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Article: cAMP perturbs inter-Sertoli tight junction permeability barrier in vitro via its effect on proteasome-sensitive ubiquitination of occludin

TitlecAMP perturbs inter-Sertoli tight junction permeability barrier in vitro via its effect on proteasome-sensitive ubiquitination of occludin
Authors
Issue Date2005
PublisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/31010
Citation
Journal Of Cellular Physiology, 2005, v. 203 n. 3, p. 564-572 How to Cite?
AbstractThroughout spermatogenesis, inter-Sertoli tight junctions (TJs) that constitute the blood-testis barrier must be disassembled and reassembled to permit the timely movement of preleptotene and leptotene spermatocytes from the basal to the adluminal compartment of the seminiferous epithelium. However, the mechanism and the participating molecules that regulate the bioavailability of TJ proteins are entirely unknown. Using Sertoli cell culture, it was shown that there was an increase in occludin level, concomitant with a reduction of an E3 ubiquitin ligase, Itch, at the time when inter-Sertoli TJs were assembled. By co-immunoprecipitation, occludin was shown to associate with Itch at the TJs. A novel interaction between Itch and UBC4 (an ubiquitin-conjugating enzyme) was identified. When TJs were disrupted by dibutyryl-cAMP (db-cAMP), an increase in protein levels of Itch and UBC4 along with a significant reduction in endogenous occludin was detected. These results seemingly suggest that the interaction of Itch and UBC4on occludin is potentially involved in regulating Sertoli TJ dynamics. Addition of a proteasome inhibitor, MG-132, into Sertoli cells cultured with db-cAMP blocked the db-cAMP-induced occludin loss in vitro. Accumulations of ubiquitin-conjugated and Itch-conjugated occludin were detected in Sertoli cells cultured in the presence of both MG-132 and db-cAMP. These results suggest that MG-132 prevented db-cAMP-induced TJ disruption by altering the rate of occludin degradation. Taken collectively, the results reported herein support the notion that db-cAMP-induced TJ disruption was mediated by an induction of Itch protein expression, which in turn triggered the ubiquitination of occludin resulting in TJ disruption. © 2004 Wiley-Liss, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/84852
ISSN
2015 Impact Factor: 4.155
2015 SCImago Journal Rankings: 1.842
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWing, YLen_HK
dc.contributor.authorLee, WMen_HK
dc.date.accessioned2010-09-06T08:57:52Z-
dc.date.available2010-09-06T08:57:52Z-
dc.date.issued2005en_HK
dc.identifier.citationJournal Of Cellular Physiology, 2005, v. 203 n. 3, p. 564-572en_HK
dc.identifier.issn0021-9541en_HK
dc.identifier.urihttp://hdl.handle.net/10722/84852-
dc.description.abstractThroughout spermatogenesis, inter-Sertoli tight junctions (TJs) that constitute the blood-testis barrier must be disassembled and reassembled to permit the timely movement of preleptotene and leptotene spermatocytes from the basal to the adluminal compartment of the seminiferous epithelium. However, the mechanism and the participating molecules that regulate the bioavailability of TJ proteins are entirely unknown. Using Sertoli cell culture, it was shown that there was an increase in occludin level, concomitant with a reduction of an E3 ubiquitin ligase, Itch, at the time when inter-Sertoli TJs were assembled. By co-immunoprecipitation, occludin was shown to associate with Itch at the TJs. A novel interaction between Itch and UBC4 (an ubiquitin-conjugating enzyme) was identified. When TJs were disrupted by dibutyryl-cAMP (db-cAMP), an increase in protein levels of Itch and UBC4 along with a significant reduction in endogenous occludin was detected. These results seemingly suggest that the interaction of Itch and UBC4on occludin is potentially involved in regulating Sertoli TJ dynamics. Addition of a proteasome inhibitor, MG-132, into Sertoli cells cultured with db-cAMP blocked the db-cAMP-induced occludin loss in vitro. Accumulations of ubiquitin-conjugated and Itch-conjugated occludin were detected in Sertoli cells cultured in the presence of both MG-132 and db-cAMP. These results suggest that MG-132 prevented db-cAMP-induced TJ disruption by altering the rate of occludin degradation. Taken collectively, the results reported herein support the notion that db-cAMP-induced TJ disruption was mediated by an induction of Itch protein expression, which in turn triggered the ubiquitination of occludin resulting in TJ disruption. © 2004 Wiley-Liss, Inc.en_HK
dc.languageengen_HK
dc.publisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/31010en_HK
dc.relation.ispartofJournal of Cellular Physiologyen_HK
dc.rightsJournal of Cellular Physiology. Copyright © John Wiley & Sons, Inc.en_HK
dc.titlecAMP perturbs inter-Sertoli tight junction permeability barrier in vitro via its effect on proteasome-sensitive ubiquitination of occludinen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0021-9541&volume=203&spage=564&epage=572&date=2005&atitle=cAMP+Perturbs+Inter-Sertoli+Tight+Junction+Permeability+Barrier+In+Vitro+via+its+Effect+on+Proteasome-Sensitive++Ubiquitination+of+Occludinen_HK
dc.identifier.emailLee, WM: hrszlwm@hku.hken_HK
dc.identifier.authorityLee, WM=rp00728en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1002/jcp.20254en_HK
dc.identifier.pmid15605377-
dc.identifier.scopuseid_2-s2.0-18244375541en_HK
dc.identifier.hkuros98890en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-18244375541&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume203en_HK
dc.identifier.issue3en_HK
dc.identifier.spage564en_HK
dc.identifier.epage572en_HK
dc.identifier.isiWOS:000228877600014-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridWing, YL=7004821188en_HK
dc.identifier.scopusauthoridLee, WM=24799156600en_HK

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