Dual functional characteristic of human aquaporin 10 for solute transport

Abstract

Background/Aims: Although aquaglyceroporins have been generally believed to operate in a channel mode, which is of nonsaturable nature, for glycerol as well as for water, we recently found that human aquaporin 9 (hAQP9) operates in a carrier-mediated mode, which is of saturable nature, for glycerol. Based on the finding, we assumed that such a characteristic might be shared by the other aquaglyceroporins and examined the functional characteristics of hAQP10, which is an intestine-specific aquaglyceroporin. Methods: Transport assays were conducted using Xenopus laevis oocytes expressing hAQP10 derived from the microinjected cRNA. Results: The transport of glycerol by hAQP10 was found to be highly saturable with a Michaelis constant of 10.4 μM and specifically inhibited by several glycerol analogs such as monoacetin. Furthermore, when glycerol was preloaded in hAQP10-expressing oocytes, its efflux was trans-stimulated by extracellular glycerol. These results indicate the involvement of a carrier-mediated mechanism in glycerol transport by hAQP10. Interestingly, a channel mechanism was also found to be involved in part in hAQP10-mediated glycerol transport. Conclusion: The present study unveiled the uniquely dual functional characteristic of hAQP10 as a carrier/channel for solute transport, providing a novel insight into its operation mechanism, which would help further elucidate its physiological role. Copyright © 2011 S. Karger AG, Basel.