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BOR - Papers in Press, published online ahead of print April 16, 2003.
Biol Reprod 2003, 10.1095/biolreprod.103.016881
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BIOLOGY OF REPRODUCTION 69, 656–672 (2003)
DOI: 10.1095/biolreprod.103.016881
© 2003 by the Society for the Study of Reproduction, Inc.

Testis

Fer Kinase/FerT and Adherens Junction Dynamics in the Testis: An In Vitro and In Vivo Study1

Yong-mei Chen3, Nikki P.Y. Lee3, Dolores D. Mruk3, Will M. Lee4, and C. Yan Cheng2,3

Population Council,3 New York, New York, 10021 Department of Zoology,4 University of Hong Kong, Hong Kong, Special Administrative Region of China

Fer kinase is a 94-kDa cytoplasmic cell-cell actin-based adherens junction (AJ)-associated nonreceptor protein tyrosine kinase (PTK) found in multiple epithelia including the testis, whereas FerT kinase (51 kDa) is the truncated testis-specific form of Fer kinase, lacking the Fps/Fes/Fer/CIP4 (products of oncogenes identified in avian and feline sarcoma, encoding tyrosine protein kinases) and the three coiled-coil domains versus Fer kinase. Yet the role(s) of Fer kinase in AJ dynamics in the testis remains largely unexplored. We have used an in vitro model of AJ assembly with Sertoli-germ cell cocultures and an in vivo model of AJ disassembly in which adult rats were treated with 1-(2,4-dichlorobenzyl)-indazole-3-carbohydrazide (AF-2364) to study changes in the expression and/or localization of Fer kinase during AJ restructuring. Fer kinase/FerT was expressed by Sertoli and germ cells when cultured in vitro. Using an antibody prepared against a synthetic peptide, NH2-SAPQNCPEEIFTIMMKCWDYK-COOH, corresponding to residues 779–799 of Fer kinase in the rat, which failed to cross-react with FerT kinase, for immunohistochemistry, Fer kinase was detected in the seminiferous epithelium in virtually all stages of the epithelial cycle. At stages XIII-VI, Fer kinase was associated largely with round and elongating spermatids. At stages VII-VIII, Fer kinase associated almost exclusively with round spermatids with very weak staining associated with elongated spermatids. This stage-specific localization of Fer kinase in the epithelium was confirmed by using staged tubules for semiquantitative reverse transcription-polymerase chain reaction. Studies by immunoprecipitation revealed that Fer kinase associated with N-cadherin, {gamma}-catenin, p120ctn, c-Src (a putative PTK and the product of the transforming, sarcoma-inducing gene of Rous sarcoma virus), Rab 8 (a GTPase), actin, vimentin, but not E-cadherin, afadin, nectin-3, and integrin ß1, suggesting Fer kinase associates not only with the actin-based cell-cell AJ structures, such as the N-cadherin/catenin complex (but not the {alpha}6ß1 integrin/laminin and the afadin/nectin complex), but also with intermediate filament-based cell-cell desmosomes. An induction in Fer kinase expression was detected during Sertoli-germ cell AJ assembly in vitro but not during AF-2364-induced AJ disruption in vivo. Yet this AF-2364-induced Fer kinase plummeting associated with an induction in N-cadherin, ß-catenin, and p120ctn, particularly at the base of the seminiferous epithelium. In summary, Fer kinase structurally associates with the N-cadherin/catenin protein complex in the testis and can possibly be used to mediate signaling function via the cadherin/catenin protein complex.

1 This work was supported in part by grants from the CONRAD Program (CICCR CIG 96-05-A and CIG 01-72 to C.Y.C.; CIG-01-74 to D.M.), National Institutes of Health (NICHD, U54 HD29990, Project 3 to C.Y.C.), United States Agency for International Development (HRN-A-00-99-00010, Subproject: AF-2364 Toxicity Study to C.Y.C.), and the Hong Kong Research Grant Council (HKU 7194/01M to W.M.L. and C.Y.C.). Y.-m.C was supported by a fellowship from China Medical Board (6-mo) and a fellowship from the University of Hong Kong (6-mo) during her stay in C.Y.C.'s laboratory. Y.-m.C. and N.P.Y.L. contributed equally to the completion of this work.

2 Correspondence: C. Yan Cheng, Population Council, Center for Biomedical Research, 1230 York Avenue, New York, NY 10021. FAX: 212 327 8733; Y-Cheng{at}popcbr.rockefeller.edu




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