Current Status and Advances in Quantitative Proteomic Mass Spectrometry

Wasinger, Valerie C.; Zeng, Mingyong; Yau, Yunki

doi:10.1155/2013/180605

Cited by 138 publications

(90 citation statements)

References 94 publications

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“…The crux of selecting candidate biomarkers in proteomic studies rely detecting differences in abundances between cases and controls; therefore quantitative proteomics is an essential aspect. Multiple reaction monitoring (MRM) is a quantitative technique that achieves absolute quantitation and has a relatively high sensitivity when detecting peptides in low abundance, suiting it towards application in proteomic biomarker studies [19] .…”

Section: Proteomicsmentioning

confidence: 99%

Current application of proteomics in biomarker discovery for inflammatory bowel disease

Chan¹,

Wasinger²,

Leong³

2016

WJGP

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Recently, the field of proteomics has rapidly expanded in its application towards clinical research with objectives ranging from elucidating disease pathogenesis to discovering clinical biomarkers. As proteins govern and/or reflect underlying cellular processes, the study of proteomics provides an attractive avenue for research as it allows for the rapid identification of protein profiles in a biological sample. Inflammatory bowel disease (IBD) encompasses several heterogeneous and chronic conditions of the gastrointestinal tract. Proteomic technology provides a powerful means of addressing major challenges in IBD today, especially for identifying biomarkers to improve its diagnosis and management. This review will examine the current state of IBD proteomics research and its use in biomarker research. Furthermore, we also discuss the challenges of translating proteomic research into clinically relevant tools. The potential application of this growing field is enormous and is likely to provide significant insights towards improving our future understanding and management of IBD.

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Section: Proteomicsmentioning

confidence: 99%

Current application of proteomics in biomarker discovery for inflammatory bowel disease

Chan¹,

Wasinger²,

Leong³

2016

WJGP

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“…In order to utilize triple quadrupole mass spectrometry for protein quantification, prior protein digestion and quantification of peptide products through a bottom-up approach has been the norm [7,24,25]. However, such methods can be time-consuming and possible errors in the protein digestion steps can easily propagate, which can compromise precision and accuracy [26].…”

Section: Introductionmentioning

confidence: 99%

Multiple Reaction Monitoring for Direct Quantitation of Intact Proteins Using a Triple Quadrupole Mass Spectrometer

Wang

Combe²,

Schug

2016

J. Am. Soc. Mass Spectrom.

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Abstract. Methods that can efficiently and effectively quantify proteins are needed to support increasing demand in many bioanalytical fields. Triple quadrupole mass spectrometry (QQQ-MS) is sensitive and specific, and it is routinely used to quantify small molecules. However, low resolution fragmentation-dependent MS detection can pose inherent difficulties for intact proteins. In this research, we investigated variables that affect protein and fragment ion signals to enable protein quantitation using QQQ-MS. Collision induced dissociation gas pressure and collision energy were found to be the most crucial variables for optimization. Multiple reaction monitoring (MRM) transitions for seven standard proteins, including lysozyme, ubiquitin, cytochrome c from both equine and bovine, lactalbumin, myoglobin, and prostatespecific antigen (PSA) were determined. Assuming the eventual goal of applying such methodology is to analyze protein in biological fluids, a liquid chromatography method was developed. Calibration curves of six standard proteins (excluding PSA) were obtained to show the feasibility of intact protein quantification using QQQ-MS. Linearity (2-3 orders), limits of detection (0.5-50 μg/mL), accuracy (<5% error), and precision (1%-12% CV) were determined for each model protein. Sensitivities for different proteins varied considerably. Biological fluids, including human urine, equine plasma, and bovine plasma were used to demonstrate the specificity of the approach. The purpose of this model study was to identify, study, and demonstrate the advantages and challenges for QQQ-MS-based intact protein quantitation, a largely underutilized approach to date.

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“…After protein extraction, tryptic peptides can be analyzed by liquid chromatography (LC) coupled to MS/MS (40,41). This detection method allows for high resolution separation of hundreds of proteins to be quantified concurrently, thereby precisely revealing differential protein expression profiles.…”

Section: Chemical Proteomic Techniquesmentioning

confidence: 99%

Chemical Proteomic Approaches Targeting Cancer Stem Cells: A Review of Current Literature

Jung

2017

CGP

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Current Status and Advances in Quantitative Proteomic Mass Spectrometry

Cited by 138 publications

References 94 publications

Current application of proteomics in biomarker discovery for inflammatory bowel disease

Current application of proteomics in biomarker discovery for inflammatory bowel disease

Multiple Reaction Monitoring for Direct Quantitation of Intact Proteins Using a Triple Quadrupole Mass Spectrometer

Chemical Proteomic Approaches Targeting Cancer Stem Cells: A Review of Current Literature

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