Members of the Lajoie Team
BMSL Manager
As Manager of the Biological Mass Spectrometry Laboratory, I am responsible for general upkeep and maintenance of the instruments in the lab, training of personnel, interacting with engineers, and performing experiments for both service and collaborative research. I have been involved in several collaborative projects pertaining to the identification of proteins, post-translational modification of proteins (phosphorylation, sulfation, glycosylation, etc.), as well as identification of phospholipids and secondary metabolites, etc. Whenever I have time, I study gas phase protein-protein interactions by ESI MS. For further information about our facility, please go to our web site.
I joined Professor Lajoie's team as a Laboratory Technician with a Bachelor’s degree in Chemistry from McMaster University. I have over 12 years of experience in both the Chemical and Pharmaceutical QC/QA industries. My responsibilities in the Don Rix Protein Identification Facility/Biological Mass Spectrometry Lab and in the Peptide Synthesis lab include the operation and maintenance of various instruments such as HPLC, capillary HPLC, MALDI R mass spectormeter, and electrospray-based mass spectormeters namely the triple quadrupole, the Q-ToF2 and the Micro Q-ToF. I am involved in various projects pertaining to the purification and characterization of biomolecules such as synthetic peptides, peptides from trypsin digestion as well as recombinant proteins, etc.
I joined Professor Lajoie's team as a Research Technician in June 2002. My background is in both molecular biology and bioinformatics. My responsibilities in the Don Rix Protein Identification Facility/Biological Mass Spectrometry Lab include mass spectrometry data processing and analysis, new program evaluation, method development and sample preparation, designing and adapting protocols to meet the needs of the various research projects, and designing databases for mass spectrometry as well as data management. I am also involved with the training of students for mass spectrometry data analysis and database searches.
I have several years of accounting and audit experience including experience in the financial, academic and public sectors of the economy. As Financial Officer for the Ontario-Wide Protein Identification Facility my responsibility includes the review, analysis and the financial reporting of the project funds for UWO and all the participating partners.
James Leushner is the Business Development Officer of the Ontario Wide Protein Identification Facility (OWPIF). He holds a Masters and PhD in molecular biology and has published widely on a variety of scientific and business topics. Jim has broad experience in both large and small public and private sector organizations. He developed marketing strategies and strategic alliances on an international level most recently as Director Business Development of Sequenom, a Genomics company in San Diego and, prior to that with Visible Genetics in Toronto. His current role is to provide business leadership to the OWPIF to expand and strengthen their position as the premier provider of state-of-the-art proteomic services to Ontario's academic and industry researchers.
Cyclic peptides play an important role in the study and design of useful therapeutic agents. They can be used to mimic protein turn regions and motifs. An important feature of cyclic peptides is that they are typically more stable to proteolytic degradation than their linear forms. Cyclic peptide analogs have shown utility as antibacterial, antiproliferative, as well as metal binding agents.
We are interested in evaluating methods for the synthesis of 3 to 8 amino acid (all L conformation) cyclic peptides, using chemistry that is compatible with standard Fmoc solid phase peptide synthesis (SPPS) protocols. The project involves the selective introduction of acid-labile backbone amide N-protecting groups that are removed in mild standard conditions after cyclization.
MSc Student, Study of potential binding targets of histatin 5 (H5) in Saccharomyces cerevisiac
Histatins are peptides found in human saliva and, due to their potency and low toxicity, have been considered as candidates for the development of new drugs for treating fungal infections.1 Histatin 5 and histatin 3 have been shown to be the most potent antifungals within the histatin family. Potent analogs were designed in our laboratory.2 Three different targets have been suggested for histatin 5 in Candida albicans.3,4,5 In our lab, histatin 5 is being studied using Saccharomyces cerevisiae, a non-pathogenic fungi found to be quite similar in its morphology to Candida albicans. Three different approaches to determine possible targets or mechanisms of action are being developed:
MSc Student, Mapping the locations of phosphorylated residues on native rat bone osteopontin using mass spectrometry
Osteopontin (OPN) is a phosphorylated glycoprotein that occurs at high levels in bone but is also present at sites of pathological calcification such as kidney stones and atherosclerotic plaque. The major focus of this project is to find the phosphorylation sites on OPN and determine their biological function. Previous studies in the laboratories of Dr. Graeme K. Hunter and Dr. Harvey Goldberg demonstrated that OPN is a potent inhibitor of hydroxyapatite (HA) crystal formation. However, different forms of OPN (native, recombinant protein, bone isoform and kidney isoform) exhibit different degree of HA inhibition suggesting that phosphorylation of this protein is an important modular of its function. MS can also accurately provide the molecular mass of the intact phosphorylated protein allowing the determination of average number of attached phosphate group. To determine the exact site (s) of phosphorylation on both recombinant and native OPN from rat bone, we are using a combination of proteolytic digestion and tandem mass spectrometry (MS/MS).
I obtained my Ph.D. degree in Biochemistry at the Lomonosov Moscow State University, Russia. Currently, I am working as a Post Doctoral Fellow at the laboratory of Dr. Graeme K. Hunter and Dr. Harvey Goldberg. We collaborate with the laboratory of Proefrssor Gilles Lajoie for synthesis of vairous peptides, including phosphopeptides, corresponding to fragments of osteopontin (OPN) and of bone sialoprotein (BSP). This bone proteins are extracelluar matrix proteins which have been shown to be involved in the processes of mineral cristallisation. This study will provide fundamental information on how these proteins are involved in tissue regeneration and inflammatory processes. This will be important for the development therapeutic reagents to promote mineralization at bone repair sites, and to inhibit pathological calcification in vivo.
My project involves the study of post-translational modifications in eukaryotic cells with respect to protein phosphorylation and protein stability. In particular, I will be using immobilized metal affinity chromatography (IMAC) to study Protein Kinase CK2 in mammalian cells in collaboration with my former PhD supervisor Dr. David W. Litchfield. Protein Kinase CK2 is a serine/threonine/tyrosine kinase that participates in numerous pathways involved in cellular signaling. Aberrent levels of CK2 have been observed in tumour cell lines. However, the precise mechanisms of how CK2 alters cellular signaling are still poorly understood. Identifying novel targets of CK2 will lead to a better understanding of the role of this interesting kinase in mammalian cells.
I obtained my PhD on bioanalytical chemistry at Wuhan University, China in 1998. Currently I am working in Professor Lajoie Group as a postdoctoral fellow. My project is focusing on proteomic quantification of proteins and peptides using mass spectrometry, especially ICAT, O18 labeling and other stable isotope labeling by chemical modification. We hope to standardize methods applied to biosamaples.
Suya Liu, Ph.D.
Post Doctoral Fellow, Proteomics
I received my PhD degree from Karolinska Institutet, Stockholm, Sweden, in 2003. During my PhD study, supervised by Dr. William G. Griffiths and Professor Jan Sjovall, I worked on capillary liquid chromatography / electrospray mass spectometry for the analysis of neurosteroids from rat brain. Currently, I am working as a Post Doctoral Fellow in the laboratories of Professor Gilles A. Lajoie and Dr. Victor Han. The joint project is the study of the molecular mechanism of preeclampsia, with an aim to look for diagnostic markers. The project involves proteomics analysis as well as metabolomics analysis by MS and LC/MS.
----- 
----- 
----- 
----- 
----- 
----- 
\
