Speakers at ICG-13

Speakers at ICG-13




























Dr. Borchers received his B.S., M.S. and Ph.D. from the University of Konstanz, Germany. After his post-doctoral training and employment as a staff scientist at NIEHS/NIH/RTP in North Carolina, he became the director of the UNC-Duke Proteomics Facility and held a faculty position at the UNC Medical School in Chapel Hill, NC (2001-2006). Since then, Dr. Borchers has been employed at the University of Victoria (UVic), Canada and holds the current positions of Professor in the Department of Biochemistry and Microbiology and the Don and Eleanor Rix BC Leadership Chair in Biomedical and Environmental Proteomics. He is also the Director of the UVic – Genome BC Proteomics Centre, which is a member of the Genome Canada funded Genomics Innovation Network.Dr. Borchers is also appointed asProfessor at McGill University in the Department of Oncology, Montreal, QC and where he holds the Segal Chair in Molecular Oncology at the Jewish General Hospital at McGill University.


Dr. Borchers’ research is centered around the improvement, development and application of proteomics technologies with a major focus on techniques for quantitative targeted proteomics for clinical diagnostics. Multiplexed LC-MRM-MS approaches and the immuno-MALDI (iMALDI) technique are of particular interest. Another focus of his research is on technology development and application of the combined approach of protein chemistry and mass spectrometry for structural proteomics. Dr. Borchers has published over 280 peer-reviewed papers in scientific journals and is the founder and CSO of two companies, Creative Molecules. Inc. and MRM Proteomics Inc. He is also involved in promoting proteomic research and education through his function as HUPO International Council Member, Past Scientific Director of the BC Proteomics Network and Vice-President, External of the Canadian National Proteomics Network. 


Quantitative Proteomics in Cancer Diagnosis

Frohlich B 1,2 , Popp R 1,2 , Aguilar-Mahecha A 3,4 , Basik M 5 , LeBlanc A 6 , Poetz O 7 , Borchers C 1,2,5,6

1 University of Victoria - Genome British Columbia Proteomics Centre, Victoria British Columbia, Canada. 2 Department of Biochemistry and Microbiology, University of Victoria, Victoria British Columbia, Canada. 3 Goodman Cancer Research Centre, McGill University, Montréal Quebec, Canada. 4 Department of Biochemistry, McGill University, Montréal Quebec, Canada. 5 Gerald Bronfman Department of Oncology, Segal Cancer Centre, Lady Davis Institute, Jewish General Hospital, Montréal Quebec, Canada. 6 Proteomics Centre, Segal Cancer Centre, Lady Davis Institute, Jewish General Hospital, McGill University, Montréal Quebec, Canada. 7 Natural and Medical Sciences Institute (NMI) at the University of Tübingen, Reutlingen Baden-Württemberg, Germany

Cancer is one area in clinical diagnostics where mass-spectrometry-based techniques are poised to make a significant impact. Many proteins have been found in “discovery” proteomics experiments to be up- or down-regulated in cancer patients, including proteins involved in specific cancer-related pathways.

To determine if these proteins are actual “biomarkers” – or to determine the levels of these proteins in patient samples -- involves quantitative proteomics.  For quantitating multiple protein targets, the “gold-standard” method is multiple reaction monitoring (MRM), a mass spectrometric technique involving a specific precursor ion and a specific fragment ion – typically with on-line LC separation.  In contrast, the technique of immuno-MALDI (iMALDI) utilizes affinity purification for the precise quantitation of a smaller number of extremely low-abundance target peptides, without LC separation and on instruments that are already utilized in clinics for bacterial identification.

Both techniques involve “bottom-up proteomics – i.e., the quantitation of peptides specific to a target protein as a surrogate for the intact protein.  In both techniques, cancer cell lysates are digested into peptides using trypsin, and stable-isotope labeled internal standard peptides (SIS peptides) are added to compensate for any changes in instrument performance or sensitivity. In LC/MRM-MS, the use of SIS peptides also compensates for any drift in LC retention time.

My laboratory has already developed ~250 MRM assays for plasma proteins.  Assays for other proteins in other biofluids (e.g., CSF and urine) and in other species -- for example, for phenotyping mouse models of human diseases, are also being developed.

My current research in iMALDI involves the PI3K/AKT/mTOR pathway, which is commonly upregulated in colorectal cancer and is the target of many anti-cancer therapies. iMALDI can be used to quantify the expression levels and phosphorylation status of key proteins in this pathway, which could be useful for patient stratification.


[1] Siegel RL, Miller KD, Jemal A, CA Cancer J Clin. 2015 Jan-Feb;65(1):5-29.

[2] Papadatos-Pastos D et al, Crit Rev Oncol Hematol. 2015 Apr;94(1):18-30

[3] Domanski D, Murphy LC, Borchers CH, Anal Chem. 2010 Jul 1;82(13):5610-20

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