Identification of Proteins Differentially Expressed in the Conventional Renal Cell Carcinoma by Proteomic Analysis

Hwa, Jeong Seok; Park, Hyojin; Jung, Jae Hun; Kam, Sung Chul; Park, Hyung Chul; Kim, Choong Won; Kang, Kee Ryeon; Hyun, Jea Seog; Kihan, Chung

doi:10.3346/jkms.2005.20.3.450

Cited by 43 publications

(29 citation statements)

References 26 publications

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“…Although the ketohexokinase is mostly abundant in liver, it was also found in kidney, small intestine and pancreas (4). Hwa et al (4) found lower levels of ketohexokinase in ccRCC tissues, in accordance with our findings.…”

Section: Discussionsupporting

confidence: 83%

“…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%

“…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%

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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: Discussionsupporting

confidence: 83%

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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“…34 However, it has been reported that ECHS1 expression is decreased in renal cell carcinomas 35 and in hepatocellular carcinomas. 36 This most likely indicates that alterations in fatty acid metabolism pathways vary among PCa and other cancers.…”

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confidence: 99%

Identification of candidate prostate cancer biomarkers in prostate needle biopsy specimens using proteomic analysis

Lin

Tian

et al. 2007

Intl Journal of Cancer

115

101

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Although serum prostate specific antigen (PSA) is a well-established diagnostic tool for prostate cancer (PCa) detection, the definitive diagnosis of PCa is based on the information contained in prostate needle biopsy (PNBX) specimens. To define the proteomic features of PNBX specimens to identify candidate biomarkers for PCa, PNBX specimens from patients with PCa or benign prostatic hyperplasia (BPH) were subjected to comparative proteomic analysis. 2-DE revealed that 52 protein spots exhibited statistically significantly changes among PCa and BPH groups. Interesting spots were identified by MALDI-TOF-MS/MS. The 2 most notable groups of proteins identified included latent androgen receptor coregulators and FKBP4] and enzymes involved in mitochondrial fatty acid b-oxidation (DCI and ECHS1). An imbalance in the expression of peroxiredoxin subtypes was noted in PCa specimens. Furthermore, different post-translationally modified isoforms of HSP27 and HSP70.1 were identified. Importantly, changes in FLNA(7-15), FKBP4, and PRDX4 expression were confirmed by immunoblot analyses. Our results suggest that a proteomics-based approach is useful for developing a more complete picture of the protein profile of PNBX specimen. The proteins identified by this approach may be useful molecular targets for PCa diagnostics and therapeutics. ' 2007 Wiley-Liss, Inc.

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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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Identification of Proteins Differentially Expressed in the Conventional Renal Cell Carcinoma by Proteomic Analysis

Cited by 43 publications

References 26 publications

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

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

Identification of candidate prostate cancer biomarkers in prostate needle biopsy specimens using proteomic analysis

Proteomics in renal research

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