Proteome alterations in response to aristolochic acids in experimental animal model

Ručević, Marijana; Rosenquist, Thomas A.; Breen, Lucas; Cao, Lulu; Clifton, James R; Hixson, Douglas C.; Josić, Djuro

doi:10.1016/j.jprot.2012.06.026

Cited by 13 publications

(11 citation statements)

References 46 publications

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“…However, this method showed lower reproducibility of separating proteins (Imai, Koshiyama, & Nakata, ). Although Rucevic et al () set up an acute animal model of aristolochic acid nephropathy for 4 days, we would like to explore long‐term pathological conditions of aristolochic acid nephropathy.…”

Section: Introductionmentioning

confidence: 99%

Proteomics analysis of altered proteins in kidney of mice with aristolochic acid nephropathy using the fluorogenic derivatization–liquid chromatography–tandem mass spectrometry method

Lin

Chang

Lee

et al. 2017

Biomedical Chromatography

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Aristolochic acid (AA) causes interstitial renal fibrosis, called aristolochic acid nephropathy (AAN). There is no specific indicator for diagnosing AAN, so this study aimed to investigate the biomarkers for AAN using a proteomics method. The C3H/He female mice were given ad libitum AA-distilled water (0.5 mg/kg/day) and distilled water for 56 days in the AA and normal groups, respectively. The AA-induced proteins in the kidney were investigated using a proteomics study, including fluorogenic derivatization with 7-chloro-N-[2-(dimethylamino)ethyl]-2,1,3-benzoxadiazole-4-sulfonamide, followed by high-performance liquid chromatography analysis and liquid chromatography tandem mass spectrometry with a MASCOT database searching system. There were two altered proteins, thrombospondin type 1 (TSP1) and G protein-coupled receptor 87 (GPR87), in the kidney of AA-group mice on day 56. GPR87, a tumorigenesis-related protein, is reported for the first time in the current study. The renal interstitial fibrosis was certainly induced in the AA-group mice under histological examination. Based on the results of histological examination and the proteomics study, this model might be applied to AAN studies in the future. TSP1 might be a novel biomarker for AAN, and the further role of GPR87 leading to AA-induced tumorigenesis should be researched in future studies.

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Section: Introductionmentioning

confidence: 99%

Proteomics analysis of altered proteins in kidney of mice with aristolochic acid nephropathy using the fluorogenic derivatization–liquid chromatography–tandem mass spectrometry method

Lin

Chang

Lee

et al. 2017

Biomedical Chromatography

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“…During stepwise solubilization, plasma membranes are frozen and thawed, and subsequently treated with salts, usually at higher pH, followed by chaotropic reagents, and then by different ionic or non-ionic detergents, or by combination of these substances [5, 8, 12]. We used this solubilization schema for qualitative and semi-quantitative comparison of proteomes of tissues and for identification of candidate biomarkers for hepatocellular carcinomas [13, 15]. Peng’s group recommended the use of a similar method for enrichment of membranes from the liver microsomal fraction, to be followed by SDS-PAGE, tryptic digestion of excised proteins and identification by LC-MS/MS [15].…”

Section: Introductionmentioning

confidence: 99%

Mass Spectrometry-Based Analysis of Rat Liver and Hepatocellular Carcinoma Morris Hepatoma 7777 Plasma Membrane Proteome

et al. 2013

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The gel-based proteomic analysis of plasma membranes from rat liver and chemically induced, malignant hepatocellular carcinoma Morris hepatoma 7777 was systematically optimized to yield the maximum number of proteins containing transmembrane domains (TMDs). Incorporation of plasma membrane proteins into polyacrylamide “tube gel” followed by in-gel digestion of “tube gel” pieces significantly improved detection by ESI-LC-MS/MS. Removal of less hydrophobic proteins by washing isolated plasma membranes with 0.1 M sodium carbonate enables detection of hydrophobic proteins with one or more TMDs in both tissues. Subsequent treatment of plasma membranes by a proteolytic enzyme (trypsin) causes the loss of some of the proteins that are detected after washing with sodium carbonate, but it enables the detection of other hydrophobic proteins containing TMDs. Introduction of mass spectrometers with higher sensitivity, higher mass resolution and mass accuracy, and a faster scan rate significantly improved detection of membrane proteins, but the improved sample preparation is still useful, and enables detection of additional hydrophobic proteins. Proteolytic pre-digestion of plasma membranes enables detection of additional hydrophobic proteins and better sequence coverage of TMD-containing proteins in plasma membranes from both tissues.

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“…The comparative tissue proteome analysis was performed with a C++‐based software that was developed to quickly process large data sets, using a simple recursive algorithms for searching and sorting. By use of this programme, the comparison of common and differentially expressed proteins identified by LC‐ESI‐MS/MS analysis of tissue extracts that corresponded to control was completed .…”

Section: Methodsmentioning

confidence: 99%

Proteomics profiling of keratocystic odontogenic tumours reveals AIDA as novel biomarker candidate

Malčić

Breen

Josić

et al. 2014

J Oral Pathology Medicine

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Proteome alterations in response to aristolochic acids in experimental animal model

Cited by 13 publications

References 46 publications

Proteomics analysis of altered proteins in kidney of mice with aristolochic acid nephropathy using the fluorogenic derivatization–liquid chromatography–tandem mass spectrometry method

Proteomics analysis of altered proteins in kidney of mice with aristolochic acid nephropathy using the fluorogenic derivatization–liquid chromatography–tandem mass spectrometry method

Mass Spectrometry-Based Analysis of Rat Liver and Hepatocellular Carcinoma Morris Hepatoma 7777 Plasma Membrane Proteome

Proteomics profiling of keratocystic odontogenic tumours reveals AIDA as novel biomarker candidate

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