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Article: Protein kinases and adherens junction dynamics in the seminiferous epithelium of the rat testis

TitleProtein kinases and adherens junction dynamics in the seminiferous epithelium of the rat testis
Authors
Issue Date2005
PublisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/31010
Citation
Journal Of Cellular Physiology, 2005, v. 202 n. 2, p. 344-360 How to Cite?
AbstractEarlier studies in multiple epithelia have shown that cell-cell actin-based adherens junction (AJ) dynamics are regulated, at least in part, by the interplay of kinases and phosphatases that determines the intracellular phosphoprotein content. Yet it is virtually unknown regarding the role of protein kinases in Sertoli-germ cell AJ dynamics in the seminiferous epithelium of the testis. To address this issue, an in vitro coculture system utilizing Sertoli and germ cells was used to study the regulation of several protein kinases, including c-Src (the cellular form of the v-src transforming gene of Rous Sarcoma virus, RSV), carboxyl-terminal Src kinase (Csk), and casein kinase 2 (CK2), during AJ assembly. Both Sertoli and germ cells were shown to express c-Src, Csk, and CK2 with a relative Sertoli:germ cell ratio of ∼1:1, suggesting both cell types contributed equally to the pool of these kinases in the epithelium. c-Src and Csk were shown to be stage-specific proteins during the epithelial cycle, being highest at stages VII-VIII. Studies using immunoprecipitation have illustrated that these kinases were structurally associated with the N-cadherin/β-catenin, but not the nectin/afadin, protein complex, implicating that the cadherin/catenin protein complex is their likely putative substrate. An induction in c-Src, Csk, and CK2 were detected during Sertoli-germ cell AJ assembly in vitro but not when Sertoli cells were cultured alone. When adult rats were treated with 1-(2,4-dichlorobenzyl)- indazole-3-carbohydrazide (AF-2364), a compound known to induce germ cell loss from the seminiferous epithelium, in particular elongating/elongate and round spermatids, by disrupting Sertoli-germ cell AJs, an induction of c-Src and Csk, but not CK2, was detected. Furthermore, a transient increase in the intrinsic kinase activities of c-Src, but not CK2, was also detected. This event was also associated with a loss of protein-protein association of N-cadherin and β-catenin from the cadherin/catenin/c-Src/Csk/CK2 protein complex. Administration of PP1, a c-Src inhibitor, into adult rats via the jugular vein could induce the loss of spermatocytes and round spermatids, but not elongating/elongate spermatids, from the seminiferous epithelium. This result thus implicates the importance of c-Src in maintaining the integrity of AJs and possibly desmosome-like junctions between Sertoli cells and spermatocytes/round spermatids. In short, the data reported herein have shown that c-Src, Csk, and CK2 are novel protein kinases in AJ dynamics in the testis. © 2004 Wiley-Liss, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/143480
ISSN
2015 Impact Factor: 4.155
2015 SCImago Journal Rankings: 1.842
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLee, NPYen_HK
dc.contributor.authorCheng, CYen_HK
dc.date.accessioned2011-12-02T05:22:11Z-
dc.date.available2011-12-02T05:22:11Z-
dc.date.issued2005en_HK
dc.identifier.citationJournal Of Cellular Physiology, 2005, v. 202 n. 2, p. 344-360en_HK
dc.identifier.issn0021-9541en_HK
dc.identifier.urihttp://hdl.handle.net/10722/143480-
