Abstract
Recently, we identified an outer hair cell (OHC) lateral membrane conductance, G metL, that colocalizes with prestin and passes Cl−, thereby influencing prestin’s (SLC26A5) electromechanical activity. In this study, we report on a comparison of the temperature and tension dependence of G metL and prestin. Though we find significant temperature and tension dependence of each, substantial differences exist which indicate their independent identity. The following data support this conclusion: (1) The voltage dependence of G metL does not follow that of prestin’s nonlinear capacitance (NLC) function when the latter is shifted by either temperature or membrane tension; (2) Unlike native OHCs whose NLC can be modulated by influx of extracellular Cl−, prestin-transfected Chinese hamster ovary (CHO) cells do not show this phenomenon; (3) Stretch-sensitive, single channel currents are not evidenced after prestin transfection in CHO cells; and (4) There is no correlation between prestin expression level (gauged via NLC) and transmembrane current through G metL. Thus, G metL must result from the activity of another molecular species within the lateral membrane of the OHC. A clue to its identity is the conductance’s nonlinear temperature dependence in contrast to prestin and other OHC conductances’ linear dependence. Whereas K+ conductances in OHCs present a uniform Q 10 close to 1.2, G metL shows a bimodal Q 10, with a Q 10 of 1.5 below 34°C and a Q 10 of greater than 4 and above. The dissociation of SLC26A5 (prestin) and G metL theoretically provides for a modifiable anionic feedback to prestin via the degree of spatial separation between these interacting partners within the OHC lateral membrane.
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Acknowledgements
This research was supported by NIH NIDCD grant DC000273 to JSS and grant K08 DC05352 to DN. We also thank Margaret Mazzucco for the technical help.
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Santos-Sacchi, J., Rybalchenko, V., Bai, JP. et al. On the temperature and tension dependence of the outer hair cell lateral membrane conductance G metL and its relation to prestin. Pflugers Arch - Eur J Physiol 452, 283–289 (2006). https://doi.org/10.1007/s00424-005-0037-2
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DOI: https://doi.org/10.1007/s00424-005-0037-2