Membrane Domain Specificity in the Spatial Distribution of Aquaporins 5, 7, 9, and 11 in Efferent Ducts and Epididymis of Rats

Louis Hermo ^1*, Morgan Schellenberg ¹, Lauren Ye Liu ¹, Bama Dayanandan ¹, Tong Zhang ¹, Craig A. Mandato ¹ and Charles E. Smith ¹

¹ Department of Anatomy and Cell Biology, McGill University, Montreal, Quebec, Canada (LH,MS,LYL,BD,TZ,CAM), and Department de Stomatologie, Université de Montréal, Montreal, Quebec, Canada (CES)

^* To whom correspondence should be addressed. E-mail: louis hermo{at}mcgill. Ca.

Submitted on May 20, 2008
Accepted on 28 August 2008

	Abstract

Water content within the epididymis of the male reproductive system is stringently regulated in order to promote sperm maturation. Several members of the aquaporin (AQP) family of water channel-forming integral membrane proteins have been identified in epididymal cells, but expression profiling for this epithelium is presently incomplete and no AQP isoform has yet been identified on basolateral plasma membranes of these cells. In this study we explored AQP expression by RT-PCR and LM immunolocalizations using peroxidase and wide-field fluorescence techniques. The results indicate that several AQPs are co-expressed in the epididymis including AQP 5, 7, 9 and 11. Immunolocalizations suggested complex patterns in the spatial distribution of these AQPs. In principal cells, AQP 9 and 11 were present mainly on microvilli, while AQP 7 was localized primarily to lateral then to basal plasma membranes in a region-specific manner. AQP 5 was also expressed regionally but was associated with membranes of endosomes. Additionally, AQPs were expressed by some but not all basal (AQP 7,11), clear (AQP 7,9) and halo (AQP 7,11) cells. These findings indicate unique associations of AQPs with specific membrane domains in a cell type and region specific manner within the epididymis of adult animals.

Key Words: aquaporins, efferent ducts, epididymis, principal and clear cells, RT-PCR, immunocytochemistry

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