Juergen Kast

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Juergen Kast

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Research and Teaching Interests

In synthetic chemistry, a few reactants are mixed with a solvent, placed in a vessel and allowed to react for a specified time under defined conditions. Spectroscopic methods are then used for the analysis of the resulting mixture as a whole, or of individual compounds upon isolation if more detailed information is required. Proteomics – the study of the proteins present in a cell, tissue, or organism – follows the same general concept. It has to operate on a very different scale, however. Specifically, it needs to account for the potential presence of millions of compounds in the sample, deal with the dramatically increased number of possibilities of reactions, or interactions, between these compounds, and keep track of any quantitative changes they may undergo. Nonetheless, basic chemical principles still apply, and spectroscopic methods can still be used for sample analysis. Due to the vastly increased numbers of compounds, an analytical technique capable of handling complex mixtures and distinguishing compounds by inherent molecular and submolecular characteristics would be highly preferential for proteome research.

Modern mass spectrometry has proved to best fit that description. Invented more than a century ago by Sir Joseph John Thomson (1906 Nobel prize in Physics) – mass spectrometry has traditionally been used to study the composition of atoms and small molecules. The introduction of the soft ionization techniques electrospray and laser desorption (2002 Nobel prices in Chemistry awarded to John B. Fenn and Koichi Tanaka) in the late 1980’s enabled the direct analysis of biological macromolecules such as DNA, RNA, and proteins. Advances in MS instrumentation, DNA sequencing, and computer technology now make possible the analysis of increasingly complex mixtures, establishing mass spectrometry as an essential analytical technique in proteomics.

In our research, we heavily rely on mass spectrometry to study cellular reactions and their products, to identify the proteins present in human cells, their interactions, and any modifications they may undergo. Comparing this information across multiple cellular states allows us to gain a better understanding of how the system is balanced, and how it responds to changes. We can determine, for example, how certain blood cells receive and process external signals and how specific drugs influence these mechanisms. To accomplish this, we utilize mass spectrometry to characterize the products of chemical reactions such as cross-linking of proteins in live cells and stable isotope labeling of proteins or peptides, identify drug-induced protein modifications and other cellular responses, and to trace them with high specificity and sensitivity in targeted experiments across multiple states. Step by step, this provides us with a detailed picture of the various cellular processes and their underlying biochemical mechanisms. For details on current projects, please click on "Biomedical Research Centre" above.

Contact

Real name: 
Email: 
Office Room Number(s): 
Biomedical Research Centre 401
Office Phone Number: 
604-822-7841
Office Hours: 
Tu (2-3 pm) & Th (3-4 pm), D324
Fax Number: 
604-822-7815

Curriculum Vitae

Diploma, University of Konstanz (1993); Ph.D., University of Konstanz (M. Przybylski, 1998); Postdoc, EMBL Heidelberg (M. Wilm, 1998-2001)

Publications

2009

Wong, J. P. ; Reboul, E. ; Molday, R. S. ; Kast, J. A Carboxy-Terminal Affinity Tag For The Purification And Mass Spectrometric Characterization Of Integral Membrane Proteins. Journal of Proteome Research 2009, 8, 2388-2396.
Hoffman, M. D. ; Walsh, G. M. ; Rogalski, J. C. ; Kast, J. Identification Of Nitroxyl-Induced Modifications In Human Platelet Proteins Using A Novel Mass Spectrometric Detection Method. Molecular & Cellular Proteomics 2009, 8, 887-903.
Walsh, G. M. ; Lin, S. ; Evans, D. M. ; Khosrovi-Eghbal, A. ; Beavis, R. C. ; Kast, J. Implementation Of A Data Repository-Driven Approach For Targeted Proteomics Experiments By Multiple Reaction Monitoring. Journal of Proteomics 2009, 72, 838-852.
Gossens, K. ; Naus, S. ; Corbel, S. Y. ; Lin, S. J. ; Rossi, F. M. V. ; Kast, J. ; Ziltener, H. J. Thymic Progenitor Homing And Lymphocyte Homeostasis Are Linked Via S1P-Controlled Expression Of Thymic P-Selectin/ccl25. Journal of Experimental Medicine 2009, 206, 761-778.

2008

Toews, J. ; Rogalski, J. C. ; Clark, T. J. ; Kast, J. Mass Spectrometric Identification Of Formaldehyde-Induced Peptide Modifications Under In Vivo Protein Cross-Linking Conditions. Analytica Chimica Acta 2008, 618, 168-183.
Sutherland, B. W. ; Toews, J. ; Kast, J. Utility Of Formaldehyde Cross-Linking And Mass Spectrometry In The Study Of Protein-Protein Interactions. Journal of Mass Spectrometry 2008, 43, 699-715.
Hoffman, M. D. ; Sniatynski, M. J. ; Kast, J. Current Approaches For Global Post-Translational Modification Discovery And Mass Spectrometric Analysis. Analytica Chimica Acta 2008, 627, 50-61.
Thon, J. N. ; Schubert, P. ; Duguay, M. ; Serrano, K. ; Lin, S. J. ; Kast, J. ; Devine, D. V. Comprehensive Proteomic Analysis Of Protein Changes During Platelet Storage Requires Complementary Proteomic Approaches. Transfusion 2008, 48, 425-435.

2007

Hoffman, M. D. ; Rogalski, J. C. ; Sniatynski, M. J. ; Locke, J. ; Kast, J. A Multiplexed Post-Translational Modification Monitoring Approach On A Matrix-Assisted Laser Desorption/ionization Time-Of-Flight/time-Of-Flight Mass Spectrometer. Rapid Communications in Mass Spectrometry 2007, 21, 2147-2156.

2006

Hoffman, M. D. ; Sniatynski, M. J. ; Rogalski, J. C. ; Le Blanc, J. C. Y. ; Kast, J. Multiple Neutral Loss Monitoring (Mnm): A Multiplexed Method For Post-Translational Modification Screening. Journal of the American Society for Mass Spectrometry 2006, 17, 307-317.
Hoffman, M. D. ; Kast, J. Mass Spectrometric Characterization Of Lipid-Modified Peptides For The Analysis Of Acylated Proteins. Journal of Mass Spectrometry 2006, 41, 229-241.

2005

Wu, W. W. H. ; Wong, J. P. ; Kast, J. ; Molday, R. S. Rs1, A Discoidin Domain-Containing Retinal Cell Adhesion Protein Associated With X-Linked Retinoschisis, Exists As A Novel Disulfide-Linked Octamer. Journal of Biological Chemistry 2005, 280, 10721-10730.
Rogalski, J. C. ; Lin, M. S. ; Sniatynski, M. J. ; Taylor, R. J. ; Youhnovski, N. ; Przybylski, M. ; Kast, J. Statistical Evaluation Of Electrospray Tandem Mass Spectra For Optimized Peptide Fragmentation. Journal of the American Society for Mass Spectrometry 2005, 16, 505-514.

Research Projects