Astrocyte contributions to clearing tau aggregates in Alzheimer's disease and other tauopathies Professor Wendy Noble (University of Exeter) presents her work on understanding the molecular mechanisms underlying neurodegenerative diseases. Hosted by Dr Ines Hahn.
Event details
Abstract
Distinct forms of modified tau deposit in a cell- and region-specific manner to mediate synapse damage and neuron loss in a family of neurodegenerative disorders named tauopathies, of which Alzheimer's disease is the best known. Reactive astrocytes, displaying altered functions, are also a prominent feature of tauopathy brain. This large and heterogeneous population of cells are increasingly recognised as contributing to early phases of disease. However, the contribution of astrocytes to the emergence and/or resolution of tau pathology is not well understood. Our data show that interactions between astrocytes and neurons are important for the development and/or clearance of tau aggregates. Importantly, this includes roles in the non-cell autonomous clearance of tau aggregates. These functions of astrocytes might provide novel routes for therapeutic intervention.
About the speaker
Professor Wendy Noble
Wendy is Professor of Molecular Neurobiology at the University of Exeter. Her work is focussed on understanding the molecular mechanisms underlying neurodegenerative diseases, with a particular interest in tau.
Wendy leads a research programme to elucidate the molecular mechanisms underlying the development of Alzheimer’s disease (AD) and other tauopathies. These neurodegenerative diseases, for which there are no effective treatments, are characterised by deposits of abnormal tau that spread across the brain as disease progresses. We use rodent and human (iPS and iNP)-cells, transgenic rodent models of disease and post-mortem human brain.
Current projects address:
- How and why tau becomes altered.
- How protein modifications affect tau function and cause toxicity.
- How glial cells influence tau biology.
- Novel strategies to prevent tau-associated damage and to treat other neurodegenerative diseases.