dc.description.abstractEarlier studies in multiple epithelia have shown that cell-cell actin-based adherens junction (AJ) dynamics are regulated, at least in part, by the interplay of kinases and phosphatases that determines the intracellular phosphoprotein content. Yet it is virtually unknown regarding the role of protein kinases in Sertoli-germ cell AJ dynamics in the seminiferous epithelium of the testis. To address this issue, an in vitro coculture system utilizing Sertoli and germ cells was used to study the regulation of several protein kinases, including c-Src (the cellular form of the v-src transforming gene of Rous Sarcoma virus, RSV), carboxyl-terminal Src kinase (Csk), and casein kinase 2 (CK2), during AJ assembly. Both Sertoli and germ cells were shown to express c-Src, Csk, and CK2 with a relative Sertoli:germ cell ratio of ∼1:1, suggesting both cell types contributed equally to the pool of these kinases in the epithelium. c-Src and Csk were shown to be stage-specific proteins during the epithelial cycle, being highest at stages VII-VIII. Studies using immunoprecipitation have illustrated that these kinases were structurally associated with the N-cadherin/β-catenin, but not the nectin/afadin, protein complex, implicating that the cadherin/catenin protein complex is their likely putative substrate. An induction in c-Src, Csk, and CK2 were detected during Sertoli-germ cell AJ assembly in vitro but not when Sertoli cells were cultured alone. When adult rats were treated with 1-(2,4-dichlorobenzyl)- indazole-3-carbohydrazide (AF-2364), a compound known to induce germ cell loss from the seminiferous epithelium, in particular elongating/elongate and round spermatids, by disrupting Sertoli-germ cell AJs, an induction of c-Src and Csk, but not CK2, was detected. Furthermore, a transient increase in the intrinsic kinase activities of c-Src, but not CK2, was also detected. This event was also associated with a loss of protein-protein association of N-cadherin and β-catenin from the cadherin/catenin/c-Src/Csk/CK2 protein complex. Administration of PP1, a c-Src inhibitor, into adult rats via the jugular vein could induce the loss of spermatocytes and round spermatids, but not elongating/elongate spermatids, from the seminiferous epithelium. This result thus implicates the importance of c-Src in maintaining the integrity of AJs and possibly desmosome-like junctions between Sertoli cells and spermatocytes/round spermatids. In short, the data reported herein have shown that c-Src, Csk, and CK2 are novel protein kinases in AJ dynamics in the testis. © 2004 Wiley-Liss, Inc.en_HK
dc.languageengen_US
dc.publisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/31010en_HK
dc.relation.ispartofJournal of Cellular Physiologyen_HK
dc.subject.meshAdherens Junctionsen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCadherinsen_US
dc.subject.meshCasein Kinase IIen_US
dc.subject.meshCell Adhesionen_US
dc.subject.meshCell Cycleen_US
dc.subject.meshCells - Cultureden_US
dc.subject.meshCoculture Techniquesen_US
dc.subject.meshCytoskeletal Proteinsen_US
dc.subject.meshHydrazinesen_US
dc.subject.meshIndazolesen_US
dc.subject.meshMaleen_US
dc.subject.meshProtein Kinasesen_US
dc.subject.meshProtein - Tyrosine Kinasesen_US
dc.subject.meshProto - Oncogene Proteins pp60(c-src)en_US
dc.subject.meshPyrazolesen_US
dc.subject.meshPyrimidinesen_US
dc.subject.meshRatsen_US
dc.subject.meshRats - Sprague - Dawleyen_US
dc.subject.meshSeminiferous Epitheliumen_US
dc.subject.meshSertoli Cellsen_US
dc.subject.meshSpermatozoaen_US
dc.subject.meshTestisen_US
dc.subject.meshTissue Distributionen_US
dc.subject.meshTrans - Activatorsen_US
dc.subject.meshbeta Cateninen_US
dc.titleProtein kinases and adherens junction dynamics in the seminiferous epithelium of the rat testisen_HK
dc.typeArticleen_HK
dc.identifier.emailLee, NPY: nikkilee@hku.hken_HK
dc.identifier.authorityLee, NPY=rp00263en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1002/jcp.20119en_HK
dc.identifier.pmid15389520-
dc.identifier.scopuseid_2-s2.0-11144249434en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-11144249434&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume202en_HK
dc.identifier.issue2en_HK
dc.identifier.spage344en_HK
dc.identifier.epage360en_HK
dc.identifier.isiWOS:000226089400004-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLee, NPY=7402722690en_HK
dc.identifier.scopusauthoridCheng, CY=7404797787en_HK

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