Dale W. Laird is a Professor in the Department of Anatomy and Cell Biology and the Department of Physiology and Pharmacology at the University of Western Ontario. His laboratory studies the connexin family of gap junction proteins and, more recently, a related set of proteins called pannexins.
Dale's research interests encompass studies related to the function of gap junction proteins, connexins, in health and disease. Areas of focus include; intracellular connexin trafficking, gap junction assembly and turnover, fluorescent-based live cell imaging, connexin mutants and their link to human diseases, connexin regulation and relationship to breast cancer, and the role of connexins in tissue differentiation and carcinogenesis. His research program is funded by grants from the Canadian Institutes of Health Research, the Canadian Breast Cancer Research Alliance, the Canada Research Chairs Program and the Canadian Foundation for Innovation.
Dale completed his PhD in Biochemistry from the University of British Columbia where he studied photoreceptor and retinal pigment epithelial cell interactions. After a productive Postdoctoral Fellowship at the California Institute of Technology where he began his studies on connexins, he accepted a position as an Assistant Professor at McGill University in Montreal. Following promotion to Associate Professor with Tenure, he relocated to the University of Western Ontario. Dale has been the recipient of the Premier's Research Excellence Award and the Medical Research Council Scientist Award. In 2004 he was awarded a Tier I Canada Research Chair in Gap Junctions and Disease. He is an Editor for Biochemical Journal and the Journal of Biological Chemistry.
His laboratory has been heavily engaged in imaging technologies for the past decade. They use Openlab software with a Leica fluorescent microscope equipped with an Eppendorf microinjection system and a Hamamatsu digital camera. Openlab is used to quantify functional gap junction mediated intercellular communication by assessing fluorescent dye transfer following single cell microinjection. The imaging workstation is also employed to acquire images suitable for localizing fluorescent protein tagged connexins (Figure 1) and disease-linked connexin mutants.
Dale writes “Openlab software has been invaluable to us for analyzing the functional status and localization of human disease-linked connexin mutants. Typically, we assess the channel forming properties of connexin mutants using fluorescent dye tracers prior to proceeding to use double labeling techniques to localize these mutants to specific subcellular compartments.”
For more information about Dale Laird’s research please visit his website.
Normal rat kidney cells expressing yellow fluorescent protein tagged-connexin26 (green) and immunolabeled for the resident Golgi protein TGN38 (red) counterstained with Hoechst 33342 dye to denote the nuclei (blue). Note the localization of connexin26 at sites of cell to cell apposition typical of gap junctions. Image courtesy of Jamie Simek.