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Isoforms of angiotensin I-converting enzyme in the development and differentiation of human testis and epididymis: ACEin human testis and epididymis by K. Pauls; R. Metzger; K. Steger; T. Klonisch; S. Danilov; F. E. Franke is a Medicine article available to read on EtoBox.

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Angiotensin I-converting enzyme (ACE; CD143, Kininase II, EC 3.4.15.1) is known to be crucial for male fertility in animal models. We therefore studied its testicular (tACE) and somatic (sACE) isoforms in foetal and adult human testis and epididymis using monoclonal antibodies and cRNA probes. During spermatogenesis, tACE was found only in differentiating germ cells and was the only isoform within the seminiferous tubules of adult men. Although tACE mRNA was present in spermatocytes, tACE protein was initially found in post-meiotic step 3 spermatids and increased markedly during further differentiation. The enzyme was strictly confined to the adluminal membrane site of elongating spermatids and was localized at the neck and midpiece region of released and ejaculated spermatozoa. In contrast, sACE was expressed heterogeneously in Leydig cells and endothelial cells of the testicular interstitium, and homogeneously along the luminal surface of epithelial cells lining the ductuli efferents, corpus and cauda of epididymis, and vas deferens. The cell- and site-restricted pattern of sACE corresponded to that found in foetal tissues except an additional and transient expression of sACE in

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Author

K. Pauls; R. Metzger; K. Steger; T. Klonisch; S. Danilov; F. E. Franke

Publisher

Hindawi Limited

Published

2003

Language

EN

Field

Medicine (Health Sciences)