Welcome to the Otago School of Medical Sciences
Congratulations to new Professor and Associate Professors
29 January 2015
The OSMS is proud to announce that Rhonda Rosengren has been promoted to full professorship.
Congratulations to all on these well-deserved promotions.
In total the University announced 15 new Professors and 39 new Associate Professors. Read the University of Otago media release to find out more.
Salt Research in the Media
27 January 2015
Associate Professor Colin Brown is part of an international research team, led by Professor Charles Bourque of McGill University, which has advanced the understanding of the link between salt intake and blood pressure.
Genesis Oncology Trust Funding
21 January 2015
Congratulations to Dr Roslyn Kemp, Professor Catherine Day and Dr Sebastien Taurin, who were awarded Genesis Oncology Trust research project grants.
Dr Roslyn Kemp was awarded $39,407 for her project titled Improved survival with cimetidine in early colorectal cancer: impact on the Immunoscore.
Professor Catherine Day was awarded $54,335 for her research on Targeting ubiquitin pathways to control chronic inflammation.
Dr Sebastian Taurin was awarded $62,035 for his project titled Targeted delivery of raloxifene nanomedicine as a new therapeutic strategy for the treatment of castrate resistant prostate cancer.
Click here for more information about the funded projects.
Protein folding and quality control, one molecule at a time
26 January 2015
The Wilbanks lab investigates molecular chaperones, enzymes which manage the incorrectly folded protein molecules that contribute to degenerative diseases. A conundrum of twentieth century molecular biology was how the comparatively short set of instructions in the human (or any other organism's) genome can provide sufficient instructions to assemble all of the intricate three dimensional structures of the myriad proteins which make up the architecture of living cells: the motors that move them, the energy systems that power them, the enzymes which make their chemical building blocks and the signaling networks which controls it all. The conundrum was resolved by the Nobel-prize discovery that these proteins fold spontaneously to the correct shape. Each gene needs only to specify a particular order in which amino acids are joined to form a chain; given the correct sequence each chain can automatically folds into its unique three-dimensional shape.
But sometimes the process goes wrong, and this contributes to disease. Soon after this discovery, proofreading mechanisms, called molecular chaperones, were discovered which allow cells to detect protein chains that fail to fold into the correct shape, and to correct or eliminate the errant protein molecule. Understanding how molecular chaperones recognise incorrectly folded proteins and put them right is a fundamental challenge in twenty-first century molecular biology. The basic challenge is daunting: although there is only one correct way to fold most proteins, there are many wrong ways to fold one. How can a molecular chaperone detect them all? The problem is urgent at an applied level, as many neurodegenerative diseases, such as Alzheimer's and Huntington's, involve incorrect folding of proteins. Better understanding of the proofreading process can improve care for an ageing population.
If incorrectly folded proteins are each unique (just as Tolstoi described unhappy families in the opening lines of Anna Karenina) this poses a problem for the researcher as well as the molecular chaperone. Traditional biochemical techniques monitor many molecules at once. Such studies of molecular chaperones tell us about the average interaction of a chaperone with an average incorrectly folded protein, obscuring the details of individual variation. Advances for the last decade allow us now to monitor individual molecules. The Wilbanks lab has engineered a ubiquitous molecular chaperone, Hsp70, so that its action can be monitored with a sophisticated light microscope. Current research focuses on the bacterial family member, DnaK. Because the Hsp70 family is highly similar from bacteria to man, the behaviour of DnaK will show what the human version can do. A parallel thrust of the project is extending the study to the human family member, and its interaction with incorrectly folded proteins important in disease. Together these lines on inquiry ask fundamental questions: Where in a cell does Hsp70 find its incorrectly folded clients? For how long does it bind to each? How much variation is there between individual molecules? Answers to these simple questions will aid in therapies recruiting our endogenous molecular chaperones to fight disease.