Journal Article

DZNE-2020-03632

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Neuronal activity regulates extracellular tau in vivo.

Yamada, K. ; Holth, J. K. ; Liao, F. ; Stewart, F. R. ; Mahan, T. E. ; Jiang, H. ; Cirrito, J. R. ; Patel, T. K. ; Hochgräfe, K.DZNE* ; Mandelkow, E.-M.DZNE* ; Holtzman, D. M. (Corresponding author)

2014
Rockefeller Univ. Press New York, NY

This record in other databases:    

Please use a persistent id in citations: doi:10.1084/jem.20131685

Abstract: Tau is primarily a cytoplasmic protein that stabilizes microtubules. However, it is also found in the extracellular space of the brain at appreciable concentrations. Although its presence there may be relevant to the intercellular spread of tau pathology, the cellular mechanisms regulating tau release into the extracellular space are not well understood. To test this in the context of neuronal networks in vivo, we used in vivo microdialysis. Increasing neuronal activity rapidly increased the steady-state levels of extracellular tau in vivo. Importantly, presynaptic glutamate release is sufficient to drive tau release. Although tau release occurred within hours in response to neuronal activity, the elimination rate of tau from the extracellular compartment and the brain is slow (half-life of ∼11 d). The in vivo results provide one mechanism underlying neuronal tau release and may link trans-synaptic spread of tau pathology with synaptic activity itself.

Keyword(s): Analysis of Variance (MeSH) ; Animals (MeSH) ; Brain: metabolism (MeSH) ; Electroencephalography (MeSH) ; Enzyme-Linked Immunosorbent Assay (MeSH) ; Extracellular Space: metabolism (MeSH) ; Female (MeSH) ; Glutamic Acid: metabolism (MeSH) ; Half-Life (MeSH) ; Kinetics (MeSH) ; Luciferases (MeSH) ; Male (MeSH) ; Mice (MeSH) ; Mice, Transgenic (MeSH) ; Microdialysis (MeSH) ; Neurons: metabolism (MeSH) ; Synaptic Transmission: physiology (MeSH) ; Tauopathies: physiopathology (MeSH) ; Tetrodotoxin (MeSH) ; tau Proteins: metabolism (MeSH) ; tau Proteins ; Glutamic Acid ; Tetrodotoxin ; Luciferases

---

Contributing Institute(s):

1. Structural Principles of Neurodegeneration (AG Mandelkow 1)
2. Cell and Animal Models of Neurodegeneration (AG Mandelkow 2)

Research Program(s):

1. 342 - Disease Mechanisms and Model Systems (POF3-342) (POF3-342)

Appears in the scientific report 2014

---

Database coverage:
; BIOSIS Previews ; Clarivate Analytics Master Journal List ; Current Contents - Life Sciences ; IF >= 10 ; JCR ; NCBI Molecular Biology Database ; PubMed Central ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Web of Science Core Collection

---