Adhesion and signaling proteins spatiotemporally associated with spermiation in the rat

Spermiation, the process by which late spermatids separate from the Sertoli cell, is disrupted by a number of toxicants. In this study, we used immunohistochemistry (IHC) to identify some of the proteins associated with the spermatid‐Sertoli junction. We confirmed the presence of tubulin, actin, and...

Full description

Saved in:
Bibliographic Details
Published inJournal of andrology Vol. 20; no. 2; pp. 198 - 213
Main Authors Wine, R. N, Chapin, R. E
Format Journal Article
LanguageEnglish
Published Oxford, UK Am Soc Andrology 01.03.1999
Blackwell Publishing Ltd
American Society of Andrology
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary:Spermiation, the process by which late spermatids separate from the Sertoli cell, is disrupted by a number of toxicants. In this study, we used immunohistochemistry (IHC) to identify some of the proteins associated with the spermatid‐Sertoli junction. We confirmed the presence of tubulin, actin, and vinculin at the luminal edge of the seminiferous tubule, and we determined that paxillin is also present here. In other cell types, these proteins have been reported to colocalize with p integrins. Numerous attempts to identify 0 integrins by IHC and by use of Western blots were unsuccessful. Clear evidence was found for the presence of N‐cadherin and its associated intracellular proteins: β‐catenin, pp120, desmoglein, pp60src, and Csk. In addition, N‐cadherin and desmoglein were found around spermatids retained by the epithelium. From these data and previous literature reports, we propose a hypothetical model for spermatid adhesion and the control of that adhesion, thus providing a framework for hypotheses on the steps involved in the complex process of spermiation in rat testes.
ISSN:0196-3635
1939-4640
DOI:10.1002/j.1939-4640.1999.tb02511.x