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Regular Article |
a Program in Membrane Biology and Renal Unit, Department of Medicine, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts 02114
b Unit of Molecular Toxicology, Institute for Medical Research and Occupational Health, 10001 Zagreb, Croatia
ABSTRACT
Fluid movement across epithelia lining portions of the male reproductive tract is important for modulating the luminal environment in which sperm mature and reside, and for increasing sperm concentration. Some regions of the male reproductive tract express aquaporin (AQP) 1 and/or AQP2, but these transmembrane water channels are not detectable in the epididymis. Therefore, we used a specific antibody to map the cellular distribution of another AQP, AQP9 (which is permeable to water and to some solutes), in the male reproductive tract. AQP9 is enriched on the apical (but not basolateral) membrane of nonciliated cells in the efferent duct and principal cells of the epididymis (rat and human) and vas deferens, where it could play a role in fluid reabsorption. Western blotting revealed a strong 30-kDa band in brush-border membrane vesicles isolated from the epididymis. AQP9 is also expressed in epithelial cells of the prostate and coagulating gland where fluid transport across the epithelium is important for secretory activity. However, it was undetectable in the seminal vesicle, suggesting that an alternative fluid transport pathway may be present in this tissue. Intracellular vesicles in epithelial cells along the reproductive tract were generally poorly stained for AQP9. Furthermore, the apical membrane distribution of AQP9 was unaffected by microtubule disruption. These data suggest that AQP9 is a constitutively inserted apical membrane protein and that its cell-surface expression is not acutely regulated by vesicular trafficking. AQP9 was detectable in the epididymis and vas deferens of 1-wk postnatal rats, but its expression was comparable with adult rats only after 3–4 wk. AQP9 could provide a route via which apical fluid and solute transport occurs in several regions of the male reproductive tract. The heterogenous and segment-specific expression of AQP9 and other aquaporins along the male reproductive tract shown in this and in our previous studies suggests that fluid reabsorption and secretion in these tissues could be locally modulated by physiological regulation of AQP expression and/or function.
First decision: 26 January 2001.
1 This work was supported by NIH grant DK38452 (D.B. and S.B.), DK55864 (A.V.H.), and an NIH Fogerty International Research Collaboration Award TW01057 (I.S. and D.B.). The Microscopy Core Facility of the MGH Program in Membrane Biology is additionally supported by a CSIBD Center Grant DK43351 and a DERC award DK57521. Research fellowships from INSERM, the Arthur Sachs Foundation (as part of the Fullbright Program), L'Assistance Publique, and the Association des Femmes Diplômées des Universités supported C.B. N.P.-S. was supported by an NIH NRSA HD08684.
2 Correspondence: Dennis Brown, Program in Membrane Biology/Renal Unit, Massachusetts General Hospital East, 149 13th Street, Charlestown, MA 02129. FAX: 617 726 5669; brown{at}receptor.mgh.harvard.edu
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