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Immunohistochemical Demonstration of Androgen-Binding Protein in the Rat Prostatic Gland1
Author(s) -
Jorge LarrivaSahd,
Héctor Orozco,
Rogelio HernándezPando,
Rosa María OliartRos,
Neal A. Musto,
Fernando Larrea
Publication year - 1991
Publication title -
biology of reproduction
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.366
H-Index - 180
eISSN - 1529-7268
pISSN - 0006-3363
DOI - 10.1095/biolreprod45.3.417
Subject(s) - epididymis , androgen binding protein , efferent ducts , sertoli cell , biology , seminal vesicle , endocrinology , medicine , androgen , prostate , testicle , immunohistochemistry , spermatogenesis , testosterone (patch) , epithelium , andrology , sperm , hormone , immunology , botany , genetics , cancer
Androgen-binding protein (ABP) is one of the best-characterized products of synthesis by the Sertoli cells in the rat. Although the exact physiological role of ABP remains to be determined, it has been widely used to study Sertoli cells and testicular function in this species. Since this protein is the principal carrier for testosterone in rat testis and epididymis, we decided to investigate ABP immunoreactivity (ABP-I) in androgen-dependent organs, including testicle, epididymides, prostate, and seminal vesicles. The location of ABP was investigated by immunohistochemistry using specific antisera against rat ABP. As previously described in the testis, rat ABP-I was identified in the seminiferous tubules within the cytoplasm of the Sertoli cells and the tubular luminae. The epididymis showed ABP-I only in epithelial cells of the proximal caput. We demonstrated ABP-I in the apical portions of epithelial cells of the rat prostate. Short-term castration and/or ligation of the efferent ducts did not suppress prostatic ABP-I. ABP-I was not present in seminal vesicles of control rats nor under any of the experimental conditions used throughout this study. The results also indicate the presence of ABP-I in prostatic epithelium, probably because of a mechanism similar to that described in epididymis. Our data support and enhance the concept that ABP may serve as a transmembrane carrier protein for androgens in androgen target organs in the male reproductive tract.

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