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From the * Department of Morphology, Federal
University of Minas Gerais, Belo Horizonte, MG, Brazil; and the
Department of Veterinary Biosciences,
University of Illinois, Urbana, Illinois.
| Correspondence to: Dr Rex A. Hess, Department of Veterinary Biosciences, University of Illinois, 2001 S Lincoln, Urbana, IL 61802-6199 (e-mail: rexhess{at}illinois.edu). |
Efferent ductules of the male reproductive tract contain high
concentrations of estrogen receptors (ER), which are essential for the
regulation of fluid reabsorption and maintenance of normal epithelial
morphology. Treatments with the antiestrogen ICI 182,780 and
17β-estradiol cause a reduction in ER
expression; however, the
mechanisms governing the down-regulation are undetermined. In other tissues,
the ubiquitin-proteasome pathway appears to have a dominant role in regulating
ER
turnover, although in the efferent ductules, an abundance of
epithelial lysosomes could also participate in protein turnover. To study this
activity, the expressions of proteasome, ubiquitin, and markers for the
endocytotic apparatus (early endosome antigen-1 [EEA1], clusterin, and
cathepsin D) were examined in rat efferent ductules and initial segment of
epididymis. Distinct cellular, subcellular, and regional distributions of
these proteins were observed in the epithelial cells. A gradient of
proteasome, ubiquitin, EEA1, and clusterin staining was seen in the efferent
ducts, which decreased 30%–41% from the proximal zone to the terminal
common duct. Antiestrogen treatment resulted in significant decreases in
proteasome, EEA1, and clusterin in the efferent ducts. Localization of
ubiquitin-proteasome and endocytotic pathway components suggests that
differential regulation is required for protein degradation and turnover in
efferent ductules and head of the epididymis.
Key words: Lysosome, endosome, cathepsin, ICI 182,780
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