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John Hardy, PhD, right, accepted the 2015 Robert A. Pritzker Prize from MJFF VP Brian Fiske, PhD, and Michael J. Fox on April 15.

John Hardy awarded 2015 Robert A. Pritzker Prize for Leadership in Parkinson's Research

One of the UK Parkinson's Disease Consortium Principal Investigators, Prof John Hardy, has been awarded the 2015 Robert A. Pritzker Prize for his leadership in Parkinson's genetics research. The award was presented by Michael J. Fox at a ceremony in New York on April 15. From the Michael J. Fox Foundation website: More...

Webcast - Prof Nicholas Wood - Advances in Genetic Understanding of Parkinson's Disease.

Video: Advances in Genetic Understanding of Parkinson's Disease

Webcast of the presentation entitled ‘Advances in Genetic Understanding of Parkinson's Disease’ given by Nicholas Wood (University College London, United Kingdom) presented at the Biochemical Society Hot Topic event, PINK1-Parkin Signalling in Parkinson’s Disease and Beyond, held in December 2014. More...

Pedigrees and I-FP-CIT SPECT scan images of the four families with GCH1 mutations involved in this study.

GCH1 gene and Parkinson's risk

A study published in Brain, led by researchers at UCL Institute of Neurology, has shown that genetic mutations which cause a decrease in dopamine production in the brain and lead to a form of childhood-onset Dystonia, also play a role in the development of Parkinson’s disease.
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Leonard Wolfson Experimental Neurology Centre (LWENC)

The new Leonard Wolfson Experimental Neurology Centre (LWENC) has opened for clinical studies and trials

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Audioslide presentation on Claudia Manzoni's paper examining how fibroblasts with LRRK2 mutations react to starvation conditions and the possible deficits that they have in autophagy.

LRRK2 and autophagy in fibroblasts

In this paper Claudia Manzoni studies how fibroblast cells from people with Parkinson’s disease caused by mutations in LRRK2 react to starvation. Although the changes are quite subtle, there are differences between the way that fibroblasts that contain mutant LRRK2 respond to being starved – suggesting that there may be changes in the way that these cells regulate a key process called autophagy (a term which comes from the greek meaning to eat yourself, and is one of the ways that cells get rid of waste and recycle proteins and organellles).
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Alpha-synuclein in LRRK2 brains

9 July 2013

Image of alpha-synuclein

First author Adamantios Mamais tells us about his recent publication in Neurobiology of Disease: At the Queen Square Brain Bank (part of the UCL Institute of Neurology) we hold a large collection of post-mortem human brain tissue from patients with neurodegenerative diseases including Parkinson’s disease (PD); a debilitating neurological disorder that affects the central nervous system. In the United States alone about 50,000 new cases are reported every year. The main symptoms include tremor, slow movement, rigid limbs and a shuffling gait while these worsen with time.

A common pathological characteristic in PD patients is the abnormal accumulation of a protein named α-synuclein that can be seen under the microscope in neurons in the brain. This protein aggregation forms what we call Lewy bodies, named after the prominent neurologist Dr Frederic Lewy that characterised them in 1912. This is also followed by α-synuclein becoming very insoluble in detergents in the lab. In fact protein aggregation is a common pathological phenomenon seen in other neurodegenerative diseases like Alzheimer’s disease and frontotemporal dementia.

Our goal is to understand what causes these changes in α-synuclein. In 5% of PD patients the disease is directly caused by genetic mutations that can be inherited. We hold four post-mortem PD cases from patients that carried the most prevalent mutation of the inherited form of the disease, the LRRK2 mutation G2019S. By studying these brains we found a striking difference in the insolubility properties of α-synuclein compared to brains of PD patients that did not carry mutations.

This is the first time that a difference in α-synuclein properties has been discovered between genetic and not-genetic PD and can give us clues as to the effect of the mutation in abnormal protein aggregation and neurodegeneration. Most importantly this suggests that the real detrimental effect in G2019S PD may not be caused by α-synuclein becoming insoluble while it is being deposited in Lewy bodies.

Mamais, A., Raja, M., Manzoni, C., Dihanich, S., Lees, A., Moore, D., Lewis, P., Bandopadhyay, R., 2013. Divergent a-synuclein solubility and aggregation properties in G2019S LRRK2 Parkinson’s disease brains with Lewy Body pathology compared to idiopathic cases. Neurobiol Dis.

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