File Download
  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Regulation of ectoplasmic specialization dynamics in the seminiferous epithelium by focal adhesion-associated proteins in testosterone-suppressed rat testes

TitleRegulation of ectoplasmic specialization dynamics in the seminiferous epithelium by focal adhesion-associated proteins in testosterone-suppressed rat testes
Authors
KeywordsB1-integrin
c-Src
Ectoplasmic specialization
Focal adhesion kinase
Issue Date2005
PublisherThe Endocrine Society. The Journal's web site is located at http://endo.endojournals.org
Citation
Endocrinology, 2005, v. 146 n. 3, p. 1192-1204 How to Cite?
AbstractApical ectoplasmic specialization (ES) is a unique testis-specific cell-cell actin-based adherens junction type restricted to the Sertoli-round/elongating/elongate spermatid interface in the seminiferous epithelium. An endogenous testosterone (T) suppression model was used to study the regulation of apical ES dynamics in the testis. By providing sustained releases of T and estradiol using subdermal implants in rats, this treatment reduced endogenous testicular T level. This in turn led to sloughing of spermatids (step 8 and beyond) from the seminiferous epithelium, which can be reversed by removing the implants, or replacing them with a higher dose of T implants. This model thus allows us to study the restructuring events at the apical ES. It was shown that apical ES restructuring involved proteins that were usually restricted to the cell-matrix focal adhesion site in other epithelia. For instance, the protein levels of β1-integrin, Tyr-phosphorylated focal adhesion kinase (p-FAK), and c-Src were induced during the T suppression-induced germ cell loss and recovery, implicating that these proteins are putative regulators of ES dynamics. Indeed, the formation of p-FAK/c-Src protein complex, but not their association with β1-integrin, was stimulated during T suppression-induced germ cell loss. ERK, a MAPK known to regulate focal adhesion turnover, was also activated during the androgen suppression-induced spermatid loss and the early phase of the recovery when germ cells began to repopulate the epithelium. Collectively, these data suggest that the apical ES is a cell-cell adherens junction type with the characteristics of cell-matrix focal contacts. In addition to its role in conferring cell adhesion formation, the p-FAK/c-Src protein complex apparently also regulates apical ES disruption via the ERK signaling pathway.
Persistent Identifierhttp://hdl.handle.net/10722/48687
ISSN
2015 Impact Factor: 4.159
2015 SCImago Journal Rankings: 2.363
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWong, CHen_HK
dc.contributor.authorXia, Wen_HK
dc.contributor.authorLee, NPYen_HK
dc.contributor.authorMruk, DDen_HK
dc.contributor.authorLee, WMen_HK
dc.contributor.authorCheng, CYen_HK
dc.date.accessioned2008-05-22T04:21:23Z-
dc.date.available2008-05-22T04:21:23Z-
dc.date.issued2005en_HK
dc.identifier.citationEndocrinology, 2005, v. 146 n. 3, p. 1192-1204en_HK
dc.identifier.issn0013-7227en_HK
dc.identifier.urihttp://hdl.handle.net/10722/48687-
dc.description.abstractApical ectoplasmic specialization (ES) is a unique testis-specific cell-cell actin-based adherens junction type restricted to the Sertoli-round/elongating/elongate spermatid interface in the seminiferous epithelium. An endogenous testosterone (T) suppression model was used to study the regulation of apical ES dynamics in the testis. By providing sustained releases of T and estradiol using subdermal implants in rats, this treatment reduced endogenous testicular T level. This in turn led to sloughing of spermatids (step 8 and beyond) from the seminiferous epithelium, which can be reversed by removing the implants, or replacing them with a higher dose of T implants. This model thus allows us to study the restructuring events at the apical ES. It was shown that apical ES restructuring involved proteins that were usually restricted to the cell-matrix focal adhesion site in other epithelia. For instance, the protein levels of β1-integrin, Tyr-phosphorylated focal adhesion kinase (p-FAK), and c-Src were induced during the T suppression-induced germ cell loss and recovery, implicating that these proteins are putative regulators of ES dynamics. Indeed, the formation of p-FAK/c-Src protein complex, but not their association with β1-integrin, was stimulated during T suppression-induced germ cell loss. ERK, a MAPK known to regulate focal adhesion turnover, was also activated during the androgen suppression-induced spermatid loss and the early phase of the recovery when germ cells began to repopulate the epithelium. Collectively, these data suggest that the apical ES is a cell-cell adherens junction type with the characteristics of cell-matrix focal contacts. In addition to its role in conferring cell adhesion formation, the p-FAK/c-Src protein complex apparently also regulates apical ES disruption via the ERK signaling pathway.en_HK
dc.format.extent1477193 bytes-
dc.format.extent2457 bytes-
dc.format.mimetypeapplication/pdf-
dc.format.mimetypetext/plain-
dc.languageengen_HK
dc.publisherThe Endocrine Society. The Journal's web site is located at http://endo.endojournals.orgen_HK
dc.relation.ispartofEndocrinologyen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.rightsEndocrinology. Copyright © The Endocrine Society.en_HK
dc.subjectB1-integrinen_HK
dc.subjectc-Srcen_HK
dc.subjectEctoplasmic specializationen_HK
dc.subjectFocal adhesion kinaseen_HK
dc.titleRegulation of ectoplasmic specialization dynamics in the seminiferous epithelium by focal adhesion-associated proteins in testosterone-suppressed rat testesen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0013-7227&volume=146&issue=3&spage=1192&epage=1204&date=2005&atitle=Regulation+of+ectoplasmic+specialization+dynamics+in+the+seminiferous+epithelium+by+focal+adhesion-associated+proteins+in+testosterone-suppressed+rat+testesen_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.naturepostprinten_HK
dc.identifier.doi10.1210/en.2004-1275en_HK
dc.identifier.pmid15591141-
dc.identifier.scopuseid_2-s2.0-14244268279en_HK
dc.identifier.hkuros98810-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-14244268279&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume146en_HK
dc.identifier.issue3en_HK
dc.identifier.spage1192en_HK
dc.identifier.epage1204en_HK
dc.identifier.isiWOS:000227035400028-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridWong, CH=8849630400en_HK
dc.identifier.scopusauthoridXia, W=8672244100en_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

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats