were collected after surgery and their protein extracts were quantified, pooled and separated by two--dimensional polyacrylamide gel electrophoresis (2DE), followed by statistical analysis of the stained gels. Spots of interest were excised from the gels, digested with trypsin and identified by MALDI-TOF-TOF mass spectrometry. Results: Twenty-six differential spots were detected between the two classes of tissues, among which twenty were identified by mass spectrometry and sixteen were found to be non-redundant. Eleven proteins were either underexpressed or undetected in the ccRCC extracts, such as prohibitin and peroxiredoxin-3, whereas five were found to be overexpressed or exclusively detected in the ccRCC extract, including αβ crystalin and heat shock protein 27. Conclusions: Several proteins were detected at differential levels when compared to normal adjacent tissues, and, moreover, many have been previously described by their relationship with RCC. Therefore, this work corroborates previous reports on the search for biomarkers for ccRCC, as well as it points out new candidates that may be validated in future studies.

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Section: Discussionmentioning

confidence: 99%

“…A constant effort has been made (3)(4)(5)(6)(7)(8) in the search for biomarker candidates for RCC. However, none of them achieved definitive diagnostic and prognostic value in clinical practice so far.…”

Section: Introductionmentioning

confidence: 99%

Differencial proteome of clear-cell renal cell carcinoma (ccRCC) tissues

et al. 2013

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“…Sarto et al 56 detected more than 2000 protein spots on a single 2-D gel of the whole kidney tissue and identified 47…”

Section: Data Processing and Analysismentioning

confidence: 99%

Toward Quantitative Proteomics of Organ Substructures: Implications for Renal Physiology

Velić

Maček

Wagner

2010

Seminars in Nephrology

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AcknowledgementsResearch in the laboratories of the authors has been supported by grants from the Minstry of Science, Baden-Wuerttenberg (to BM) and the Swiss National Science Foundation, the 6 th and 7 th EU Framework projects (EuReGene and EUNEFRON) (to CAW). We thank MatthiasMann for critically reading and discussing the manuscript. Summary 2Organs are complex structures that consist of multiple tissues with different levels of gene expression. To achieve a comprehensive coverage and accurate quantitation data, organs should ideally be separated into morphological and/or functional substructures prior to gene or protein expression analysis. However, due to complex morphology and elaborate isolation protocols, this was so far often difficult to achieve. Kidneys are organs where functional and morphological subdivision is especially important. Each subunit of the kidney, the nephron, itself consists of more than 10 subsegments with distinct morphological and functional characteristics. For a full understanding of kidney physiology, global gene and protein expression analyses have to be performed at the level of the nephron subsegments; however, such studies have so far been extremely rare.Here we describe the latest approaches in quantitative high accuracy mass spectrometrybased proteomics and their application to quantitative proteomics studies of the whole kidney and nephron subsegments, both in humans and in animal models. We compare these studies with similar studies performed on other organ substructures. We argue that the newest technologies used for preparation, processing and measurement of small amounts of starting material are finally enabling global and subsegment-specific quantitative measurement of protein levels in the kidney and other organs. These new technologies and approaches are making a decisive impact on our understanding of the (patho)physiological processes at the molecular level.3

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“…We will not review this area in great depth but will use examples of specific techniques that have been used. A number of studies have used 2D gels to compare proteins expressed in tumors to normal tissue (10,51,61,100,101,104).…”

Section: Urological Cancersmentioning

confidence: 99%

Proteomics in renal research

Janech¹,

Raymond²,

Arthur³

2007

American Journal of Physiology-Renal Physiology

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Proteomic technologies are used with increasing frequency in the renal community. In this review, we highlight the use in renal research of a number of available techniques including two-dimensional gel electrophoresis, liquid chromatography/mass spectrometry, surface-enhanced laser desorption/ionization, capillary electrophoresis/mass spectrometry, and antibody and tissue arrays. These techniques have been used to identify proteins or changes in proteins specific to regions of the kidney or associated with renal diseases or toxicity. They have also been used to examine protein expression changes and posttranslational modifications of proteins during signaling. A number of studies have used proteomic methodologies to look for diagnostic biomarkers in body fluids. The rapid rate of development of the technologies along with the combination of classic physiological and biochemical techniques with proteomics will enable new discoveries.

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Renal cell carcinoma and normal kidney protein expression

Cited by 124 publications

References 34 publications

Differencial proteome of clear-cell renal cell carcinoma (ccRCC) tissues

Differencial proteome of clear-cell renal cell carcinoma (ccRCC) tissues

Toward Quantitative Proteomics of Organ Substructures: Implications for Renal Physiology

Proteomics in renal research

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