scholarly journals Identification of potential biomarkers for complex III deficiency by 2D-DIGE proteomic approach

2012 ◽  
Vol 1817 ◽  
pp. S139-S140
Author(s):  
L. Marin-Buera ◽  
M. Martínez Gomáriz ◽  
C. Ugalde
Keyword(s):  
Complex Iii ◽  
2D Dige ◽  
Proteomic Approach ◽  
Potential Biomarkers

A proteomic approach to investigate potential biomarkers directed against membrane-associated breast cancer proteins

2006 ◽  
Vol 27 (8) ◽  
pp. 1609-1616 ◽  
Author(s):  
Ludovic Canelle ◽  
Jordane Bousquet ◽  
Cedric Pionneau ◽  
Julie Hardouin ◽  
Genevieve Choquet-Kastylevsky ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Proteomic Approach ◽  
Potential Biomarkers

Abstract P277: Cardioprotection Enabled by Proteomic Remodeling of the Mitochondrial Respiratory Chain

2011 ◽  
Vol 109 (suppl_1) ◽  
Author(s):  
Christopher Lotz ◽  
Ning Deng ◽  
Jun Zhang ◽  
Yueju Wang ◽  
Chenggong Zong ◽  
...  
Keyword(s):  
Respiratory Chain ◽  
Nuclear Genome ◽  
Mitochondrial Respiratory Chain ◽  
Superoxide Production ◽  
Complex Iii ◽  
Molar Ratio ◽  
Label Free ◽  
Enzymatic Function ◽  
Proteomic Approach ◽  
Mitochondrial Respiratory

The mitochondrial respiratory chain is a collection of five multi-protein complexes, whose unobstructed functionality represents a pivotal element at the crossroads of cell death or survival. However, its molecular composition and stochiometric information remains elusive and the adaptive abilities of the chain remain largely unknown. We employed a quantitative proteomic approach to investigate the hypothesis that cardioprotection against ischemic injury is afforded by a salutary proteomic remodeling of the mitochondrial respiratory chain. The respiratory chain of cardiac mitochondria isolated from wild type (WT) mice and from mice expressing a constitutively active protein kinase Cε (AE-PKCε) were characterized using 15N-stable isotope labeled murine models (SILAM), as well as a label-free method in conjunction with high resolution LC-MS/MS, respectively. Enzymatic function of electron transport chain and the ATP synthase were evaluated (n=7/group); and mitochondrial superoxide production was examined by ESR-spectroscopy (n=3/group). Three novel and important observations are made: (i) five individual respiratory complexes exhibited a molar ratio of 1:1:1.4:1.2:4.5 in the WT-heart; (ii) subunits within the five complexes encoded by the mitochondrial genome were expressed at much lower abundance (p<0.05) than those encoded by the nuclear genome; and (iii) Genetic cardioprotection by AE-PKCε elicited a proteomic remodeling of complex I and III, mitochondria from AE-PKCε exhibited an increased expression of multiple subunits, including the catalytic complex III subunit Cyc1. This finding was accompanied by a preserved complex III activity (p<0.05), as well as tempered superoxide production (p<0.01) subsequent to Ca2+-induced damage. This is the first study documenting a salutary proteomic remodeling of the mitochondrial respiratory machinery in cardioprotection. Quantitative proteomics technology enabled novel information and new insights into mitochondrial biology.

scholarly journals Proteomic Approach to Evaluate Mechanisms That Contribute to Food Allergenicity: Comparative 2D-DIGE Analysis of Radioallergosorbent Test Positive and Negative Patients

2011 ◽  
Vol 2011 ◽  
pp. 1-13 ◽  
Author(s):  
Bindukumar Nair ◽  
John C. Wheeler ◽  
Donald E. Sykes ◽  
Paula Brown ◽  
Jessica L. Reynolds ◽  
...  
Keyword(s):  
Map Kinases ◽  
Allergic Response ◽  
Food Allergies ◽  
Analysis Tool ◽  
Th2 Response ◽  
Bioinformatics Analyses ◽  
2D Dige ◽  
Proteomic Approach ◽  
Retinoic Acid Binding Proteins ◽  
Dige Analysis

Proteomic profiles of RAST+ subjects with severe food allergies and RAST− subjects were compared using 2D-DIGE analysis to obtain candidate biomarkers specific to food allergies. Our analysis highlighted 52 proteins that were differentially expressed between the RAST+ and RAST− groups of which 37 were successfully identified that include chondroitin sulfates, zinc finger proteins, C-type lectins, retinoic acid binding proteins, heat shock proteins, myosin, cytokines, mast cell expressed proteins, and MAP kinases. Biological network analysis tool Metacore revealed that most of these regulated proteins play a role in immune tolerance, hypersensitivity and modulate cytokine patterns inducing a Th2 response that typically results in IgE-mediated allergic response which has a direct or indirect biological link to food allergy. Identifying unique biomarkers associated with certain allergic phenotypes and potentially cross-reactive proteins through bioinformatics analyses will provide enormous insight into the mechanisms that underlie allergic response in patients with food allergies.

scholarly journals Identification of potential biomarkers of head and neck squamous cell carcinoma using iTRAQ based quantitative proteomic approach

