Andy Hill
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Processing of proteins and RNA in neurodegenerative diseases
Neurodegenerative diseases such as Alzheimer’s and Parkinson’s disease have an increasing prevalence amongst ageing population. Recent estimates suggest the numbers of Australians suffering from dementia is set to double to 500,000 individuals by the year 2030. Many of these diseases are associated with the misfolding of certain proteins into aberrant forms that are found in the tissues of individuals with these diseases.
The Hill lab uses a combination of Biochemistry, Molecular and Cell Biology to investigate these diseases. Prion and Alzheimer’s diseases involve the processing of distinct proteins which when misfolded cause neurodegeneration. We are interested in understanding the molecular mechanisms by which these proteins exert their neurodegenerative properties and in the case of prion proteins, gain their infectious properties.
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Amyloid deposits (left) and spongiform change (right) in the brain are characteristic pathological features of prion disease. | |
Prion diseases such as Creutzfeldt‐Jakob disease (CJD) in humans and bovine spongiform encephalopathy (BSE or ‘mad‐cow’ disease) in cattle are invariably fatal neurodegenerative diseases. Prions differ from conventional infectious agents in being highly resistant to treatments that destroy the nucleic acids found in bacteria and viruses. The infectious prion is thought to be an abnormally folded isoform (PrPSc) of a host protein known as the prion protein (PrPC). The conversion of PrPC to PrPSc occurs post‐translationally and involves conformational change from a predominantly α‐helical protein to one rich in β‐sheet structure.
Alzheimer’s disease (AD) is the most common form of dementia in humans, of which the key pathological hallmark is the deposition of the 39‐46 amino acid beta‐amyloid peptide (Aβ) in the brain. Aβ peptides are derived from sequential cleavage of the amyloid precursor protein (APP) by β‐ and γ‐secretases.
We are investigating the processing and secretion of the prion protein and the APP in association with small membrane vesicles known as exosomes. We have shown that exosomes can transfer infectious prions between different cell types.
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