Extracellular proteolysis in structural and functional plasticity of mossy fiber synapses in hippocampus

Brain is continuously altered in response to experience and environmental changes. One of the underlying mechanisms is synaptic plasticity, which is manifested by modification of synapse structure and function. It is becoming clear that regulated extracellular proteolysis plays a pivotal role in the...

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Main Authors: Grzegorz eWiera, Jerzy W Mozrzymas
Format: Article
Language:English
Published: Frontiers Media S.A. 2015-11-01
Series:Frontiers in Cellular Neuroscience
Subjects:
Online Access:http://journal.frontiersin.org/Journal/10.3389/fncel.2015.00427/full
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author Grzegorz eWiera
Grzegorz eWiera
Jerzy W Mozrzymas
Jerzy W Mozrzymas
author_facet Grzegorz eWiera
Grzegorz eWiera
Jerzy W Mozrzymas
Jerzy W Mozrzymas
author_sort Grzegorz eWiera
collection DOAJ
description Brain is continuously altered in response to experience and environmental changes. One of the underlying mechanisms is synaptic plasticity, which is manifested by modification of synapse structure and function. It is becoming clear that regulated extracellular proteolysis plays a pivotal role in the structural and functional remodeling of synapses during brain development, learning and memory formation. Clearly, plasticity mechanisms may substantially differ between projections. Mossy fiber synapses onto CA3 pyramidal cells display several unique functional features, including pronounced short-term facilitation, a presynaptically expressed LTP that is independent of NMDAR activation, and NMDA-dependent metaplasticity. Moreover, structural plasticity at mossy fiber synapses ranges from the reorganization of projection topology after hippocampus-dependent learning, through intrinsically different dynamic properties of synaptic boutons to pre- and postsynaptic structural changes accompanying LTP induction. Although concomitant functional and structural plasticity in this pathway strongly suggests a role of extracellular proteolysis, its impact only starts to be investigated in this projection. In the present report, we review the role of extracellular proteolysis in various aspects of synaptic plasticity in hippocampal mossy fiber synapses. A growing body of evidence demonstrates that among perisynaptic proteases, tPA/plasmin system, β-site amyloid precursor protein-cleaving enzyme 1 (BACE1) and metalloproteinases play a crucial role in shaping plastic changes in this projection. We discuss recent advances and emerging hypotheses on the roles of proteases in mechanisms underlying mossy fiber target specific synaptic plasticity and memory formation.
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spelling doaj.art-09fae50c9e4b4e06a7d02848edff45942022-12-21T19:44:07ZengFrontiers Media S.A.Frontiers in Cellular Neuroscience1662-51022015-11-01910.3389/fncel.2015.00427152926Extracellular proteolysis in structural and functional plasticity of mossy fiber synapses in hippocampusGrzegorz eWiera0Grzegorz eWiera1Jerzy W Mozrzymas2Jerzy W Mozrzymas3University of WroclawWroclaw Modecal universityUniversity of WroclawWroclaw Modecal universityBrain is continuously altered in response to experience and environmental changes. One of the underlying mechanisms is synaptic plasticity, which is manifested by modification of synapse structure and function. It is becoming clear that regulated extracellular proteolysis plays a pivotal role in the structural and functional remodeling of synapses during brain development, learning and memory formation. Clearly, plasticity mechanisms may substantially differ between projections. Mossy fiber synapses onto CA3 pyramidal cells display several unique functional features, including pronounced short-term facilitation, a presynaptically expressed LTP that is independent of NMDAR activation, and NMDA-dependent metaplasticity. Moreover, structural plasticity at mossy fiber synapses ranges from the reorganization of projection topology after hippocampus-dependent learning, through intrinsically different dynamic properties of synaptic boutons to pre- and postsynaptic structural changes accompanying LTP induction. Although concomitant functional and structural plasticity in this pathway strongly suggests a role of extracellular proteolysis, its impact only starts to be investigated in this projection. In the present report, we review the role of extracellular proteolysis in various aspects of synaptic plasticity in hippocampal mossy fiber synapses. A growing body of evidence demonstrates that among perisynaptic proteases, tPA/plasmin system, β-site amyloid precursor protein-cleaving enzyme 1 (BACE1) and metalloproteinases play a crucial role in shaping plastic changes in this projection. We discuss recent advances and emerging hypotheses on the roles of proteases in mechanisms underlying mossy fiber target specific synaptic plasticity and memory formation.http://journal.frontiersin.org/Journal/10.3389/fncel.2015.00427/fullADAM ProteinsIntegrinsProteolysisfeedforward inhibitionTPAMMP
spellingShingle Grzegorz eWiera
Grzegorz eWiera
Jerzy W Mozrzymas
Jerzy W Mozrzymas
Extracellular proteolysis in structural and functional plasticity of mossy fiber synapses in hippocampus
Frontiers in Cellular Neuroscience
ADAM Proteins
Integrins
Proteolysis
feedforward inhibition
TPA
MMP
title Extracellular proteolysis in structural and functional plasticity of mossy fiber synapses in hippocampus
title_full Extracellular proteolysis in structural and functional plasticity of mossy fiber synapses in hippocampus
title_fullStr Extracellular proteolysis in structural and functional plasticity of mossy fiber synapses in hippocampus
title_full_unstemmed Extracellular proteolysis in structural and functional plasticity of mossy fiber synapses in hippocampus
title_short Extracellular proteolysis in structural and functional plasticity of mossy fiber synapses in hippocampus
title_sort extracellular proteolysis in structural and functional plasticity of mossy fiber synapses in hippocampus
topic ADAM Proteins
Integrins
Proteolysis
feedforward inhibition
TPA
MMP
url http://journal.frontiersin.org/Journal/10.3389/fncel.2015.00427/full
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