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Conference Paper: Transforming Growth Factor-β3-Mediated Regulation of Junctional Adhesion Molecule-B (JAM-B) in Testicular Cells

TitleTransforming Growth Factor-β3-Mediated Regulation of Junctional Adhesion Molecule-B (JAM-B) in Testicular Cells
Authors
Issue Date2012
PublisherAmerican Society for Cell Biology. The Journal's web site is located at http://www.molbiolcell.org/
Citation
The 52nd Annual Meeting of the American Society of Cell Biology (ASCB), San Francisco, California, USA, 15-19 December 2012. In Molecular Biology of the Cell, 2012, v. 23 n. Suppl., p. abstract no. 1345 How to Cite?
AbstractJunctional adhesion molecule-B (JAM-B) is found between Sertoli cells as well as between Sertoli and germ cells in the testis. The expression of JAM-B is highly regulated to facilitate the passage of developing germ cells across the blood-testis barrier as well as the release of mature spermatids. Transforming growth factor beta (TGF-β) family is implicated in the regulation of testicular cell junction dynamics during spermatogenesis. This study aims to investigate the influence of TGF-β3 on the expression of JAM-B as well as the underlying mechanisms. TGF-β3 (5 ng/ml) treatment coupled with RT-PCR and immunoblot analyses have shown that TGF-β3 down-regulates JAM-B expression on mRNA and protein levels in a timedependent manner in mouse Sertoli cell line, MSC-1 cells. Cycloheximide assay further indicates that the reduction of JAM-B protein by TGF-β3 is mediated via post-translational modification. Moreover, the involvement of ubiquitin-proteasome pathway in TGF-β3-mediated JAM-B protein destabilization was demonstrated by proteasome inhibitor, MG-132, treatment and ubiquitin siRNA knockdown assays. Furthermore, co-immunoprecipitation (Co-IP) assay has further confirmed that JAM-B protein is conjugated by a chain of ubiquitin upon TGF-β3 stimulation in the presence of MG-132. TGF-β3 also speeds up the degradation of JAM-B through Smad-dependent pathway. As knockdown of Smad3 and/or Smad4 effectively abolish TGF-β3-mediated JAM-B degradation. Taken together, the involvement of both ubiquitinproteasome pathway and Smad-dependent signalling are essential for TGF-β3-mediated JAM-B regulation in mouse Sertoli cells. [This work was supported by Hong Kong Research Grants Council (HKU772009 and HKU773710) and CRCG Seed Funding for Basic Research.]
DescriptionSession: Cell-Cell Junctions II
Poster presentation
Persistent Identifierhttp://hdl.handle.net/10722/199691
ISSN
2015 Impact Factor: 4.037
2015 SCImago Journal Rankings: 3.665

 

DC FieldValueLanguage
dc.contributor.authorZhang, Xen_US
dc.contributor.authorLui, WYen_US
dc.date.accessioned2014-07-22T01:28:11Z-
dc.date.available2014-07-22T01:28:11Z-
dc.date.issued2012en_US
dc.identifier.citationThe 52nd Annual Meeting of the American Society of Cell Biology (ASCB), San Francisco, California, USA, 15-19 December 2012. In Molecular Biology of the Cell, 2012, v. 23 n. Suppl., p. abstract no. 1345en_US
dc.identifier.issn1059-1524-
dc.identifier.urihttp://hdl.handle.net/10722/199691-
dc.descriptionSession: Cell-Cell Junctions II-
dc.descriptionPoster presentation-
dc.description.abstractJunctional adhesion molecule-B (JAM-B) is found between Sertoli cells as well as between Sertoli and germ cells in the testis. The expression of JAM-B is highly regulated to facilitate the passage of developing germ cells across the blood-testis barrier as well as the release of mature spermatids. Transforming growth factor beta (TGF-β) family is implicated in the regulation of testicular cell junction dynamics during spermatogenesis. This study aims to investigate the influence of TGF-β3 on the expression of JAM-B as well as the underlying mechanisms. TGF-β3 (5 ng/ml) treatment coupled with RT-PCR and immunoblot analyses have shown that TGF-β3 down-regulates JAM-B expression on mRNA and protein levels in a timedependent manner in mouse Sertoli cell line, MSC-1 cells. Cycloheximide assay further indicates that the reduction of JAM-B protein by TGF-β3 is mediated via post-translational modification. Moreover, the involvement of ubiquitin-proteasome pathway in TGF-β3-mediated JAM-B protein destabilization was demonstrated by proteasome inhibitor, MG-132, treatment and ubiquitin siRNA knockdown assays. Furthermore, co-immunoprecipitation (Co-IP) assay has further confirmed that JAM-B protein is conjugated by a chain of ubiquitin upon TGF-β3 stimulation in the presence of MG-132. TGF-β3 also speeds up the degradation of JAM-B through Smad-dependent pathway. As knockdown of Smad3 and/or Smad4 effectively abolish TGF-β3-mediated JAM-B degradation. Taken together, the involvement of both ubiquitinproteasome pathway and Smad-dependent signalling are essential for TGF-β3-mediated JAM-B regulation in mouse Sertoli cells. [This work was supported by Hong Kong Research Grants Council (HKU772009 and HKU773710) and CRCG Seed Funding for Basic Research.]-
dc.languageengen_US
dc.publisherAmerican Society for Cell Biology. The Journal's web site is located at http://www.molbiolcell.org/-
dc.relation.ispartofMolecular Biology of the Cellen_US
dc.rightsMolecular Biology of the Cell. Copyright © American Society for Cell Biology.-
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.titleTransforming Growth Factor-β3-Mediated Regulation of Junctional Adhesion Molecule-B (JAM-B) in Testicular Cellsen_US
dc.typeConference_Paperen_US
dc.identifier.emailLui, WY: wylui@hku.hken_US
dc.identifier.authorityLui, WY=rp00756en_US
dc.description.naturepublished_or_final_version-
dc.identifier.hkuros231858en_US
dc.identifier.volume23-
dc.identifier.issueSuppl.-
dc.identifier.spageabstract no. 1345-
dc.identifier.epageabstract no. 1345-
dc.publisher.placeUnited States-

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