Format

Send to

Choose Destination
Front Neuroanat. 2014 Oct 20;8:116. doi: 10.3389/fnana.2014.00116. eCollection 2014.

Extracellular matrix control of dendritic spine and synapse structure and plasticity in adulthood.

Author information

1
Interdepartmental Neuroscience Program, Yale University New Haven, CT, USA ; Department of Molecular Biophysics and Biochemistry, Yale University New Haven, CT, USA.
2
Interdepartmental Neuroscience Program, Yale University New Haven, CT, USA ; Department of Molecular Biophysics and Biochemistry, Yale University New Haven, CT, USA ; Department of Neurobiology, Yale University New Haven, CT, USA.

Abstract

Dendritic spines are the receptive contacts at most excitatory synapses in the central nervous system. Spines are dynamic in the developing brain, changing shape as they mature as well as appearing and disappearing as they make and break connections. Spines become much more stable in adulthood, and spine structure must be actively maintained to support established circuit function. At the same time, adult spines must retain some plasticity so their structure can be modified by activity and experience. As such, the regulation of spine stability and remodeling in the adult animal is critical for normal function, and disruption of these processes is associated with a variety of late onset diseases including schizophrenia and Alzheimer's disease. The extracellular matrix (ECM), composed of a meshwork of proteins and proteoglycans, is a critical regulator of spine and synapse stability and plasticity. While the role of ECM receptors in spine regulation has been extensively studied, considerably less research has focused directly on the role of specific ECM ligands. Here, we review the evidence for a role of several brain ECM ligands and remodeling proteases in the regulation of dendritic spine and synapse formation, plasticity, and stability in adults.

KEYWORDS:

RGD peptide; agrin; chondroitin sulfate proteoglycans; dendritic spine; extracellular matrix; extracellular proteases; integrins; reelin

Supplemental Content

Full text links

Icon for Frontiers Media SA Icon for PubMed Central
Loading ...
Support Center