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Article: Adhering junction dynamics in the testis are regulated by an interplay of β1-integrin and focal adhesion complex-associated proteins

TitleAdhering junction dynamics in the testis are regulated by an interplay of β1-integrin and focal adhesion complex-associated proteins
Authors
Issue Date2003
PublisherThe Endocrine Society. The Journal's web site is located at http://endo.endojournals.org
Citation
Endocrinology, 2003, v. 144 n. 5, p. 2141-2163 How to Cite?
AbstractDuring spermatogenesis, the movement of developing germ cells across the seminiferous epithelium associates with extensive restructuring of cell-cell actin-based adherens junctions (AJs), such as ectoplasmic specialization (ES, a testis-specific AJ junction), between Sertoli and germ cells. Although this event of germ cell movement is essential to the completion of spermatogenesis, the mechanism(s) that regulates AJ restructuring is largely unknown. Using Sertoli-germ cells cocultured in vitro to study the regulation of AJ assembly, it was shown that this event associated with a transient induction of β1-integrin, vinculin, p-FAK-Tyr397, and phosphatidylinositol 3-kinase (PI3K) but not the nonphosphorylated form of focal adhesion kinase (FAK), paxillin, and p130 Cas. Furthermore, p-FAK-Tyr397 was shown to coimmunoprecipitate with β1-integrin, vinculin, and c-Src both in vitro and in vivo using Sertoli-germ cell cocultures and seminiferous tubules, respectively. These results seemingly suggest that the testis is using constituent proteins of the focal adhesion complex (FAC) found in other epithelia between cell and extracellular matrix to regulate AJ dynamics. To further confirm that p-FAK, a putative FAC protein in other epithelia, is indeed present at the site of ES, immunohistochemistry and immunofluorescent microscopy were used. The p-FAK-Tyr397 and p-FAK-Tyr576 were found to localize almost exclusively at the site of apical ES with weak staining at the basal ES in the seminiferous epithelium in a stage-specific manner, being highest at stages VI-VIII. In contrast, FAK was largely restricted to the basal compartment but with weak staining at the apical compartment. When rats were treated with 1-(2,4-dichlorobenzyl)-indazole-3-carbohydrazide (AF-2364) to perturb Sertoli-germ cell AJs, an induction of β1-integrin, vinculin, p-FAK-Tyr397, PI3K, and p130 Cas but not the nonphosphorylated form of FAK and paxillin was also detected in the testis, coinciding with the time spermatids began to deplete from the epithelium, indicating their involvement in AJ disassembly. Thereafter, the levels of vinculin, p-FAK-Tyr397, PI3K, and p130 Cas in the testis plunged, coinciding with the declining events of AJ disruption when virtually all spermatids were depleted from the epithelium. Taken collectively, these results suggest a bifunctional role of p-FAK, being involved in the events of Sertoli-germ cell AJ assembly and disassembly. In summary, the events of AJ dynamics in the testis, in particular at the site of ES, are regulated, at least in part, by proteins that are found in the FAC in other epithelia, such as β1-integrin, vinculin, and FAK utilizing the integrin/pFAK/PI3K/p130 Cas signaling pathway.
Persistent Identifierhttp://hdl.handle.net/10722/178799
ISSN
2015 Impact Factor: 4.159
2015 SCImago Journal Rankings: 2.363
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorSiu, MKYen_US
dc.contributor.authorMruk, DDen_US
dc.contributor.authorLee, WMen_US
dc.contributor.authorCheng, CYen_US
dc.date.accessioned2012-12-19T09:49:48Z-
dc.date.available2012-12-19T09:49:48Z-
dc.date.issued2003en_US
dc.identifier.citationEndocrinology, 2003, v. 144 n. 5, p. 2141-2163en_US
dc.identifier.issn0013-7227en_US
dc.identifier.urihttp://hdl.handle.net/10722/178799-
