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Article: C-Yes regulates cell adhesion at the blood-testis barrier and the apical ectoplasmic specialization in the seminiferous epithelium of rat testes

TitleC-Yes regulates cell adhesion at the blood-testis barrier and the apical ectoplasmic specialization in the seminiferous epithelium of rat testes
Authors
KeywordsApical ectoplasmic specialization
Blood-testis barrier
c-Yes
Cell adhesion
Seminiferous epithelial cycle
Spermatogenesis
Testis
Issue Date2011
PublisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/biocel
Citation
International Journal Of Biochemistry And Cell Biology, 2011, v. 43 n. 4, p. 651-665 How to Cite?
AbstractDuring spermatogenesis, extensive junction restructuring takes place at the blood-testis barrier (BTB) and the Sertoli cell-spermatid interface known as the apical ectoplasmic specialization (apical ES, a testis-specific adherens junction) in the seminiferous epithelium. However, the mechanism(s) that regulates these critical events in the testis remains unknown. Based on the current concept in the field, changes in the phosphorylation status of integral membrane proteins at these sites can induce alterations in protein endocytosis and recycling, causing junction restructuring. Herein, c-Yes, a non-receptor protein tyrosine kinase, was found to express abundantly at the BTB and apical ES stage-specifically, coinciding with junction restructuring events at these sites during the seminiferous epithelial cycle of spermatogenesis. c-Yes also structurally associated with adhesion proteins at the BTB (e.g., occludin and N-cadherin) and the apical ES (e.g., β1-integrin, laminins β3 and γ3), possibly to regulate phosphorylation status of proteins at these sites. SU6656, a selective c-Yes inhibitor, was shown to perturb the Sertoli cell tight junction-permeability barrier in vitro, which is mediated by changes in the distribution of occludin and N-cadherin at the cell-cell interface, moving from cell surface to cytosol, thereby destabilizing the tight junction-barrier. However, this disruptive effect of SU6656 on the barrier was blocked by testosterone. Furthermore, c-Yes is crucial to maintain the actin filament network in Sertoli cells since a blockade of c-Yes by SU6656 induced actin filament disorganization. In summary, c-Yes regulates BTB and apical ES integrity by maintaining proper distribution of integral membrane proteins and actin filament organization at these sites. © 2011 Elsevier Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/140890
ISSN
2015 Impact Factor: 3.905
2015 SCImago Journal Rankings: 2.003
PubMed Central ID
ISI Accession Number ID
Funding AgencyGrant Number
National Institutes of HealthNICHD R01 HD056034
R01 HD056034-02S1
HD029990
R03 HD061401
Hong Kong Research Grants Council
CRCG of the University of Hong Kong
Funding Information:

This work was supported in part by grants from the National Institutes of Health (NICHD R01 HD056034 and R01 HD056034-02S1 to CYC; HD029990 Project 5 to CYC: R03 HD061401 to DDM) and Hong Kong Research Grants Council and CRCG of the University of Hong Kong (to WML).

References

 

DC FieldValueLanguage
dc.contributor.authorXiao, Xen_HK
dc.contributor.authorMruk, DDen_HK
dc.contributor.authorLee, WMen_HK
dc.contributor.authorCheng, CYen_HK
dc.date.accessioned2011-09-23T06:20:59Z-
dc.date.available2011-09-23T06:20:59Z-
dc.date.issued2011en_HK
dc.identifier.citationInternational Journal Of Biochemistry And Cell Biology, 2011, v. 43 n. 4, p. 651-665en_HK
dc.identifier.issn1357-2725en_HK
dc.identifier.urihttp://hdl.handle.net/10722/140890-
dc.description.abstractDuring spermatogenesis, extensive junction restructuring takes place at the blood-testis barrier (BTB) and the Sertoli cell-spermatid interface known as the apical ectoplasmic specialization (apical ES, a testis-specific adherens junction) in the seminiferous epithelium. However, the mechanism(s) that regulates these critical events in the testis remains unknown. Based on the current concept in the field, changes in the phosphorylation status of integral membrane proteins at these sites can induce alterations in protein endocytosis and recycling, causing junction restructuring. Herein, c-Yes, a non-receptor protein tyrosine kinase, was found to express abundantly at the BTB and apical ES stage-specifically, coinciding with junction restructuring events at these sites during the seminiferous epithelial cycle of spermatogenesis. c-Yes also structurally associated with adhesion proteins at the BTB (e.g., occludin and N-cadherin) and the apical ES (e.g., β1-integrin, laminins β3 and γ3), possibly to regulate phosphorylation status of proteins at these sites. SU6656, a selective c-Yes inhibitor, was shown to perturb the Sertoli cell tight junction-permeability barrier in vitro, which is mediated by changes in the distribution of occludin and N-cadherin at the cell-cell interface, moving from cell surface to cytosol, thereby destabilizing the tight junction-barrier. However, this disruptive effect of SU6656 on the barrier was blocked by testosterone. Furthermore, c-Yes is crucial to maintain the actin filament network in Sertoli cells since a blockade of c-Yes by SU6656 induced actin filament disorganization. In summary, c-Yes regulates BTB and apical ES integrity by maintaining proper distribution of integral membrane proteins and actin filament organization at these sites. © 2011 Elsevier Ltd. All rights reserved.en_HK
dc.languageengen_US
dc.publisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/biocelen_HK
dc.relation.ispartofInternational Journal of Biochemistry and Cell Biologyen_HK
dc.subjectApical ectoplasmic specializationen_HK
dc.subjectBlood-testis barrieren_HK
dc.subjectc-Yesen_HK
dc.subjectCell adhesionen_HK
dc.subjectSeminiferous epithelial cycleen_HK
dc.subjectSpermatogenesisen_HK
dc.subjectTestisen_HK
dc.subject.meshAdherens Junctions - drug effects - metabolism-
dc.subject.meshBlood-Testis Barrier - drug effects - metabolism-
dc.subject.meshClathrin - metabolism-
dc.subject.meshProto-Oncogene Proteins c-yes - metabolism-
dc.subject.meshSeminiferous Epithelium - cytology - drug effects - metabolism-
dc.titleC-Yes regulates cell adhesion at the blood-testis barrier and the apical ectoplasmic specialization in the seminiferous epithelium of rat testesen_HK
dc.typeArticleen_HK
dc.identifier.emailLee, WM: hrszlwm@hku.hken_HK
dc.identifier.authorityLee, WM=rp00728en_HK
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1016/j.biocel.2011.01.008en_HK
dc.identifier.pmid21256972-
dc.identifier.pmcidPMC3047590-
dc.identifier.scopuseid_2-s2.0-79952100337en_HK
dc.identifier.hkuros194359en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-79952100337&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume43en_HK
dc.identifier.issue4en_HK
dc.identifier.spage651en_HK
dc.identifier.epage665en_HK
dc.identifier.isiWOS:000288736800025-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridXiao, X=40361736200en_HK
dc.identifier.scopusauthoridMruk, DD=6701823934en_HK
dc.identifier.scopusauthoridLee, WM=24799156600en_HK
dc.identifier.scopusauthoridCheng, CY=7404797787en_HK
dc.identifier.citeulike8743068-

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