Meeting details menu

Meeting Authors
Meeting Abstracts
Keynote lectures
Oral communications
Poster presentations
Special symposia
Other

Acta Physiologica Congress

Back

Acta Physiologica 2007; Volume 189, Supplement 653
The 86th Annual Meeting of The German Physiological Society
3/25/2007-3/28/2007
Hannover, Germany


DYNAMICS OF SINGLE POTASSIUM CHANNEL PROTEINS IN THE PLASMA MEMBRANE OF MIGRATING CELLS
Abstract number: O04-2

Nechyporuk-Zloy1 V, Dieterich1 P, Oberleithner1 H, Stock1 C, Schillers1 H, Schwab1 A

1Institute of Physiology II, University of Mnster, Germany

Cell migration is an important cell physiological process, which is controlled by regulated ion channel activity. It was revealed that potassium channels, in particular calcium-activated potassium channels (KCa 3.1), are required for optimal cell migration. In order to study the dynamics of individual channel proteins in the plasma membrane under physiological conditions we tracked single channel proteins during migration. Previously, we identified single KCa 3.1 channel proteins in the plasma membrane by means of quantum dot (QD) labeling (Nechyporuk- Zloy et al., AJP. 291:C266-9., 2006). In migrating MDCK-F cells the single QD-labeled channels were visualised and tracked using time lapse total internal reflection fluorescence microscopy. The main type of motion was subdiffusion with mean diffusion coefficient 0.0553 ± 0.0072 mm 2/s and subdiffusion exponent 0.88 ± 0.05. We detected no preferred direction for the movement of KCa 3.1 channels in the plasma membrane. Ion channel proteins had lower diffusion coefficients and smaller subdiffusion exponents at the rear part of the lamellipodium and at the uropod than in other parts of the cell. We suggest that subdiffusion is the main dynamical process for the transport of the KCa 3.1 channels in the membrane. The trajectories of individual QDs indicate that a combination of trapping and movement phases may be the origin of the subdiffusive behaviour.

To cite this abstract, please use the following information:
Acta Physiologica 2007; Volume 189, Supplement 653 :O04-2

Our site uses cookies to improve your experience.You can find out more about our use of cookies in our standard cookie policy, including instructions on how to reject and delete cookies if you wish to do so.

By continuing to browse this site you agree to us using cookies as described in our standard cookie policy .

CLOSE