Contact Waterloo Institute for Nanotechnology
Mike & Ophelia Lazaridis Quantum-Nano Centre, Room 3606
University of Waterloo
200 University Ave. W.
Waterloo, ON. N2L 3G1
+1 519 888 4567, ext.38654
Research interests: mitochondrial biogenesis and myopathies; microfluidics, assembly of cytochrome oxidase
Professor Moira Glerum obtained her PhD in Biochemistry from the University of Toronto in 1998, working under the supervision of Professor Brian Robinson, an expert in inherit metabolic diseases, at The Hospital for Sick Children. Following postdoctoral training in the laboratory of Professor Alexander Tzagoloff at Columbia University in New York City, where she was supported by an MRC postdoctoral fellowship, Glerum took a position as Assistant Professor in Medical Genetics at the University of Alberta in Edmonton (1997). Glerum was promoted to Associate Professor with Tenure in 2003 and became a Full Professor in the Department of Cell Biology in January 2009. In July 2011, Glerum moved into her present position as a Professor in the Department of Biology at the University of Waterloo.
- PhD, Biochemistry, University of Toronto, 1990
- BSc, Biochemistry, University of Toronto, 1984
Professor Moira Glerum has developed a research program aimed at understanding the macromolecular assembly pathway for cytochrome oxidase (COX), the terminal electron acceptor in the mitochondrial respiratory chain. Using yeast as a model system, Dr Glerum's research has identified and characterized novel proteins involved in COX assembly. Since mutations in some of these proteins result in a spectrum of inherited diseases, her studies in yeast have improved our understanding of the molecular mechanisms underlying human mitochondrial disorders. Her current studies are geared towards understanding the relationship between copper provision/distribution and mitochondrial peroxide metabolism.
Mitochondrial myopathies; mitochondrial biogenesis; assembly of cytochrome oxidase in yeast and humans.
Mitochondria are the "power plants" of our cells and generate almost all of the energy we need to live. The failure of these energy generators results in a wide variety of human diseases. In fact, defects in mitochondrial function may be the most common underlying cause of neurodegenerative disease! Mitochondria are created from proteins encoded in two different genomes - the nuclear and the mitochondrial. Our lab is studying the contributions of both of these genomes to neurodegenerative diseases and cancer. The nuclear genome encodes most of the proteins required for mitochondrial formation. One of the key enzymes found in mitochondria is cytochrome oxidase (COX), which consists of 13 subunits - 3 encoded in mtDNA and 10 encoded in the nucleus. However, there are also more than a dozen proteins involved in ensuring that COX is correctly assembled, all of which are also encoded in the nucleus. The COX assembly pathway is most often defective in human COX deficiencies, which are the most common of the mitochondrial respiratory chain disorders. These diseases usually present early in life and are almost always fatal. The COX assembly pathway is still only partially understood and we are using yeast as a model system for delineating this process. Our studies are furthering our understanding of how mutations in COX assembly genes result in fatal neurological disease. Microfluidic chip, or lab-on-a-chip, technologies have the potential to revolutionize both health care delivery and biomedical research. Given the ever-increasing list of disorders with a documented mitochondrial dysfunction, technologies that would enable us to investigate mitochondrial function at the level of a single cell would further our understanding of the contributions of this organelle to disease pathologies. In collaboration with the Backhouse lab in Electrical and Computer Engineering, we are therefore also developing microfluidic chip-based assays for use in studying mitochondrial disease.
Martinez-Quijada, Jose; Ma, Tianchi; Hall, Gordon H.; Reynolds, Matt; Sloan, David; Caverhill-Godkewitsch, Saul;Glerum, D. Moira; Sameoto, Dan; Elliott, Duncan G.; Backhouse, Christopher J., “Robust thermal control for CMOS-based lab-on-chip systems”, JOURNAL OF MICROMECHANICS AND MICROENGINEERING, 25(7), (2015)
Hall, Gordon H.; Sloan, David L.; Ma, Tianchi; Couse, Madeline H.; Martel, Stephane; Elliott, Duncan G.; Glerum, D. Moira; Backhouse, Christopher J., “An optical relay approach to very low cost hybrid polymer-complementary metal-oxide semiconductor electrophoresis instrumentation”, JOURNAL OF CHROMATOGRAPHY A, 1349, pp122-128, (2014)
Hall, Gordon H.; Ma, Tianchi; Couse, Madeline H.; Hume, Stacey; Sloan, David L.; Elliott, Duncan G.; Glerum, D. Moira; Backhouse, Christopher J., “An automated hand-held CMOS-based instrument for hand-held mutation detection via electrophoresis”, 2014 IEEE 14TH INTERNATIONAL CONFERENCE ON NANOTECHNOLOGY (IEEE-NANO), pp8-12, (2014)
Ma, Tianchi; Northrup, Victoria; Fung, Andrew O.; Glerum, D. Moira; Backhouse, Christopher J., “Polymeric rapid prototyping for inexpensive and portable medical diagnostics”, PHOTONICS NORTH 2012, 8412, (2012)
- Veniamin, S., Sawatzky, L.G., Banting, G., Glerum, D.M. (2011) Characterization of the peroxide sensitivity of COX deficient yeast strains reveals unexpected relationships between COX assembly proteins. Free Rad. Biol. Med., in press.
