Signals and Chaperones: Learning to Speak Protein
The cells of any organism are regularly passing on information in the form of biochemical signals, which usually direct the cell to make internal physiological responses to changes in the surrounding environment. Such signals are also associated with the development of many different types of inflammatory and degenerative diseases, such as cancer and viral or bacterial infections. Researchers have become interested in identifying the nature and function of these signaling mechanisms, which could reveal new avenues for treating these diseases at the molecular level.
As holder of a Canada Research Chair, David Thomas will explore the operation of what he calls molecular machines, the physically and functionally interacting components of cells. His expertise will become part of the state-of-the-art Montreal Genomics and Proteomics Centre at McGill University, a facility that is expected to be completed in 2002. His work will also be a part of the integrated research that is going to be conducted at the McGill Life Sciences Complex.
His interests also extend to a specialized class of proteins known as chaperones, which oversee how proteins fold themselves into the correct shape to carry out their physiological duties. These proteins play a significant role in medical problems such as Alzheimer's disease or immune system disorders, a role that might serve as the target for an innovative drug therapy.
The work of Dr. Thomas and his colleagues builds on pioneering research into a molecular chaperone called calnexin, which acts as a quality control mechanism for mutant proteins found within cells. When this mechanism fails to function, the improper folding of molecules can result in degenerative diseases.