Abstract
The perineuronal net (PNN) is a mesh-like proteoglycan structure on the neuronal surface which is involved in regulating plasticity. The PNN regulates plasticity via multiple pathways, one of which is direct regulation of synapses through the control of AMPA receptor mobility. Since neuronal pentraxin 2 (Nptx2) is a known regulator of AMPA receptor mobility and Nptx2 can be removed from the neuronal surface by PNN removal, we investigated whether Nptx2 has a function in the PNN. We found that Nptx2 binds to the glycosaminoglycans hyaluronan and chondroitin sulphate E in the PNN. Furthermore, in primary cortical neuron cultures, the addition of NPTX2 to the culture medium enhances PNN formation during PNN development. These findings suggest Nptx2 as a novel PNN binding protein with a role in the mechanism of PNN formation.
Highlights
The perineuronal net (PNN) is a mesh-like extracellular matrix (ECM) structure formed on the surface of neurons to regulate plasticity
The PNN consists of a hyaluronan (HA) backbone [6, 7], to which are bound a variety of chondroitin sulphate proteoglycans (CSPGs), such as aggrecan, versican, brevican, and neurocan [8]
The CSPGs are bound stably to HA by hyaluronan and proteoglycan link proteins (HAPLNs) [8, 11, 12], and the structure is further stabilised by tenascin R binding to the C-termini of the CSPGs [13, 14]
Summary
The perineuronal net (PNN) is a mesh-like extracellular matrix (ECM) structure formed on the surface of neurons to regulate plasticity. It appears at the closure of critical periods [1,2,3,4]. The PNN consists of a hyaluronan (HA) backbone [6, 7], to which are bound a variety of chondroitin sulphate proteoglycans (CSPGs), such as aggrecan, versican, brevican, and neurocan [8]. Several enzymes are known to break down the PNN Both chondroitinase ABC (chABC) [4, 15] and hyaluronidase [16, 17] remove the PNN from the surface of the neurons and induce a renewed capacity for plasticity. When the PNN is removed in the visual cortex, ocular dominance plasticity can be reopened [4]
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