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Article: Tumor necrosis factor α reversibly disrupts the blood-testis barrier and impairs Sertoli-germ cell adhesion in the seminiferous epithelium of adult rat testes

TitleTumor necrosis factor α reversibly disrupts the blood-testis barrier and impairs Sertoli-germ cell adhesion in the seminiferous epithelium of adult rat testes
Authors
Issue Date2006
PublisherSociety for Endocrinology. The Journal's web site is located at http://joe.endocrinology-journals.org
Citation
Journal Of Endocrinology, 2006, v. 190 n. 2, p. 313-329 How to Cite?
AbstractThe timely restructuring of the blood-testis barrier (BTB) that facilitates the migration of preleptotene and leptotene spermatocytes from the basal to the adluminal compartment in the seminiferous epithelium of adult rat testes, which occurs at late stage VII through early stage VIII of the epithelial cycle, is a crucial cellular event of spermatogenesis. However, the regulation of BTB dynamics at the biochemical level remains elusive. In this study, tumor necrosis factor α (TNFα), a secretory product of Sertoh and germ cells in rat testes, was shown to affect junction dynamics in vivo. Following an acute administration of recombinant TNFα directly to adult rat testes in vivo at 0·5 and 2 μg/testis (with a body weight ∼300 g), this treatment significantly and transiently disrupted the BTB. It also transiently inhibited the steady-state protein levels of occludin, zonula occludens-1, and N-cadherin, but not junction adhesion molecule-A, α-, and β-catenin in testes at the BTB site as illustrated by immunoblottings, immunohistochemistry, electron microscopy, and fluorescent microscopy. This transient disruption of the BTB integrity induced by TNFα treatment was further demonstrated by a functional test to assess the passage of a fluorescent dye (e.g. fluorescein-5-isothiocyanate) from the systemic circulation to the adluminal compartment. Additionally, both the phosphorylated-Ser/Thr protein kinase activated by MAP kinase kinase (p-p38) and phosphorylated-externally regulated kinase (p-ERK) mitogen -activated protein kinase-signaling pathways were transiently activated. Collectively, these data coupled with the recently published in vitro studies have illustrated that the BTB is likely utilizing a novel mechanism in which localized production of TNFα by Sertoli and germ cells into the microenvironment at the basal compartment facilitates the timely restructuring ('opening'?) of the BTB during spermatogenesis to facilitate germ cell migration. © 2006 Society for Endocrinology.
Persistent Identifierhttp://hdl.handle.net/10722/88604
ISSN
2015 Impact Factor: 4.498
2015 SCImago Journal Rankings: 1.910
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLi, MWMen_HK
dc.contributor.authorXia, Wen_HK
dc.contributor.authorMruk, DDen_HK
dc.contributor.authorWang, CQFen_HK
dc.contributor.authorYan, HHNen_HK
dc.contributor.authorSiu, MKYen_HK
dc.contributor.authorLui, WYen_HK
dc.contributor.authorLee, WMen_HK
dc.contributor.authorCheng, CYen_HK
dc.date.accessioned2010-09-06T09:45:34Z-
dc.date.available2010-09-06T09:45:34Z-
dc.date.issued2006en_HK
dc.identifier.citationJournal Of Endocrinology, 2006, v. 190 n. 2, p. 313-329en_HK
dc.identifier.issn0022-0795en_HK
dc.identifier.urihttp://hdl.handle.net/10722/88604-
dc.description.abstractThe timely restructuring of the blood-testis barrier (BTB) that facilitates the migration of preleptotene and leptotene spermatocytes from the basal to the adluminal compartment in the seminiferous epithelium of adult rat testes, which occurs at late stage VII through early stage VIII of the epithelial cycle, is a crucial cellular event of spermatogenesis. However, the regulation of BTB dynamics at the biochemical level remains elusive. In this study, tumor necrosis factor α (TNFα), a secretory product of Sertoh and germ cells in rat testes, was shown to affect junction dynamics in vivo. Following an acute administration of recombinant TNFα directly to adult rat testes in vivo at 0·5 and 2 μg/testis (with a body weight ∼300 g), this treatment significantly and transiently disrupted the BTB. It also transiently inhibited the steady-state protein levels of occludin, zonula occludens-1, and N-cadherin, but not junction adhesion molecule-A, α-, and β-catenin in testes at the BTB site as illustrated by immunoblottings, immunohistochemistry, electron microscopy, and fluorescent microscopy. This transient disruption of the BTB integrity induced by TNFα treatment was further demonstrated by a functional test to assess the passage of a fluorescent dye (e.g. fluorescein-5-isothiocyanate) from the systemic circulation to the adluminal compartment. Additionally, both the phosphorylated-Ser/Thr protein kinase activated by MAP kinase kinase (p-p38) and phosphorylated-externally regulated kinase (p-ERK) mitogen -activated protein kinase-signaling pathways were transiently activated. Collectively, these data coupled with the recently published in vitro studies have illustrated that the BTB is likely utilizing a novel mechanism in which localized production of TNFα by Sertoli and germ cells into the microenvironment at the basal compartment facilitates the timely restructuring ('opening'?) of the BTB during spermatogenesis to facilitate germ cell migration. © 2006 Society for Endocrinology.en_HK
dc.languageengen_HK
dc.publisherSociety for Endocrinology. The Journal's web site is located at http://joe.endocrinology-journals.orgen_HK
dc.relation.ispartofJournal of Endocrinologyen_HK
dc.rightsJournal of Endocrinology. Copyright © Society for Endocrinology.en_HK
dc.titleTumor necrosis factor α reversibly disrupts the blood-testis barrier and impairs Sertoli-germ cell adhesion in the seminiferous epithelium of adult rat testesen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0022-0795&volume=190&issue=2&spage=313&epage=329&date=2006&atitle=Tumor+necrosis+factor-alpha+reversibly+disrupts+the+blood-testis+barrier+and+impairs+Sertoli-germ+cell+adhesion+in+the+seminiferous+epithelium+of+adult+rat+testesen_HK
dc.identifier.emailSiu, MKY: mkysiu@hkucc.hku.hken_HK
dc.identifier.emailLui, WY: wylui@hku.hken_HK
dc.identifier.emailLee, WM: hrszlwm@hku.hken_HK
dc.identifier.authoritySiu, MKY=rp00275en_HK
dc.identifier.authorityLui, WY=rp00756en_HK
dc.identifier.authorityLee, WM=rp00728en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1677/joe.1.06781en_HK
dc.identifier.pmid16899565-
dc.identifier.scopuseid_2-s2.0-33747881517en_HK
dc.identifier.hkuros118911en_HK
dc.identifier.hkuros149049-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33747881517&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume190en_HK
dc.identifier.issue2en_HK
dc.identifier.spage313en_HK
dc.identifier.epage329en_HK
dc.identifier.isiWOS:000240020500012-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridLi, MWM=27168276300en_HK
dc.identifier.scopusauthoridXia, W=8672244100en_HK
dc.identifier.scopusauthoridMruk, DD=6701823934en_HK
dc.identifier.scopusauthoridWang, CQF=14319463500en_HK
dc.identifier.scopusauthoridYan, HHN=14018807300en_HK
dc.identifier.scopusauthoridSiu, MKY=24924018400en_HK
dc.identifier.scopusauthoridLui, WY=35220192400en_HK
dc.identifier.scopusauthoridLee, WM=24799156600en_HK
dc.identifier.scopusauthoridCheng, CY=7404797787en_HK

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