Functional trkB neurotrophin receptors are intrinsic components of the adult brain postsynaptic density

Neurotrophins have long been thought to act as target-derived factors that regulate the survival and differentiation of afferent neurons. Recently, brain-derived neurotrophic factor (BDNF) was shown to elicit rapid increases in synaptic activity of cultured hippocampal neurons by enhancing responsiv...

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Published in:Brain research. Molecular brain research. 1996-12, Vol.43 (1), p.286-290
Main Authors: Wu, Kuo, Xu, Jia-ling, Suen, Piin-chau, Levine, Eric, Huang, Yung-yu, Mount, Howard T.J, Lin, Siang-yo, Black, Ira B
Format: Article
Language:English
Subjects:
Animals
Biological and medical sciences
Brain - metabolism
Brain-derived neurotrophic factor
Brain-Derived Neurotrophic Factor - metabolism
Central nervous system
Central neurotransmission. Neuromudulation. Pathways and receptors
Fundamental and applied biological sciences. Psychology
Neurotrophin
Postsynaptic
Presynaptic Terminals - metabolism
Rats
Rats, Sprague-Dawley
Receptor protein tyrosine kinase
Receptor, trkA - metabolism
Receptor, trkB - metabolism
Synaptic plasticity
trkB
Vertebrates: nervous system and sense organs
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Summary:Neurotrophins have long been thought to act as target-derived factors that regulate the survival and differentiation of afferent neurons. Recently, brain-derived neurotrophic factor (BDNF) was shown to elicit rapid increases in synaptic activity of cultured hippocampal neurons by enhancing responsiveness to excitatory input. These findings suggest a postsynaptic localization of neurotrophin receptors. In this study, we examined the expression of trkB, a high-affinity receptor for BDNF, in the postsynaptic density (PSD), a proteinaceous specialization of the postsynaptic membrane. Western blot analyses with antibodies to trkB revealed localization to the PSD in adult rat cerebral cortex and hippocampus. Only the full-length, active form of trkB was detected in PSD samples. BDNF treatment of the adult cortical PSD resulted in a 5-fold increase in trkB autophosphorylation, supporting the contention that the PSD contains functional trkB. Truncated trkB, which does not contain the tyrosine kinase signaling domain, though present in membrane fractions, was undetectable in the PSD. The presence of trkB in the PSD is consistent with a role for neurotrophins in the regulation of synaptic activity via direct postsynaptic mechanisms.
ISSN:0169-328X
1872-6941
DOI:10.1016/S0169-328X(96)00211-2