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Article: Fer kinase/FerT and adherens junction dynamics in the testis: An in vitro and in vivo study

TitleFer kinase/FerT and adherens junction dynamics in the testis: An in vitro and in vivo study
Authors
KeywordsKinases
Sertoli cells
Signal transducers
Signal transduction
Testis
Issue Date2003
PublisherSociety for the Study of Reproduction. The Journal's web site is located at http://www.biolreprod.org/
Citation
Biology Of Reproduction, 2003, v. 69 n. 2, p. 656-672 How to Cite?
AbstractFer 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, γ-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 β1, suggesting Fer kinase associates not only with the actin-based cell-cell AJ structures, such as the N-cadherin/catenin complex (but not the α6β1 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, β-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.
Persistent Identifierhttp://hdl.handle.net/10722/172833
ISSN
2015 Impact Factor: 3.471
2015 SCImago Journal Rankings: 1.646
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorChen, YMen_HK
dc.contributor.authorLee, NPYen_HK
dc.contributor.authorMruk, DDen_HK
dc.contributor.authorLee, WMen_HK
dc.contributor.authorCheng, CYen_HK
dc.date.accessioned2012-10-30T06:25:11Z-
dc.date.available2012-10-30T06:25:11Z-
dc.date.issued2003en_HK
dc.identifier.citationBiology Of Reproduction, 2003, v. 69 n. 2, p. 656-672en_HK
dc.identifier.issn0006-3363en_HK
dc.identifier.urihttp://hdl.handle.net/10722/172833-
dc.description.abstractFer 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, γ-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 β1, suggesting Fer kinase associates not only with the actin-based cell-cell AJ structures, such as the N-cadherin/catenin complex (but not the α6β1 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, β-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.en_HK
dc.languageengen_US
dc.publisherSociety for the Study of Reproduction. The Journal's web site is located at http://www.biolreprod.org/en_HK
dc.relation.ispartofBiology of Reproductionen_HK
dc.subjectKinasesen_HK
dc.subjectSertoli cellsen_HK
dc.subjectSignal transducersen_HK
dc.subjectSignal transductionen_HK
dc.subjectTestisen_HK
dc.subject.meshAdherens Junctions - Physiologyen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCadherins - Metabolismen_US
dc.subject.meshCells, Cultureden_US
dc.subject.meshCoculture Techniquesen_US
dc.subject.meshCytoskeletal Proteins - Metabolismen_US
dc.subject.meshDna Primersen_US
dc.subject.meshGerm Cellsen_US
dc.subject.meshHydrazines - Pharmacologyen_US
dc.subject.meshIndazoles - Pharmacologyen_US
dc.subject.meshMaleen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshPeptides - Chemical Synthesisen_US
dc.subject.meshProtein-Tyrosine Kinases - Physiologyen_US
dc.subject.meshProto-Oncogene Proteins - Metabolismen_US
dc.subject.meshRna, Messenger - Biosynthesisen_US
dc.subject.meshRatsen_US
dc.subject.meshRats, Sprague-Dawleyen_US
dc.subject.meshSeminiferous Tubules - Physiologyen_US
dc.subject.meshSertoli Cells - Metabolismen_US
dc.subject.meshSpermatogenesis - Physiologyen_US
dc.subject.meshTestis - Physiologyen_US
dc.subject.meshTrans-Activators - Metabolismen_US
dc.subject.meshBeta Cateninen_US
dc.titleFer kinase/FerT and adherens junction dynamics in the testis: An in vitro and in vivo studyen_HK
dc.typeArticleen_HK
dc.identifier.emailLee, NPY: nikkilee@hku.hken_HK
dc.identifier.emailLee, WM: hrszlwm@hku.hken_HK
dc.identifier.authorityLee, NPY=rp00263en_HK
dc.identifier.authorityLee, WM=rp00728en_HK
dc.description.naturelink_to_OA_fulltexten_US
dc.identifier.doi10.1095/biolreprod.103.016881en_HK
dc.identifier.pmid12700184-
dc.identifier.scopuseid_2-s2.0-0038299227en_HK
dc.identifier.hkuros81279-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0038299227&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume69en_HK
dc.identifier.issue2en_HK
dc.identifier.spage656en_HK
dc.identifier.epage672en_HK
dc.identifier.isiWOS:000184311100036-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridChen, YM=9337790600en_HK
dc.identifier.scopusauthoridLee, NPY=7402722690en_HK
dc.identifier.scopusauthoridMruk, DD=6701823934en_HK
dc.identifier.scopusauthoridLee, WM=24799156600en_HK
dc.identifier.scopusauthoridCheng, CY=7404797787en_HK

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