Person, Project, Place
Break-through research needs talented enthusiastic scientists, matched to well designed projects, in a supportive place. The Spillantini lab has a long history of attracting postdoctoral researchers and PhD students from around the world. Many have gone on to start their own lab and purse independent research careers. Others have moved into industry or successful consulting roles. You can find the profiles of current members below.
Want to join?
Do you think you have a novel research idea? Do you have the drive to win funding? Do you want to perform world-class research at the University of Cambridge? Then please contact us to book an appointment. Call +44 (0)1223 331160 or email mgs11@cam.ac.uk.
Postdoctoral Research Associates
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Dr Jack Harry Brelstaff (jb961@cam.ac.uk)
Image: A slice through a brain showing all the aggregated tau causing degeneration in green. pFTAA labelled P301S human tau aggregates |
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Dr Laura Calo (lc232@cam.ac.uk)
Image: Neurons derived from a skin biopsy of a PD case showing alpha synuclein aggregation in green (puncta) |
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Dr Ellen Tedford (et447@cam.ac.uk) I am interested in the role extracellular vesicles play in neurodegenerative diseases. Extracellular vesicles are shed by almost every cell type, including neurons and glia, they contain RNA, DNA and protein. This is an important part of neurophysiological communication but during neurodegenerative diseases this process is altered. To investigate the mechanisms governing this dysfunction I use human iPS cells and animal models. During my PhD, I investigated the role extracellular vesicles play in epigenetic regulation of neurons.
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Dr Sanne Kaalund
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Dr Aishwarya G. Nadadhur (agn24@cam.ac.uk)
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Dr Katrina Räty (Albert) (ka524@cam.ac.uk)
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Dr Aviva Tolkovsky (amt1004@cam.ac.uk)
Nerve cells are complicated highly branched cells that are essential for our brains and our bodies. Without nerve cells we cannot think, feel, walk, pump blood or digest our food. The protein tau is a nerve cell protein that enables neurons to distribute essential proteins to distant parts of the cell in the brain, spinal cord, and in neurons that mediate sensation and control the actions of our internal organs. In Alzheimer's disease, tau ceases to function normally; it becomes misfolded and eventually forms neurofibrillary tangles (NFT) that are thought to be critical for neurodegeneration in the disease.Quite a lot is known about pathological changes that occur in tau, but one fundamental problem is still unanswered: what form of tau is truly pathological and how tau causes the nerve cells to die? These problems are difficult to solve by looking at the nervous system in post-mortem human brains because it is difficult to catch a dying nerve cell as dead nerve cells are rapidly cleared by neighbouring cells. For this reason, mouse models of tauopathy have been created where several features of the disease are replicated. However, even in mice, the dying cells in the brain are not easily accessible. To reduce animal use and still be able to investigate how tau kills cells, we have turned to a cell culture system of nerve cells from the sensory nervous system. We now know that cell death is not necessarily a random process. It can involve the orderly demolition of the cell. We develop models to determine the pathways by which tau causes nerve cell pathology and death. We also wish to explore whether we can keep the sick nerve cells alive using drugs that are being developed for eventual use in humans.
Image: Brain sections from two transgenic littermates expressing mutated tau protein stained with Cresyl Violet. Left panel shows healthy neurons in a mouse before disease onset, right hand panel shows swollen balloon neurons close to death from a symptomatic mouse |
PhD Students
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Janine Brandes (jb2274@cam.ac.uk)
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Joana Domingues (jmpd3@cam.ac.uk)
Parkinson's disease is usually thought of as a movement disorder of the brain. As the disease progesses, we can observe the protein alpha-synuclein aggregating and these aggregates spreading through the brian. However, we do not know why the aggregation begins or the source of the initial aggregated alpha-synuclein.
The aim of my PhD project is to characterise a new transgenic mouse model that expresses the protein alpha-synuclein specifically in the gut. This will help us test the emerging hypothesis that alpha-synuclein aggregates can spread from the gut to the brain, via the nerves that control the gut. If this hypothesis is correct, we will be able to test treatments that could stop alpha-synuclein aggregates spreading to the brain, leading to the development of Parkinson's disease.
Image: Cross-section of mouse's small intestine showing neuronal cells (green) and Glial cells (red) |
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Matthew Mason (mm2458@cam.ac.uk)
Ageing is one of the greatest risk factors for idiopathic neurodegenerative disease. Indeed, in recent years, it has been demonstrated that there is a significant degree of overlap between the cellular changes that occur in natural ageing and those that occur in neurodegenerative disease. The objective of my PhD project is to investigate this overlap, with a specific focus on the activity of glia in these contexts. To this end, I am generating cortical organoids and iPSC-derived microglia, to explore in vitro how disease-relevant stimuli and ageing-relevant stimuli might dovetail to perturb the function of microglia.
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Research Assistant
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Helen Henson (hh495@cam.ac.uk)
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