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Title: Up-regulation of matrix metallopeptidase 12 in motor neurons undergoing synaptic stripping
Authors: Sajjan, S
Holsinger, RMD
Fok, S
Ebrahimkhani, S
Rollo, JL
Banati, RB
Graeber, MB
Keywords: Extracellular space
Matrix isolation
Enzyme inhibitors
Nerve cells
Somatic cells
Issue Date: 22-Aug-2014
Publisher: Elsevier B.V.
Citation: Sajjan, S., Holsinger, R. D., Fok, S., Ebrahimkhani, S., Rollo, J. L., Banati, R. B., & Graeber, M. B. (2014). Up-regulation of matrix metallopeptidase 12 in motor neurons undergoing synaptic stripping. Neuroscience, 274, 331-340. doi:10.1016/j.neuroscience.2014.05.052
Abstract: Axotomy of the rodent facial nerve represents a well-established model of synaptic plasticity. Post-traumatic “synaptic stripping” was originally discovered in this system. We report upregulation of matrix metalloproteinase MMP12 in regenerating motor neurons of the mouse and rat facial nucleus. Matrix metalloproteinases (matrix metallopeptidases, MMPs) are zinc-binding proteases capable of degrading components of the extracellular matrix and of regulating extracellular signaling networks including within synapses. MMP12 protein expression in facial motor neurons was enhanced following axotomy and peaked at day 3 after the operation. The peak of neuronal MMP12 expression preceded the peak of experimentally induced synaptic plasticity. At the same time, MMP12 redistributed intracellularly and became predominantly localized beneath the neuronal somatic cytoplasmic membrane. Both findings point to a role of MMP12 in the neuronal initiation of the synaptic stripping process. MMP12 is the first candidate molecule for such a trigger function and has potential as a therapeutic target. Moreover, since statins have been shown to increase the expression of MMP12, interference with synaptic stability may represent one mechanism by which these widely used drugs exert their side effects on higher CNS functions. © 2014 by Elsevier Ltd.
Gov't Doc #: 8875
ISSN: 0306-4522
Appears in Collections:Journal Articles

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