Journal article
Katarína Ondáčová, M. Karmažínová, J. Lazniewska, N. Weiss, Ľ. Lacinová
Channels, 2016
Channels, 2016
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Ondáčová, K., Karmažínová, M., Lazniewska, J., Weiss, N., & Lacinová, Ľ. (2016). Modulation of Cav3.2 T-type calcium channel permeability by asparagine-linked glycosylation. Channels.
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Ondáčová, Katarína, M. Karmažínová, J. Lazniewska, N. Weiss, and Ľ. Lacinová. “Modulation of Cav3.2 T-Type Calcium Channel Permeability by Asparagine-Linked Glycosylation.” Channels (2016).
MLA
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Ondáčová, Katarína, et al. “Modulation of Cav3.2 T-Type Calcium Channel Permeability by Asparagine-Linked Glycosylation.” Channels, 2016.
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@article{katar2016a,
title = {Modulation of Cav3.2 T-type calcium channel permeability by asparagine-linked glycosylation},
year = {2016},
journal = {Channels},
author = {Ondáčová, Katarína and Karmažínová, M. and Lazniewska, J. and Weiss, N. and Lacinová, Ľ.}
}
Abstract
abstract Low-voltage-gated T-type calcium channels are expressed throughout the nervous system where they play an essential role in shaping neuronal excitability. Defects in T-type channel expression have been linked to various neuronal disorders including neuropathic pain and epilepsy. Currently, little is known about the cellular mechanisms controlling the expression and function of T-type channels. Asparagine-linked glycosylation has recently emerged as an essential signaling pathway by which the cellular environment can control expression of T-type channels. However, the role of N-glycans in the conducting function of T-type channels remains elusive. In the present study, we used human Cav3.2 glycosylation-deficient channels to assess the role of N-glycosylation on the gating of the channel. Patch-clamp recordings of gating currents revealed that N-glycans attached to hCav3.2 channels have a minimal effect on the functioning of the channel voltage-sensor. In contrast, N-glycosylation on specific asparagine residues may have an essential role in the conducting function of the channel by enhancing the channel permeability and / or the pore opening of the channel. Our data suggest that modulation of N-linked glycosylation of hCav3.2 channels may play an important physiological role, and could also support the alteration of T-type currents observed in disease states.
