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Article: Testin secreted by Sertoli cells is associated with the cell surface, and its expression correlates with the disruption of Sertoli-germ cell junctions but not the inter-Sertoli tight junction

TitleTestin secreted by Sertoli cells is associated with the cell surface, and its expression correlates with the disruption of Sertoli-germ cell junctions but not the inter-Sertoli tight junction
Authors
Issue Date1998
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal of Biological Chemistry, 1998, v. 273 n. 33, p. 21040-21053 How to Cite?
AbstractTestin is a testosterone-responsive Sertoli cell secretory product. In the present study, we demonstrated that the amount of testin secreted by Sertoli cells in vitro was comparable with several other Sertoli cell secretory products. However, virtually no testin was found in the luminal fluid and cytosols of the testis and epididymis when the intercellular junctions were not previously disrupted, suggesting that secreted testin may be reabsorbed by testicular cells in vivo. Studies using Sertoli cells with and without a cell surface cross-linker and radioiodination in conjunction with immunoprecipitation illustrated the presence of two polypeptides of 28 and 45 kDa, which constitute a binding protein complex that anchors testin onto the cell surface. The 28- and 45-kDa peptide appear to be residing on and inside the cell surface, respectively. Immunogold EM studies illustrated testin was abundantly localized on the Sertoli cell side of the ectoplasmic specialization (a modified adherens junction) surrounding developing spermatids. In contrast, very few testin gold particles were found at the site of inter-Sertoli tight junctions. When the inter-Sertoli tight junctions were formed or disrupted, no significant change in testin expression was noted. This is in sharp contrast to the disruption of Sertoli-germ cell junctions, which is accompanied by a surge in testin expression. These results demonstrate the usefulness of testin in examining Sertoli-germ cell interactions.
Persistent Identifierhttp://hdl.handle.net/10722/49355
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorGrima, Jen_HK
dc.contributor.authorWong, CSen_HK
dc.contributor.authorZhu, LJen_HK
dc.contributor.authorZong, SDen_HK
dc.contributor.authorCheng, CYen_HK
dc.date.accessioned2008-06-12T06:40:13Z-
dc.date.available2008-06-12T06:40:13Z-
dc.date.issued1998en_HK
dc.identifier.citationJournal of Biological Chemistry, 1998, v. 273 n. 33, p. 21040-21053en_HK
dc.identifier.issn0021-9258en_HK
dc.identifier.urihttp://hdl.handle.net/10722/49355-
dc.description.abstractTestin is a testosterone-responsive Sertoli cell secretory product. In the present study, we demonstrated that the amount of testin secreted by Sertoli cells in vitro was comparable with several other Sertoli cell secretory products. However, virtually no testin was found in the luminal fluid and cytosols of the testis and epididymis when the intercellular junctions were not previously disrupted, suggesting that secreted testin may be reabsorbed by testicular cells in vivo. Studies using Sertoli cells with and without a cell surface cross-linker and radioiodination in conjunction with immunoprecipitation illustrated the presence of two polypeptides of 28 and 45 kDa, which constitute a binding protein complex that anchors testin onto the cell surface. The 28- and 45-kDa peptide appear to be residing on and inside the cell surface, respectively. Immunogold EM studies illustrated testin was abundantly localized on the Sertoli cell side of the ectoplasmic specialization (a modified adherens junction) surrounding developing spermatids. In contrast, very few testin gold particles were found at the site of inter-Sertoli tight junctions. When the inter-Sertoli tight junctions were formed or disrupted, no significant change in testin expression was noted. This is in sharp contrast to the disruption of Sertoli-germ cell junctions, which is accompanied by a surge in testin expression. These results demonstrate the usefulness of testin in examining Sertoli-germ cell interactions.en_HK
dc.format.extent418 bytes-
dc.format.mimetypetext/html-
dc.languageengen_HK
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.rightsJournal of Biological Chemistry. Copyright © American Society for Biochemistry and Molecular Biology, Inc.en_HK
dc.subject.meshMembrane Proteins - secretionen_HK
dc.subject.meshProteins - genetics - immunology - metabolism - secretionen_HK
dc.subject.meshSertoli Cells - secretion - ultrastructureen_HK
dc.subject.meshTight Junctions - metabolismen_HK
dc.subject.meshAging - metabolismen_HK
dc.titleTestin secreted by Sertoli cells is associated with the cell surface, and its expression correlates with the disruption of Sertoli-germ cell junctions but not the inter-Sertoli tight junctionen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0021-9258&volume=273&issue=33&spage=21040&epage=21053&date=1998&atitle=Testin+secreted+by+Sertoli+cells+is+associated+with+the+cell+surface,+and+its+expression+correlates+with+the+disruption+of+Sertoli-germ+cell+junctions+but+not+the+inter-Sertoli+tight+junctionen_HK
dc.identifier.emailWong, CS: ccswong@HKUCC.hku.hken_HK
dc.description.naturepublished_or_final_versionen_HK
dc.identifier.doi10.1074/jbc.273.33.21040-
dc.identifier.pmid9694856en_HK
dc.identifier.scopuseid_2-s2.0-0032516869-
dc.identifier.hkuros34158-
dc.identifier.isiWOS:000075386100049-

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