title: Membrane domain specificity in the spatial distribution of aquaporins 5, 7, 9, and 11 in efferent ducts and epididymis of rats.
abstract: Water content within the epididymis of the male reproductive system is stringently regulated 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 light microscopy immunolocalizations using peroxidase and wide-field fluorescence techniques. The results indicate that several AQPs are coexpressed 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, whereas AQP 7 was localized primarily to lateral and 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 and 11), clear (AQP 7 and 9), and halo (AQP 7 and 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.
authors.affiliation: Department of Anatomy and Cell Biology, McGill University, 3640 University Street, Montreal, Quebec, Canada H3A 2B2. louis.hermo@mcgill.ca
authors.forename: Louis
authors.initials: L
authors.lastname: Hermo
authors.forename: Morgan
authors.initials: M
authors.lastname: Schellenberg
authors.forename: Lauren Ye
authors.initials: LY
authors.lastname: Liu
authors.forename: Bama
authors.initials: B
authors.lastname: Dayanandan
authors.forename: Tong
authors.initials: T
authors.lastname: Zhang
authors.forename: Craig A
authors.initials: CA
authors.lastname: Mandato
authors.forename: Charles E
authors.initials: CE
authors.lastname: Smith
mesh_terms: D000818:Animals; D051402:Aquaporin 5 / Q000096:biosynthesis; D020346:Aquaporins / Q000096:biosynthesis*; D002462:Cell Membrane / Q000378:metabolism* / Q000648:ultrastructure; D011992:Endosomes / Q000378:metabolism; D004822:Epididymis / Q000378:metabolism* / Q000648:ultrastructure; D007150:Immunohistochemistry; D008297:Male; D008871:Microvilli / Q000378:metabolism; D051381:Rats; D017207:Rats, Sprague-Dawley; D020133:Reverse Transcriptase Polymerase Chain Reaction; D013737:Testis / Q000378:metabolism* / Q000648:ultrastructure
chemical_list: C496040:Aqp5 protein, rat; C491926:Aqp7 protein, rat; C491637:Aqp9 protein, rat; D051402:Aquaporin 5; D020346:Aquaporins; C511252:aquaporin 11, rat
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