Data in Brief ◽  
2018 ◽  
Vol 19 ◽  
pp. 1124-1130 ◽  
Author(s):  
Niraj Babu ◽  
Sonali Mohan ◽  
Vishalakshi Nanjappa ◽  
Sandip Chavan ◽  
Jayshree Advani ◽  
...  
Keyword(s):  
Squamous Cell Carcinoma ◽  
Cell Carcinoma ◽  
Head And Neck ◽  
Squamous Cell ◽  
Neck Squamous Cell Carcinoma ◽  
Proteomic Approach ◽  
Potential Biomarkers

scholarly journals A Quantitative Proteomic Approach for Identification of Potential Biomarkers in Hepatocellular Carcinoma

2008 ◽  
Vol 7 (10) ◽  
pp. 4289-4298 ◽  
Author(s):  
Raghothama Chaerkady ◽  
H. C. Harsha ◽  
Anuradha Nalli ◽  
Marjan Gucek ◽  
Perumal Vivekanandan ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Proteomic Approach ◽  
Potential Biomarkers

scholarly journals 2D DIGE analysis of maternal plasma for potential biomarkers of Down Syndrome

2011 ◽  
Vol 9 (1) ◽  
pp. 56 ◽  
Author(s):  
Wendy E Heywood ◽  
Tracey E Madgett ◽  
Darrell Wang ◽  
Amanda Wallington ◽  
Julie Hogg ◽  
...  
Keyword(s):  
Down Syndrome ◽  
Maternal Plasma ◽  
2D Dige ◽  
Dige Analysis ◽  
Potential Biomarkers

scholarly journals Proteomics Profiling of the Urine of Patients with Hyperthyroidism after Anti-Thyroid Treatment

Molecules ◽  
2021 ◽  
Vol 26 (7) ◽  
pp. 1991
Author(s):  
Hicham Benabdelkamel ◽  
Afshan Masood ◽  
Aishah A. Ekhzaimy ◽  
Assim A. Alfadda
Keyword(s):  
Bioinformatic Analysis ◽  
Gamma Glutamyl Transferase ◽  
Urinary Proteins ◽  
Systemic Hemodynamic ◽  
2D Dige ◽  
Proteomic Approach ◽  
Significant Difference ◽  
Before And After ◽  
Thyroid Hormone Levels ◽  
Glutamyl Transferase

Hyperthyroidism, which is characterized by increased circulating thyroid hormone levels, alters the body’s metabolic and systemic hemodynamic balance and directly influences renal function. In this study, the urinary proteome of patients with hyperthyroidism was characterized using an untargeted proteomic approach with network analysis. Urine samples were collected from nine age-matched patients before and after carbimazole treatment. Differences in the abundance of urinary proteins between hyperthyroid and euthyroid states were determined using a 2D-DIGE coupled to MALDI-TOF mass spectrometry. Alterations in the abundance of urinary proteins, analyzed via Progenesis software, revealed a statistically significant difference in abundance in a total of 40 spots corresponding to 32 proteins, 25 up and 7 down (≥1.5-fold change, ANOVA, p ≤ 0.05). The proteins identified in the study are known to regulate processes associated with cellular metabolism, transport, and acute phase response. The notable upregulated urinary proteins were serotransferrin, transthyretin, serum albumin, ceruloplasmin, alpha-1B-glycoprotein, syntenin-1, and glutaminyl peptide cyclotransferase, whereas the three notable downregulated proteins were plasma kallikrein, protein glutamine gamma-glutamyl transferase, and serpin B3 (SERPINB3). Bioinformatic analysis using ingenuity pathway analysis (IPA) identified the dysregulation of pathways associated with cellular compromise, inflammatory response, cellular assembly, and organization and identified the involvement of the APP and AKT signaling pathways via their interactions with interleukins as the central nodes.

scholarly journals Proteomic Approach for Identification of IgA Nephropathy-Related Biomarkers in Urine

2017 ◽  
pp. 621-632 ◽  
Author(s):  
P. PRIKRYL ◽  
L. VOJTOVA ◽  
D. MAIXNEROVA ◽  
M. VOKURKA ◽  
M. NEPRASOVA ◽  
...  
Keyword(s):  
Iga Nephropathy ◽  
Kidney Diseases ◽  
Surrogate Marker ◽  
Pilot Project ◽  
Protein Quantification ◽  
Absolute Quantitation ◽  
Proteomic Approach ◽  
Isobaric Tag ◽  
Alpha 1 Antitrypsin ◽  
Potential Biomarkers

Proteinuria is often used as a surrogate marker in monitoring and predicting outcome in patients with chronic kidney diseases, but it is non-specific. IgAN belongs to the most common primary glomerulonephritis worldwide with serious prognosis. The main aim of this work was to assess differences in urine proteins in patients with IgA nephropathy and to identify abnormal proteins as potential biomarkers of IgA nephropathy or the renal disease. In our pilot project, we selected 20 patients and compared them with 20 healthy volunteers. Protein quantification was performed using iTRAQ (isobaric tag for relative and absolute quantitation) labeling method. The peptides were separated by the isoelectric focusing method (IEF) and nano-LC with C18 column and identified by mass spectrometry using MALDI-TOF/TOF MS. Proteins´ lists obtained from IEF-LC-MS-MS/MS analysis were combined and contained 201 proteins. It was found out that 113 proteins were common in both experiments. 30 urinary proteins were significantly up- or down-regulated in patients with IgA nephropathy. We characterized potential biomarkers such as alpha-1-antitrypsin, apolipoprotein A-I, CD44 antigen or kininogen. Potential biomarkers of IgAN should be validated in further studies.

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