Dr. Dale W. Laird

Professor and Canada Research Chair in Gap Junctions and Disease (Cross Appointment with Physiology and Pharmacology)

Ph.D. University of British Columbia
M.Sc. University of British Columbia
B.Sc. University of Prince Edward Island

Office: 00077 Dental Sciences Building
Phone: 519-661-2111 Ext. 86827
Fax: 519-850-2562
Email: Dale.Laird@schulich.uwo.ca
Visit: Dr. Laird's Home Page

Research Interests:

Dr. Laird’s research program focuses on the role of gap junctions in human health and disease. Mutations in ten genes that encode members of the connexin family of gap junction proteins lead to a wide range of human diseases that include developmental disorders, hearing loss, skin defects and neuropathies. Moreover, the ability of connexins to control the growth of cancer cells led to connexins being defined as tumor suppressors. Dr. Laird’s research centers around three themes related to normal connexin assembly and turnover, defects in disease-causing connexin mutants and mechanisms of connexin down-regulation in human breast cancer. These studies have expanded in recent years to encompass a second class of channel forming proteins called pannexins. Experimental approaches in each of these focal areas rely on biochemical, molecular, histological and cell imaging technologies. In addition, Dr. Laird’s team actively uses several mutant mouse models of connexin-linked human diseases and has now developed novel human models of human disease where wet-bench research findings are correlated with the clinical setting. His research program is currently 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

 

Selected Publications:

  1. R. Gehi, Q. Shao, D.W. Laird (2011) “Pathways regulating the trafficking and turnover of Pannexin1 and the role of the carboxyl terminal domains” Journal of Biological Chemistry 286: 27639-27653.

  2. J.M. Churko, J. Chan, Q. Shao and D.W. Laird (2011) “The G60S connexin43 mutant regulates hair growth and hair fiber morphology in a mouse model of human oculodentodigital dysplasia” Journal of Investigative Dermatology (in press).

  3. J.M. Churko, Q. Shao, X-Q Gong, K. Swoboda, D. Bai, J. Sampson, D.W. Laird (2011) “Human dermal fibroblasts derived from oculodentodigital dysplasia patients suggest that patients have wound healing defects” Human Mutation 32: 456-466.

  4. I. Plante, M.K.G. Stewart, K. Barr, A.L. Allan and D.W. Laird (2011) “Cx43 suppresses mammary tumor metastasis to the lung in a Cx43 mutant mouse model of human disease” Oncogene 30:1681-1692.\

  5. F.B. Chekeni, M.R. Elliot, J.K. Sandilo, S.F. Walk, J.M. Kinchen, E.R. Lararowski, A.J. Armstrong, S. Penuela, D.W. Laird, G.S. Salvesen, B.E. Isakson, D.A. Bayliss and K.S. Ravichandran (2010) “Pannexin 1 channels regulate “find-me” signal release and membrane permeability during apoptosis” Nature 467:863-867.

  6. J.M. Churko, S. Langlois, X. Pan, Q. Shao and D.W. Laird (2010) “The potency of the fs260 Cx43 mutant to impair keratinocyte differentiation is distinct from other disease-linked Cx43 mutants” Biochemical Journal 429: 473-483.

  7. C.C. Naus and D.W. Laird (2010) “Implications and challenges of connexin connections in cancer” Nature Cancer Reviews 10:435-441.

  8. S. Langlois, K.N. Cowan, Q. Shao, B.J. Cowan and D.W. Laird (2010) “The tumor suppressive function of connexin43 in keratinocytes is mediated in part via interaction with caveolin-1” Cancer Research 70: 4222-4232.

  9. S.J. Celetti, K.N. Cowan, S. Penuela, Q. Shao and D.W. Laird (2010) “Implications of pannexin 1 and Pannexin 3 for keratinocyte differentiation” Journal of Cell Science 123: 1363-1372.

  10. R. Bhalla-Gehi, S. Penuela, J.M. Churko, Q. Shao and D.W. Laird (2010) “Pannexin1 and Pannexin3 delivery, cell surface dynamics and cytoskeletal interactions” Journal of Biological Chemistry 285: 9147-9160.

  11. I. Plante, A. Wallis, Q. Shao and D.W.Laird (2010) “Milk secretion and ejection are impaired in the mammary gland of mice harboring a Cx43 mutant but molecular constituents of tight and adherens junctions remain intact” Biology of Reproduction 82: 837-847.

  12. D.W. Laird (2010) “The gap junction proteome and its relationship to disease” Trends in Cell Biology 20:92-101.