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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
18
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pubmed:dateCreated |
2009-5-7
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pubmed:abstractText |
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 beta1-dependent pathway. These findings describe a new target pathway for MMP-9 action in key physiological and pathological brain processes.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD29,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin G,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsins,
http://linkedlifedata.com/resource/pubmed/chemical/Ctsg protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinase 9,
http://linkedlifedata.com/resource/pubmed/chemical/NR1 NMDA receptor,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, N-Methyl-D-Aspartate,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1529-2401
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
6
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pubmed:volume |
29
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6007-12
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:19420267-Analysis of Variance,
pubmed-meshheading:19420267-Animals,
pubmed-meshheading:19420267-Antigens, CD29,
pubmed-meshheading:19420267-Cathepsin G,
pubmed-meshheading:19420267-Cathepsins,
pubmed-meshheading:19420267-Cells, Cultured,
pubmed-meshheading:19420267-Embryo, Mammalian,
pubmed-meshheading:19420267-Enzyme Inhibitors,
pubmed-meshheading:19420267-Hippocampus,
pubmed-meshheading:19420267-Matrix Metalloproteinase 9,
pubmed-meshheading:19420267-Microscopy, Confocal,
pubmed-meshheading:19420267-Mutation,
pubmed-meshheading:19420267-Neurons,
pubmed-meshheading:19420267-Protein Transport,
pubmed-meshheading:19420267-Rats,
pubmed-meshheading:19420267-Rats, Sprague-Dawley,
pubmed-meshheading:19420267-Receptors, N-Methyl-D-Aspartate,
pubmed-meshheading:19420267-Serine Endopeptidases,
pubmed-meshheading:19420267-Signal Transduction,
pubmed-meshheading:19420267-Statistics, Nonparametric
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pubmed:year |
2009
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pubmed:articleTitle |
Matrix metalloproteinase-9 controls NMDA receptor surface diffusion through integrin beta1 signaling.
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pubmed:affiliation |
The Nencki Institute, 02-093 Warsaw, Poland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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