- Northrup, V.A., Backhouse, C.J., Glerum, D.M. (2010) Development of a microfluidic chip-based plasmid miniprep. Anal. Biochem. 402, 185-190.
- Manage, D.P., Imriskova-Sosova, I., Glerum, D.M., Backhouse, C.J. (2008) A microfluidic study of mechanisms in the electrophoresis of supercoiled DNA. Electrophoresis, in press.
- Hsi, G., Cullen, L.M., Macintyre, G., Chen, M.M., Glerum, D.M., Cox, D.W. (2008) Mutations in the ATP-binding domain of the Wilson Disease Protein, ATP7B, affect Copper Transport in a Yeast Model System. Hum. Mutat. 29, 491-501.
- Zhu, Y., Antony, J., Martinez, J.A., Glerum, D.M., Brusse, V., Hoke, A., Zochodne, D., Power, C. (2007) Didanosine causes sensory neuropathy in an HIV/AIDS animal model: impaired mitochondrial and neurotrophic factor gene expression. Brain 130, 2011-2023
- Zee, J.M., Glerum, D.M. (2006) Defects in cytochrome oxidase assembly in humans: lessons from yeast. Biochem. Cell Biol. 84, 859-869.
- Banting, G.S., Glerum, D.M. (2006) Mutational analysis of the Saccharomyces cerevisiae cytochrome c oxidase assembly protein, Cox11p. Euk. Cell 5, 568-578.
- Taylor, P., Manage, D.P., Helmle, K.E., Zheng, Y., Glerum, D.M., Backhouse, C.J. (2005) Analysis of mitochondrial DNA in microfluidic systems. J. Chrom. B 822, 78-84.
- Williams, J.C., Sue, C., Banting, G.S., Yang, H., Glerum, D.M., Hendrickson, W.A., Schon, E.A. (2005) The crystal structure of human SC
- O1, a mitochondrial respiratory chain "assembly" protein: implications for peroxidase activity and redox signaling. J. Biol. Chem. 280, 15202-15211.
- Marriage, B.J., Clandinin, M.T., MacDonald, I.M., Glerum, D.M.(2004) Improvement in ATP synthetic capacity in patients with oxidative phosphorylation disorders. Molec. Genet. Metab. 81, 263-272.
- Marriage, B.J., Clandinin, M.T., Glerum, D.M. (2003) Nutritional cofactor treatment in mitochondrial disorders. J. Am. Diet. Assoc. 103, 1029-1038.
- Punter, F.A., Glerum, D.M. (2003) Random mutagenesis identifies a specific role for Cox17p in copper transport to cytochrome oxidase. J. Biol. Chem. 278, 30875-30880.
- Marriage, B.J., Clandinin, M.T., MacDonald, I.M., Glerum, D.M.(2003) The use of lymphocytes in the detection and monitoring of oxidative phosphorylation disorders. Anal. Biochem. 313, 137-144.
- Carlson, C.G., Barrientos, A., Tzagoloff, A., Glerum, D.M. (2003) COX16 encodes a novel protein required for the assembly of cytochrome oxidase in Saccharomyces cerevisiae. J. Biol. Chem. 278, 3770-3775.
- Antonicka, H., Mattman, A., Carlson, C.G., Glerum, D.M., Leary,S.C., Kennaway, N., Shoubridge, E.A.(2003) Mutations in COX15 produce a defect in the mitochondrial heme biosynthetic pathway causing early onset fatal hypertrophic cardiomyophathy. Am.J.Hum.Genet. 72, 101-114.
Office: QNC 3623
Phone: 519-888-4567, ext. 31352