Effects of vitamin C on function of different subtypes of glycine receptors
10.3969/j.issn.1001-1978.2021.02.008
- Author:
Yan XU
1
;
Gui-Chang ZOU
1
;
Xin ZUO
1
;
Wei XIONG
1
Author Information
1. School of Life Science and Medicine, University of Science and Technology of China
- Publication Type:Journal Article
- Keywords:
glycine receptor;
ion channel;
patch clamp;
sodium-dependent vitamin C transporter- type 2;
vitamin C
- From:
Chinese Pharmacological Bulletin
2021;37(2):187-191
- CountryChina
- Language:Chinese
-
Abstract:
Aim To investigate the effects of vitamin C (VC) on glycine receptor (GlyR) subtypes. Methods The HEK-293T cells were transfected with plasmids expressing different subtypes of GlyR. Then the cells were incubated with different concentrations of VC. The EC2 concentration of glycine-activated currents were recorded by patch clamp before or after incubation of VC. The effects of the sodium-dependent vitamin C transporter-type 2 ( SVCT2 ) inhibitor sulfinpyrazone on VC induced potentiation of GlyRs were also examined. The method of amino acid point mutation was used to explore the critical site for interaction between VC and GlyR. Results Ascorbic acid dose-dependently increased the currents mediated by GlyRal and GlyRa3, with a3 subunits being the most sensitive to VC. Ascorbic acid had no significant effect on the current mediated by the al subunit of GlyRs. Cell incubation with sulfinpyrazone did not affect the VC induced potentiation of GlyR function. The mutation of Ser296 at the third transmembrane domain of a3 GlyR significantly reduced the potentiation of VC on GlyR func-tion. Conclusions Ascorbic acid can enhance the function of GlyR al and a3 subunits, but not a2 sub- unit. Such enhancement is not likely to be an effect oc- curing inside cells. The Ser296 of GlyR plays a key role in the VC induced enhancement of GlyR function.
