Human proteins targeted in final 2006 Professorial Lecture

Nov 09, 2006

Research into the function of human proteins which may help society understand a variety of diseases caused by 'protein folding' was the focus of the final Professorial Lecture for the year.

A large audience shared the fascinating aspects of research being carried out by Professor Mark Wilson of the School of Biological Sciences. The topic of his address was "Cogs in the Extracellular Protein Quality Control Machine".

Professor Wilson arrived at UOW in 1994 and has focused his research on the function of human blood proteins, especially extracellular chaperones which is likely to be important for maintaining the viability of multicellular organisms and protecting people against a variety of diseases related to protein folding.

[Chaperones are proteins whose function is to assist other proteins in achieving proper folding. Protein folding is the process by which a protein assumes its characteristic functional shape.]

Professor Wilson has established a collaboration with a number of people at the University of Cambridge which will use the very latest techniques in transgenic animals (flies!) to test the role of extracellular chaperones in a model of Alzheimer's disease.

Professor Wilson told those attending the lecture that all life is dependent upon protein function, which in turn depends on the maintenance of proteins in their normal (native) shapes.

He said that in order to prevent inappropriate extracellular aggregation and deposition of proteins, and to preserve normal physiological functions, it is important to focus on how one or more protein quality control mechanisms operate in extracellular body spaces.

The capacity of these yet to be identified systems is probably exceeded in human diseases in which extracellular protein aggregation/ deposition is associated with pathology, Professor Wilson said.

"For example, in autoimmune diseases, circulating immune complexes accumulate in the kidney, joints and elsewhere and give rise to inflammatory responses," he said.

"There is also a large family of diseases (the Protein Conformational Disorders; e.g. Alzheimer's disease, prion diseases, Type II diabetes) in which proteins partially unfold in response to mutations, or physical or chemical stresses, and form pathological extracellular aggregates."