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Article: Differential interactions between transforming growth factor-β3/ TβR1, TAB1, and CD2AP disrupt blood-testis barrier and sertoli-germ cell adhesion
Title | Differential interactions between transforming growth factor-β3/ TβR1, TAB1, and CD2AP disrupt blood-testis barrier and sertoli-germ cell adhesion |
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Authors | |
Keywords | Biology Biochemistry |
Issue Date | 2006 |
Publisher | American Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/ |
Citation | Journal of Biological Chemistry, 2006, v. 281 n. 24, p. 16799-16813 How to Cite? |
Abstract | The biochemical basis that regulates the timely and selective opening of the blood-testis barrier (BTB) to migrating preleptotene/leptotene spermatocytes at stage VIII of the epithelial cycle in adult rat testes is virtually unknown. Recent studies have shown that cytokines (e.g. transforming growth factor (TGF)-β3) may play a crucial role in this event. However, much of this information relies on the use of toxicants (e.g. CdCl 2), making it difficult to relay these findings to normal testicular physiology. Here we report that overexpression of TGF-β3 in primary Sertoli cells cultured in vitro indeed perturbed the tight junction (TJ) barrier with a concomitant decline in the production of BTB constituent proteins as follows: occludin, N-cadherin, and ZO-1. Additionally, local administration of TGF-β3 to testes in vivo was shown to reversibly perturb the BTB integrity and Sertoli-germ cell adhesion via the p38 MAPK and ERK signaling pathways. Most importantly, the simultaneous activation of p38 and ERK signaling pathways is dependent on the association of the TGF-β3-TβR1 complex with adaptors TAB1 and CD2AP because if TβR1 was associated preferentially with CD2AP, only Sertoli-germ cell adhesion was perturbed without compromising the BTB. Collectively, these data illustrate that local production of TGF-β3, and perhaps other TGF-βs and cytokines, by Sertoli and germ cells into the microenvironment at the BTB during spermatogenesis transiently perturbs the BTB and Sertoli-germ cell adhesion to facilitate germ cell migration when the activated TβRI interacts with adaptors TAB1 and CD2AP. However, TGF-β3 selectively disrupts Sertoli-germ cell adhesion in the seminiferous epithelium to facilitate germ cell migration without compromising BTB when TβRI interacts only with adaptor CD2AP. © 2006 by The American Society for Biochemistry and Molecular Biology, Inc. |
Persistent Identifier | http://hdl.handle.net/10722/48684 |
ISSN | 2020 Impact Factor: 5.157 2023 SCImago Journal Rankings: 1.766 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
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dc.contributor.author | Xia, W | en_HK |
dc.contributor.author | Mruk, DD | en_HK |
dc.contributor.author | Lee, WM | en_HK |
dc.contributor.author | Cheng, CY | en_HK |
dc.date.accessioned | 2008-05-22T04:21:19Z | - |
dc.date.available | 2008-05-22T04:21:19Z | - |
dc.date.issued | 2006 | en_HK |
dc.identifier.citation | Journal of Biological Chemistry, 2006, v. 281 n. 24, p. 16799-16813 | en_HK |
dc.identifier.issn | 0021-9258 | en_HK |
dc.identifier.uri | http://hdl.handle.net/10722/48684 | - |
dc.description.abstract | The biochemical basis that regulates the timely and selective opening of the blood-testis barrier (BTB) to migrating preleptotene/leptotene spermatocytes at stage VIII of the epithelial cycle in adult rat testes is virtually unknown. Recent studies have shown that cytokines (e.g. transforming growth factor (TGF)-β3) may play a crucial role in this event. However, much of this information relies on the use of toxicants (e.g. CdCl 2), making it difficult to relay these findings to normal testicular physiology. Here we report that overexpression of TGF-β3 in primary Sertoli cells cultured in vitro indeed perturbed the tight junction (TJ) barrier with a concomitant decline in the production of BTB constituent proteins as follows: occludin, N-cadherin, and ZO-1. Additionally, local administration of TGF-β3 to testes in vivo was shown to reversibly perturb the BTB integrity and Sertoli-germ cell adhesion via the p38 MAPK and ERK signaling pathways. Most importantly, the simultaneous activation of p38 and ERK signaling pathways is dependent on the association of the TGF-β3-TβR1 complex with adaptors TAB1 and CD2AP because if TβR1 was associated preferentially with CD2AP, only Sertoli-germ cell adhesion was perturbed without compromising the BTB. Collectively, these data illustrate that local production of TGF-β3, and perhaps other TGF-βs and cytokines, by Sertoli and germ cells into the microenvironment at the BTB during spermatogenesis transiently perturbs the BTB and Sertoli-germ cell adhesion to facilitate germ cell migration when the activated TβRI interacts with adaptors TAB1 and CD2AP. However, TGF-β3 selectively disrupts Sertoli-germ cell adhesion in the seminiferous epithelium to facilitate germ cell migration without compromising BTB when TβRI interacts only with adaptor CD2AP. © 2006 by The American Society for Biochemistry and Molecular Biology, Inc. | en_HK |
dc.format.extent | 1291377 bytes | - |
dc.format.extent | 2457 bytes | - |
dc.format.mimetype | application/pdf | - |
dc.format.mimetype | text/plain | - |
dc.language | eng | en_HK |
dc.publisher | American Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/ | en_HK |
dc.relation.ispartof | Journal of Biological Chemistry | en_HK |
dc.rights | This research was originally published in the Journal of Biological Chemistry. Weiliang Xia, Dolores D. Mruk, Will M. Lee and C. Yan Cheng. Differential Interactions between Transforming Growth Factor-β3/TβR1, TAB1, and CD2AP Disrupt Blood-Testis Barrier and Sertoli-Germ Cell Adhesion. J Biol Chem. 2006; 281:16799-16813. © the American Society for Biochemistry and Molecular Biology. | en_HK |
dc.subject | Biology | en_HK |
dc.subject | Biochemistry | en_HK |
dc.title | Differential interactions between transforming growth factor-β3/ TβR1, TAB1, and CD2AP disrupt blood-testis barrier and sertoli-germ cell adhesion | en_HK |
dc.type | Article | en_HK |
dc.identifier.email | Lee, WM: hrszlwm@hku.hk | en_HK |
dc.identifier.authority | Lee, WM=rp00728 | en_HK |
dc.description.nature | postprint | en_HK |
dc.identifier.doi | 10.1074/jbc.M601618200 | en_HK |
dc.identifier.pmid | 16617054 | - |
dc.identifier.scopus | eid_2-s2.0-33745220527 | en_HK |
dc.identifier.hkuros | 122808 | - |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-33745220527&selection=ref&src=s&origin=recordpage | en_HK |
dc.identifier.volume | 281 | en_HK |
dc.identifier.issue | 24 | en_HK |
dc.identifier.spage | 16799 | en_HK |
dc.identifier.epage | 16813 | en_HK |
dc.identifier.isi | WOS:000238165700075 | - |
dc.publisher.place | United States | en_HK |
dc.identifier.scopusauthorid | Xia, W=8672244100 | en_HK |
dc.identifier.scopusauthorid | Mruk, DD=6701823934 | en_HK |
dc.identifier.scopusauthorid | Lee, WM=24799156600 | en_HK |
dc.identifier.scopusauthorid | Cheng, CY=7404797787 | en_HK |
dc.identifier.issnl | 0021-9258 | - |