Welcome to the Otago School of Medical Sciences
Great Start to the Festive Season
11 December 2013
The 2013 OSMS Foodbank Challenge, organised by the departmental financial staff members, was a great success.
The departments each collected a different type of food;
Anatomy donated dried goods, Biochemistry was in charge of tinned food, Microbiology and Immunology collected breakfast items and beverages, Pharmacology and Toxicology donated desserts and snacks and Physiology donated bottles and jars.
Trish and Tracey from Presbyterian Support Otago picked up the donations today and were very impressed by your generosity. They just managed to squeeze all the boxes into their car.
A big thank you to everyone who contributed to help make the holidays a little easier for people in need.
Royal Society Fellows
28 November 2013
Two OSMS Professors are among the six Otago academics recently elected as Fellows of the Royal Society of New Zealand. Congratulations to Professor Lisa Matisoo-Smith (Department of Anatomy) and Professor Greg Cook (Department of Microbiology and Immunology) for their well-deserved achievement!
More information about the newly elected Royal Society Fellows can be found here.
In the cradle of the double helix: a novel proposal for the origin of life
27 November 2013
Dr Harold Bernhardt (Department of Anatomy) will use his recently awarded Marsden FastStart grant ($300,000) to continue his innovative research on “In the cradle of the double helix: a novel proposal for the origin of life”.
On February 28th 1953 in Cambridge England, two men walked into their local pub and announced that they had “discovered the secret of life!”, which, as it turns out, wasn’t too far from the truth. The men of course were James Watson and Francis Crick, and they had worked out that the structure of DNA was a double helix, which – with its specific pairing of A with T and C with G – suggested the means by which duplication of a genetic message could occur, thereby explaining the mechanism of inheritance. In the sixty years since then, the iconic power of the double helix as a symbol of life’s innermost workings has, if anything, only increased. In light of this, it may not be too much of a surprise that our recent work suggests this structure may be even more important than previously thought, potentially playing a critical role in the origin of life. Specifically, we propose that double helical regions of DNA’s sister molecule RNA (in which A pairs with U rather than T) provided a protective microenvironment – or cradle – for life’s early development.
Why RNA? The RNA world hypothesis holds that RNA, with its dual ability to function as genetic material and catalyze chemical reactions, preceded both DNA and proteins in evolution. But where did RNA come from? RNA is itself a fairly complex molecule, being composed of strings of the nucleotide bases A, C, G and U connected by a ribose phosphate backbone; a strand of RNA typically contains a mixture of single- and double-stranded (or double helical) regions. It has been thought that the bases evolved first, and were then connected up to form an RNA chain, much like the joining together of pieces of LEGO. However, the isolated bases have little affinity for each other, with pairing only occurring when they are joined to a ribose phosphate backbone (as they are in RNA). Partly for this reason, we propose that the bases evolved in situ, connected to a pre-existing ribose phosphate backbone.
How might this have happened? Prior to the advent of replication and Darwinian evolution, it seems likely there occurred a period of chemical evolution, where molecular ‘survival’ was dependent upon chemical stability. We propose that the bases arose during this time from simpler precursors that formed interactions which stabilized a ribose phosphate polymer against degradation, interactions that were the forerunners to the base pairing and stacking that occur in modern RNA. Critically, some of the reactions that produce RNA bases in cells today can also occur spontaneously through reactions between ribose and simple molecules thought to have been present on the early Earth; it is likely that such reactions played a role in the chemical evolution of RNA. Our research seeks to explore whether all the reactions required to form RNA can occur spontaneously; we will computer model and hopefully synthesize potential RNA precursors, and determine their structure and stability. This project may shed light not only on early RNA evolution, but also into the structure and function of modern RNA.
Identifying the mechanisms by which CaMKII regulates cellular signaling in the diabetic heart
22 November 2013
Dr Jeffrey Erickson (Physiology) was recently awarded a FastStart Marsden grant of $300,000 for his research on “Identifying the mechanisms by which CaMKII regulates cellular signaling in the diabetic heart”.
One of the critical underlying problems associated with diabetes mellitus is an inability to control blood-sugar (glucose) levels. Consequently, diabetic patients are subjected to chronic hyperglycemia, or elevated glucose concentration in the blood. Long term hyperglycemia has profound effects on the signaling mechanisms that control our basic physiological functions. This association between hyperglycemia and human pathology is of great concern from a health care perspective, because the incidence of diabetes is rising rapidly in New Zealand and around the world.
People suffering from diabetes are more than twice as likely to develop heart diseases compared with non-diabetics, and sudden heart failure remains the most common cause of death amongst those with the disease. However, the biological events that connect diabetes to heart diseases have not yet been determined. Emerging research by my group has identified novel links between hyperglycemia and heart diseases. Our recent findings, published in the October 2013 edition of Nature, describe the mechanism by which hyperglycemia can lead to modifications of the protein CaMKII – the possible missing link between diabetes and heart failure.
Thus, our group was recently awarded a Marsden Fast-Start grant to further explore the implications of this important finding at the University of Otago. In particular we will focus on how modified CaMKII protein causes arrhythmia and cell death in the diabetic heart.
Importantly, while this study focuses on the diabetic heart, our findings could have broader implications for other tissue types that express CaMKII, including the brain and kidneys. Ultimately, our goal is to develop novel therapeutic strategies to extend lifespan and improve the overall quality of life in diabetic patients.