RGD Reference Report - In vivo roles for matrix metalloproteinase-9 in mature hippocampal synaptic physiology and plasticity. - Rat Genome Database

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In vivo roles for matrix metalloproteinase-9 in mature hippocampal synaptic physiology and plasticity.

Authors: Bozdagi, O  Nagy, V  Kwei, KT  Huntley, GW 
Citation: Bozdagi O, etal., J Neurophysiol. 2007 Jul;98(1):334-44. Epub 2007 May 9.
RGD ID: 1642034
Pubmed: PMID:17493927   (View Abstract at PubMed)
PMCID: PMC4415272   (View Article at PubMed Central)
DOI: DOI:10.1152/jn.00202.2007   (Journal Full-text)

Extracellular proteolysis is an important regulatory nexus for coordinating synaptic functional and structural plasticity, but the identity of such proteases is incompletely understood. Matrix metalloproteinases (MMPs) have well-known, mostly deleterious roles in remodeling after injury or stroke, but their role in nonpathological synaptic plasticity and function in intact adult brains has not been extensively investigated. Here we address the role of MMP-9 in hippocampal synaptic plasticity using both gain- and loss-of-function approaches in urethane-anesthetized adult rats. Acute blockade of MMP-9 proteolytic activity with inhibitors or neutralizing antibodies impairs maintenance, but not induction, of long-term potentiation (LTP) at synapses formed between Schaffer-collaterals and area CA1 dendrites. LTP is associated with significant increases in levels of MMP-9 and proteolytic activity within the potentiated neuropil. By introducing a novel application of gelatin-substrate zymography in vivo, we find that LTP is associated with significantly elevated numbers of gelatinolytic puncta in the potentiated neuropil that codistribute with immunolabeling for MMP-9 and for markers of synapses and dendrites. Such increases in proteolytic activity require NMDA receptor activation. Exposing intact area CA1 neurons to recombinant-active MMP-9 induces a slow synaptic potentiation that mutually occludes, and is occluded by, tetanically evoked potentiation. Taken together, our data reveal novel roles for MMP-mediated proteolysis in regulating nonpathological synaptic function and plasticity in mature hippocampus.

Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
positive regulation of synaptic plasticity  IMP 1642034 RGD 

Objects Annotated

Genes (Rattus norvegicus)
Mmp9  (matrix metallopeptidase 9)


Additional Information