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Volume 9 Journal of Neurology and Neuroscience
ISSN: 2171-6625
Page 29
July 23-24, 2018 Birmingham, UK
&
JOINT EVENT
24th International Conference on Neuroscience and Neurochemistry
26th Edition of International Conference on Clinical Psychology and Neuroscience
Mourad Tayebi
Western Sydney University, Australia
Mourad Tayebi, J Neurol Neurosci 2018, Volume 9
DOI: 10.21767/2171-6625-C2-010
Proteinopathies: A tale of human, dogs and kangaroos
Proteinopathies such as Alzheimer’s disease (AD) and Parkinson’s disease (PD) are a group of disorders thought to be
caused by abnormal folding or misfolding of beta amyloid (Ab) and alpha-synuclein respectively. Their pathogenesis is not
well understood due to unresolved molecular mechanisms. This is further complicated by the lack of proper natural disease
models that might be effective in aiding in the investigation of the molecular mechanisms underlying these disorders. Dogs
spontaneously deposit human-type Ab as they age and thus are a natural higher mammalian model of aging. The canine Aβ
precursor protein (APP) is virtually identical to human APP. Previous studies demonstrated that aging dogs spontaneously
accumulate human-type Aβ and parallel declines in cognition. Further, the outcomes of immunotherapy studies in aged dogs
has predicted human clinical trial outcomes; clearance of Aβ plaques with little cognitive benefits. Inmore recent work, we show
that canine-derived Aβ was toxic to human neuronal cell lines and led to aggregation of human Aβ. Eastern Grey Kangaroos
(EGK) display a typical movement disorder presentation associated with grass phalaris poisoning. We show that this disorder,
known as Phalaris Staggers displays a Parkinsonian type syndrome with associated Parkinson’s-like signs and neuropathology,
including synucleiopathy and neuromyelopathy. Studies of proteinopathies have typically used transgenic mouse models, and
subsequently translated to human clinical trials. However, the success rate of these translational studies have been limited
and unfortunately resulted in negative outcomes and some with adverse events. It is critical to identify and validate natural
higher mammalian models of proteinopathies to investigate the molecular mechanisms underlying these disorders and test
therapeutic outcomes prior to translation to human clinical trials.
Biography
Mourad Tayebi is an Associate Professor in Biomedical Sciences in the School of Medicine at Western Sydney University, Australia. He is an international expert in the field of protein
misfolding diseases, with specific focus on investigating the molecular mechanisms underlying pathogenic protein misfolding and characterizing the misfolding associated with these
disorders. His team is very active in the development of early blood diagnostic test screen for Alzheimer and effective therapies for neurodegenerative diseases.