Reproduction, Fertility and Development Reproduction, Fertility and Development Society
Vertebrate reproductive science and technology
RESEARCH ARTICLE

Lonidamine-ethyl ester-mediated remodelling of the Sertoli cell cytoskeleton induces phosphorylation of plakoglobin and promotes its interaction with α-catenin at the blood–testis barrier

Dolores D. Mruk A D , Michele Bonanomi B C and Bruno Silvestrini B C
+ Author Affiliations
- Author Affiliations

A Center for Biomedical Research, Population Council, 1230 York Avenue, New York, NY 10065, USA.

B S.B.M. Srl–Science of Biology in Medicine, Via Domenico Tardini 35-00167 Rome, Italy.

C Noopolis Foundation, Via Domenico Tardini 35-00167, Rome, Italy.

D Corresponding author. Email: mruk@popcbr.rockefeller.edu

Reproduction, Fertility and Development 29(5) 998-1011 https://doi.org/10.1071/RD15378
Submitted: 20 September 2015  Accepted: 27 January 2016   Published: 7 March 2016

Abstract

Several compounds affect male fertility by disrupting the adhesion of germ cells to Sertoli cells, which results in the release of undeveloped germ cells into the seminiferous tubule lumen that are incapable of fertilising the ovum. Indazole carboxylic acids are one class of compounds exhibiting such effects and they have been investigated as non-hormonal contraceptives for potential human use. The aims of this study were to investigate the effects of lonidamine-ethyl ester, an indazole carboxylic acid, on spermatogenesis and cell junctions, in particular, desmosomes. We found two doses of lonidamine-ethyl ester at 50 mg kg–1 to disrupt Sertoli–germ cell adhesion. By light and fluorescent microscopy, pronounced changes were observed in the distribution of actin microfilaments and intermediate filaments, as well as in the localisation of plakoglobin, a protein with structural and signalling roles at the desmosome and adherens junction at the blood–testis barrier. Furthermore, immunoblotting and immunoprecipitation experiments using testis lysates revealed a significant upregulation (P < 0.01) of plakoglobin and Tyr-phosphorylated plakoglobin. Co-immunoprecipitation experiments showed an increase in the interaction between plakoglobin and fyn proto-oncogene, an Src family non-receptor tyrosine kinase, after treatment, as well as an increase in the interaction between plakoglobin and α-catenin. Taken collectively, these data indicate that a disruption of Sertoli cell and spermatocyte–spermatid adhesion in the seminiferous epithelium by lonidamine-ethyl ester results in the phosphorylation of plakoglobin, thereby promoting its interaction with α-catenin at the blood–testis barrier.

Additional keywords: adjudin, male contraception, spermatogenesis.


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