Jens R. Coorssen

Jens R. Coorssen
Research Scholar
Top-down Proteomics
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My inter- and transdisciplinary training and research record includes graduate work in membrane biophysics, biochemistry, and cell physiology, a fellowship at the Max Planck Institute for Medical Research (electrophysiology/imaging), and an NIH Visiting Scientist position (molecular/cellular physiology and targeted proteomics). Following faculty appointments at U. Calgary (Faculty of Medicine and the Hotchkiss Brian Institute), I was recruited as Foundation Chair to help establish the Western Sydney University School of Medicine as well as the large, successful Molecular Medicine Research Group linking the university and local healthcare regions to promote the importance of quantitative molecular analyses in clinical and translational research. I returned to a faculty position in Canada in 2016. My mentorship, publication, funding, and service records are commensurate with a 30-year research career. My emphasis has always been on quantitative analyses of proteins and lipids, and thus the central importance of top-down analyses in identifying biologically active species.

     As a cornerstone of current research, the analysis of proteomes (i.e., the functional level of the genome) is complicated in that a given ‘gene product’ quite often exists as multiple different molecular species, most of which cannot be predicted from DNA or RNA sequences. Gene mutations, isoforms, splice variants, and myriad post-translational modifications tune protein function(s), localization(s), and interactions. Such modified ‘species’ — or proteoforms — are what make biology ‘happen’ (or not, as the case may be). Thus, proteoforms define proteomes, creating a level of dynamic complexity far beyond that of genomes or transcriptomes. ‘Generic’ amino acid sequences are thus insufficient to understand proteomes or the biological source material and/or physiological process(es) they underlie. To deeply assess proteomes, particularly to understand molecular mechanisms/pathways, and identify critical therapeutic targets or biomarkers, we must routinely resolve and analyze intact proteoforms; this is the most direct assessment of proteome complexity and critical alterations, and thus the best route to understanding physiological states.

     For >20 years, my research has focused heavily on developing a ‘next generation’ analytical approach by systematically optimizing integrative top-down proteomic analyses — from the moment of sampling through sample handling, prefractionation, 2D/3D gel electrophoresis/fixation/staining/washing, quantitative image analysis, and MS analyses to ensure maximal extraction of information per sample. My research has thus directly contributed to critical fundamental and clinical studies ranging from exocytosis to spinal cord assessment, novel anticancer agents, neurological diseases, assessment of preterm labour, the fundamental effects of exercise, and identifying alterations facilitating the infectivity of pathogenic organisms. I have also established and operated Proteomics and Lipidomics facilities, and thereby promoted the importance of quantitative molecular analyses in clinical and translational research.

            My ongoing efforts are directed to further refining top-down proteomic analyses to enhance rigor, throughput, and cost-effectiveness. The goal is to enable the wider application of deep, quantitative proteomic analyses.

Proteoforms, Electrophoresis, Molecular analyses, 'Omics, Healthspan, Biomarkers
Biomedical Sciences, Biotechnology, Health Sciences, Systems Science