Media Release Tuesday 27 September 2005
ComBio 2005 - Adelaide Convention Centre September 26-29
NEW INSIGHTS IN PROTEIN FUNCTION AND CONSEQUENCES FOR DISEASE
New scientific research is providing insights into failures of our natural defence systems that regulate the normal function of proteins resulting in potentially life-threatening diseases.
A major biological science conference in Adelaide today heard how so-called protein misfolding produced toxic species that kill normal cells resulting in conditions ranging from Alzheimer's and Parkinson’s disease to diabetes.
Chris Dobson, Professor of Chemical and Structural Biology at Cambridge University, told the ComBio 2005 conference that researchers had made spectacular advances in understanding the structure and function of proteins that regulate all the chemical processes upon which life depends.
“To function properly, proteins must respond to the information encoded in their sequences of amino acids and fold into specific structures,” Professor Dobson said.
“Protein folding is increasingly recognised as being coupled to many biological processes ranging from molecular trafficking to cell signalling and the regulation of cell cycle.
“This folding process is carefully regulated by enzymes and other proteins that are present in the body and it helps strengthen defences against disease.
“However, we have discovered that even perfectly normal protein molecules in the body are susceptible to unfolding and then sticking together to form clumps of misfolded aggregate.
“Once this occurs, some of the aggregate turns out to be highly toxic and itcan kill healthy cells with which the proteinsare normally associated. For example, such an event can kill neurons, or brain cells, resulting in Alzheimer’s disease and other neurodegenerative conditions.”
Professor Dobson said that by gaining greater understanding of the process of protein misfolding, researchersaregaining insights into the origins of many diseases.
“Potentially, this could lead to the development of drugs that will treat these diseases or prevent them from occurring.
“We know from our own experiments in the laboratory environment that a number of strategies based on such knowledge will work at least in principle.
“One exciting approach is to develop antibodies, a class of natural defence molecules,that will bind to selected proteins to stop or reduce the likelihood of unfolding and the onset of disease.”
Professor Dobson, a keynote speaker at the ComBio conference, said there were a number of influences that could stimulate the misfolding of otherwise normal proteinsincluding:
- genetic mutations giving rise to familial disease;
- ageing and a declining ability of the body’s natural defences against disease; and
- ingestion of proteins from organisms in which unfolding and aggregation has already occurred.
“We know, for example, that mad cow disease can be caused by young cows being fed meat from old cows in which aggregation had occurred,” he said.
“Last century there was evidence of a similar disease in humans through ritualistic cannibalism among remote tribes in Papua New Guinea.
“New research has provided an outline of how protein unfolding and aggregation occurs, and much of our efforts are now directed at measures to help the body maintain its natural defences through therapeutic strategies to maintain protein structure and function.”
The ComBio biological sciences meeting in Adelaide has brought together 900 delegates from around the world to report on new discoveries about diseases that affect millions of people around the world and crops that sustain vast populations.
ComBio 2005 is a joint meeting of the Australian Society for Biochemistry and Molecular Biology, the Australia and New Zealand Society for Cell and Developmental Biology and the Australian Society of Plant Scientists.
The conference will run at the Adelaide Convention Centre until Thursday.
For interview:
Professor Chris Dobson is available for interview. To arrange, please call Trevor Gill on 0418 821948