dc.description.abstractDuring spermatogenesis, the movement of developing germ cells across the seminiferous epithelium associates with extensive restructuring of cell-cell actin-based adherens junctions (AJs), such as ectoplasmic specialization (ES, a testis-specific AJ junction), between Sertoli and germ cells. Although this event of germ cell movement is essential to the completion of spermatogenesis, the mechanism(s) that regulates AJ restructuring is largely unknown. Using Sertoli-germ cells cocultured in vitro to study the regulation of AJ assembly, it was shown that this event associated with a transient induction of β1-integrin, vinculin, p-FAK-Tyr397, and phosphatidylinositol 3-kinase (PI3K) but not the nonphosphorylated form of focal adhesion kinase (FAK), paxillin, and p130 Cas. Furthermore, p-FAK-Tyr397 was shown to coimmunoprecipitate with β1-integrin, vinculin, and c-Src both in vitro and in vivo using Sertoli-germ cell cocultures and seminiferous tubules, respectively. These results seemingly suggest that the testis is using constituent proteins of the focal adhesion complex (FAC) found in other epithelia between cell and extracellular matrix to regulate AJ dynamics. To further confirm that p-FAK, a putative FAC protein in other epithelia, is indeed present at the site of ES, immunohistochemistry and immunofluorescent microscopy were used. The p-FAK-Tyr397 and p-FAK-Tyr576 were found to localize almost exclusively at the site of apical ES with weak staining at the basal ES in the seminiferous epithelium in a stage-specific manner, being highest at stages VI-VIII. In contrast, FAK was largely restricted to the basal compartment but with weak staining at the apical compartment. When rats were treated with 1-(2,4-dichlorobenzyl)-indazole-3-carbohydrazide (AF-2364) to perturb Sertoli-germ cell AJs, an induction of β1-integrin, vinculin, p-FAK-Tyr397, PI3K, and p130 Cas but not the nonphosphorylated form of FAK and paxillin was also detected in the testis, coinciding with the time spermatids began to deplete from the epithelium, indicating their involvement in AJ disassembly. Thereafter, the levels of vinculin, p-FAK-Tyr397, PI3K, and p130 Cas in the testis plunged, coinciding with the declining events of AJ disruption when virtually all spermatids were depleted from the epithelium. Taken collectively, these results suggest a bifunctional role of p-FAK, being involved in the events of Sertoli-germ cell AJ assembly and disassembly. In summary, the events of AJ dynamics in the testis, in particular at the site of ES, are regulated, at least in part, by proteins that are found in the FAC in other epithelia, such as β1-integrin, vinculin, and FAK utilizing the integrin/pFAK/PI3K/p130 Cas signaling pathway.en_US
dc.languageengen_US
dc.publisherThe Endocrine Society. The Journal's web site is located at http://endo.endojournals.orgen_US
dc.relation.ispartofEndocrinologyen_US
dc.rightsEndocrinology. Copyright © The Endocrine Society.-
dc.subject.meshAdherens Junctions - Physiologyen_US
dc.subject.meshAnimalsen_US
dc.subject.meshAntigens, Cd29 - Physiologyen_US
dc.subject.meshCoculture Techniquesen_US
dc.subject.meshCulture Media, Conditioned - Pharmacologyen_US
dc.subject.meshFocal Adhesion Kinase 1en_US
dc.subject.meshFocal Adhesion Protein-Tyrosine Kinasesen_US
dc.subject.meshFocal Adhesions - Metabolismen_US
dc.subject.meshGene Expression Regulation, Developmentalen_US
dc.subject.meshMaleen_US
dc.subject.meshPhosphorylationen_US
dc.subject.meshProtein-Tyrosine Kinases - Metabolismen_US
dc.subject.meshRna, Messenger - Metabolismen_US
dc.subject.meshRatsen_US
dc.subject.meshRats, Sprague-Dawleyen_US
dc.subject.meshSertoli Cells - Metabolismen_US
dc.subject.meshSpermatozoa - Metabolismen_US
dc.subject.meshTestis - Physiologyen_US
dc.subject.meshTyrosine - Metabolismen_US
dc.subject.meshVinculin - Geneticsen_US
dc.titleAdhering junction dynamics in the testis are regulated by an interplay of β1-integrin and focal adhesion complex-associated proteinsen_US
dc.typeArticleen_US
dc.identifier.emailSiu, MKY: mkysiu@hkucc.hku.hken_US
dc.identifier.emailLee, WM: hrszlwm@hku.hken_US
dc.identifier.authoritySiu, MKY=rp00275en_US
dc.identifier.authorityLee, WM=rp00728en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1210/en.2002-221035en_US
dc.identifier.pmid12697723-
dc.identifier.scopuseid_2-s2.0-0038070531en_US
dc.identifier.hkuros81235-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0038070531&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume144en_US
dc.identifier.issue5en_US
dc.identifier.spage2141en_US
dc.identifier.epage2163en_US
dc.identifier.isiWOS:000182269800057-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridSiu, MKY=24924018400en_US
dc.identifier.scopusauthoridMruk, DD=6701823934en_US
dc.identifier.scopusauthoridLee, WM=24799156600en_US
dc.identifier.scopusauthoridCheng, CY=7404797787en_US

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