Mass spectrometry biomarker proteins

Mahmoud H. Hamdan Cancer Biomarkers Analytical Techniques for Discovery Chabbil Dass Fundamentals of Contemporary Mass Spectrometry Kevin M. Downard (Editor) Mass Spectrometry of Protein Interactions... 

Isabella Dalle-Donne, Andrea Scaloni, and D. Allan Butterfield Redox Proteomics From Protein Modifications to Cellular Dysfunction and Diseases Silas G. Villas-Boas, Ute Roessner, Michael A.E. Hansen, Jom Smedsgaard, and Jens Nielsen Metabolome Analysis An Introduction Mahmoud H. Hamdan Cancer Biomarkers Analytical Techniques for Discovery Chabbil Dass Fundamentals of Contemporary Mass Spectrometry Kevin M. Downard (Editor) Mass Spectrometry of Protein Interactions Nobuhiro Takahashi and Toshiaki Isobe Proteomic Biology Using LC-MS Large Scale Analysis of Cellular Dynamics and Function... 

Wright, G. L., Cazares, L. H., Leung, S.-M., Nasim, S., Adam, B.-L., Yip, T.-T., Schellhammer, P. F., Gong, L., and Vlahou, A. (2000). ProteinChip surface enhanced laser desorption/ionization (SELDI) mass spectrometry a novel protein biochip technology for detection of prostate cancer biomarkers in complex protein mixtures. Prostate Cancer and Prostatic Diseases 2, 264-276. 

Additionally it has been our experience that mass spectrometry as a routine detection/identification technique for bacteria is not well received by microbiologists and clinicians who prefer less expensive, less complicated approaches to bacterial typing and identification, such as methods based on polymerase chain reaction (PCR) and enzyme-linked immunosorbent assays (ELISA). For that reason we have adapted our MS approach to serve as a means of biomarker discovery that feeds candidate proteins or leads into development as PCR targets or other immunoassay techniques. 

The introduction and eventual commercialization of matrix-assisted laser desorption/ionization (MALDI) and electrospray (ESI) allowed biomarker status to be extended to proteins in 1996.15"17 With a few exceptions, ESI has been used in conjunction with extractions and high-pressure liquid chromatography (UPLC) interfaced with mass spectrometry. MALDI, on the other hand, has been widely adapted for rapid analysis of intact organisms, supported by bioinformatics.1819... 

Demirev, P. A. Ramirez, J. Fenselau, C. Tandem mass spectrometry of intact proteins for characterization of biomarkers from Bacillus cereus T spores. Anal. Chem. 2001, 73, 5725-5731. 

Hathout, Y. Setlow, B. Cabrera-Martinez, R. M. Fenselau, C. Small, acid-soluble proteins as biomarkers in mass spectrometry analysis of Bacillus spores. Appl. Environ. Microbiol. 2003,69,1100-1107. 

Pineda, F. J. Antoine, M. D. Demirev, P A. Feldman, A. B. Jackman, J. Longenecker, M. Lin, J. S. Microorganism identification by matrix-assisted laser/desorption ionization mass spectrometry and model-derived ribosomal protein biomarkers. Anal. Chem. 2003,75,3817-3822. 

Many diseases are characterized by the expression of specific proteins1 in some cases, malignant cells yield unique protein profiles when total cellular protein extracts are analyzed by proteomic methods such as two-dimensional gel electrophoresis or matrix-assisted laser desorption ionization-mass spectrometry (MALDI-MS).2 High-throughput proteomic studies may be useful to differentiate normal cells from cancer cells, to identify and define the use of biomarkers for specific cancers, and to characterize the clinical course of disease. Proteomics can also be used to isolate and characterize potential drug targets and to evaluate the efficacy of treatments. 

High-throughput proteomic methods hold great promise for the discovery of novel protein biomarkers that can be translated into practical interventions for the diagnosis, treatment, and prevention of disease. These approaches may also facilitate the development of therapeutic agents that are targeted to specific molecular alterations in diseases such as cancer. In many cases, malignant cells yield unique protein profiles when total protein extracts from such cells are analyzed by 2-D gel electrophoresis or mass spectrometry (MS) methods. Such proteomic studies have the potential to provide an important complement to the analysis of DNA and mRNA extracts from these tissues.1... 

Hamdan, M.H., and Righetti, P.G. (2005) Proteomics Today Protein Assessment and Biomarkers Using Mass Spectrometry, 2D Electrophoresis, and Microarray Technology (Wiley-lnterscience Series on Mass Spectrometry), Wiley-lnterscience, ISBN-13 978-0471648178. 

If the scope of mass spectrometry is limitless, why are the applications of clinical MS almost completely small molecules The answer is that most clinical tests analyze small molecules, biomarkers that are either metabolites or steroids and, hence, mass spectrometers would target those first. Perhaps a more complete answer would also include that methods must be very robust, easily reproduced in different labs, reliable, and subjected to an extensive array of validation tests. Although peptide and protein analysis is increasing rapidly in clinical labs, the MS approaches to these assays is lagging behind somewhat. MS techniques targeting these peptides and proteins exist, but they are primarily in the research stage, with few systems and methods subjected to the clinical rigors of validation. Once the necessary validations occur and methods simplified, it will only be a short time before MS is used routinely in clinical proteomics. 

Liao, H., Wu, J., Kuhn, E., Chin, W, Chang, B., Jones, M.D., O Neil, S., Clauser, K.R., Karl, J., Hasler, F., Roubenoff, R., Zolg, W. and Guild, B.C. (2004) Use of Mass Spectrometry to Identify Protein Biomarkers of Disease Severity in the Synovial Fluid and Serum of Patients with Rheumatoid Arthritis. Arthritis Rheum, 50, 3792-3803. 

Traditional biochemical techniques such as liquid chromatography (LC), gel electrophoresis, capillary electrophoresis (CE), and mass spectrometry (MS) have been widely used for the complete analysis of salivary proteins and peptides. The recent advances in these technical approaches applied to peptidomics have allowed a better comprehensive analysis of peptides in human whole saliva, envisioning the identification of potential salivary biomarkers of oral and systemic diseases. Sample preparation is a critical experimental step for the successful identification of peptides using MS-based approaches, for their quantitation and identification of PTMs. 

Carr SA, Anderson L (2008) Protein quantitation through targeted mass spectrometry the way out of biomarker purgatory Clin Chem 54 1749-1752... 

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