Journal
JOURNAL OF NEUROSCIENCE
Volume 29, Issue 18, Pages 6007-6012Publisher
SOC NEUROSCIENCE
DOI: 10.1523/JNEUROSCI.5346-08.2009
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Funding
- Polish Ministry of Science and Higher Education Research [2 P04A 009 30]
- European Union
- Foundation for Polish Science
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Matrix metalloproteinase-9 (MMP-9) has emerged as a physiological regulator of NMDA receptor (NMDAR)-dependent synaptic plasticity and memory. The pathways by which MMP-9 affects NMDAR signaling remain, however, elusive. Using single quantum dot tracking, we demonstrate that MMP-9 enzymatic activity increases NR1-NMDAR surface trafficking but has no influence on AMPA receptor mobility. The mechanism of MMP-9 action on NMDAR is not mediated by change in overall extracellular matrix structure nor by direct cleavage of NMDAR subunits, but rather through an integrin beta 1-dependent pathway. These findings describe a new target pathway for MMP-9 action in key physiological and pathological brain processes.
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