In:
Small, Wiley, Vol. 14, No. 24 ( 2018-06)
Abstract:
The Zn 2+ stored in the secretory vesicles of glutamatergic neurons is coreleased with glutamate upon stimulation, resulting in the elevation of extracellular Zn 2+ concentration ( ). This elevation of regulates the neurotransmission and facilitates the fibrilization of amyloid‐β (Aβ). However, the exact surrounding neurons under (patho)physiological conditions is not clear and the connection between and the Aβ fibrilization remains obscure. Here, a silicon nanowire field‐effect transistor (SiNW‐FET) with the Zn 2+ ‐sensitive fluorophore, FluoZin‐3 (FZ‐3), to quantify the in real time is modified. This FZ‐3/SiNW‐FET device has a dissociation constant of ≈12 × 10 −9 m against Zn 2+ . By placing a coverslip seeded with cultured embryonic cortical neurons atop an FZ‐3/SiNW‐FET, the elevated to ≈110 × 10 −9 m upon stimulation with α‐amino‐3‐hydroxy‐5‐methyl‐4‐isoxazolepropionic acid (AMPA). Blockers against the AMPA receptor or exocytosis greatly suppress this elevation, indicating that the Zn 2+ stored in the synaptic vesicles is the major source responsible for this elevation of . In addition, a SiNW‐FET modified with Aβ could bind Zn 2+ with a dissociation constant of ≈633 × 10 −9 m and respond to the Zn 2+ released from AMPA‐stimulated neurons. Therefore, the can reach a level high enough to bind Aβ and the Zn 2+ homeostasis can be a therapeutic strategy to prevent neurodegeneration.
Type of Medium:
Online Resource
ISSN:
1613-6810
,
1613-6829
DOI:
10.1002/smll.201704439
Language:
English
Publisher:
Wiley
Publication Date:
2018
detail.hit.zdb_id:
2168935-0