Glycosylation affects rat Kv1.1 potassium channel gating by a combined surface potential and cooperative subunit interaction mechanism.

@article{Watanabe2003GlycosylationAR,
  title={Glycosylation affects rat Kv1.1 potassium channel gating by a combined surface potential and cooperative subunit interaction mechanism.},
  author={Itaru Watanabe and Hong-gang Wang and Jhon Jairo Sutachan and Jing Zhu and Esperanza Recio-Pinto and William B. Thornhill},
  journal={The Journal of physiology},
  year={2003},
  volume={550 Pt 1},
  pages={
          51-66
        }
}
The effect of glycosylation on Kv1.l potassium channel function was investigated in mammalian cells stably transfected with Kv1.l or Kv1.1N207Q. Macroscopic current analysis showed that both channels were expressed but Kv1.1N207Q, which was not glycosylated, displayed functional differences compared with wild-type, including slowed activation kinetics, a positively shifted V 1/2, a shallower slope for the conductance versus voltage relationship, slowed C-type inactivation kinetics, and a… CONTINUE READING
BETA

Topics from this paper.

Citations

Publications citing this paper.
SHOWING 1-10 OF 36 CITATIONS

Similar Papers

Loading similar papers…