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Article: An Occludin-focal Adhesion Kinase Protein Complex At The Blood-testis Barrier: A Study Using The Cadmium Model

TitleAn Occludin-focal Adhesion Kinase Protein Complex At The Blood-testis Barrier: A Study Using The Cadmium Model
Authors
Issue Date2009
PublisherThe Endocrine Society. The Journal's web site is located at http://endo.endojournals.org
Citation
Endocrinology, 2009, v. 150 n. 7, p. 3336-3344 How to Cite?
AbstractSeveral integral membrane proteins that constitute the blood-testis barrier (BTB) in mammalian testes, in particular rodents, are known to date. These include tight junction (TJ) proteins (e.g. occludin, junctional adhesion molecule-A, claudins), basal ectoplasmic specialization proteins (e.g. N-cadherin), and gap junction proteins (e.g. connexin43). However, the regulators (e.g. protein kinases and phosphatases) that affect these proteins, such as their interaction with the cytoskeletal actin, which in turn confer cell adhesion at the TJ, remain largely unknown. We report herein that focal adhesion kinase (FAK) is a putative interacting partner of occludin, but not claudin-11 or junctional adhesion molecule-A. Immunohistochemistry and fluorescence microscopy studies illustrated that the expression of FAK in the seminiferous epithelium of adult rat testes was stage specific. FAK colocalized with occludin at the BTB in virtually all stages of the seminiferous epithelial cycle but considerably diminished in stages VIII-IX, at the time of BTB restructuring to facilitate the transit of primary leptotene spermatocytes. Using Sertoli cells cultured in vitro with established TJ-permeability barrier and ultrastructures of TJ, basal ectoplasmic specialization and desmosome-like junction that mimicked the BTB in vivo, FAK was shown to colocalize with occludin and zonula occludens-1 (ZO-1) at the Sertoli-Sertoli cell interface. When these Sertoli cell cultures were treated with CdCl(2) to perturb the TJ-barrier function, occludin underwent endocytic-mediated internalization in parallel with FAK and ZO-1. Thus, these findings demonstrate that FAK is an integrated regulatory component of the occludin-ZO-1 protein complex, suggesting that functional studies can be performed to study the role of FAK in BTB dynamics.
Persistent Identifierhttp://hdl.handle.net/10722/205861
ISSN
2015 Impact Factor: 4.159
2015 SCImago Journal Rankings: 2.363
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorSiu, ER-
dc.contributor.authorWong, EWP-
dc.contributor.authorMruk, DD-
dc.contributor.authorSze, KL-
dc.contributor.authorPorto, CS-
dc.contributor.authorCheng, CY-
dc.date.accessioned2014-10-17T00:56:05Z-
dc.date.available2014-10-17T00:56:05Z-
dc.date.issued2009-
dc.identifier.citationEndocrinology, 2009, v. 150 n. 7, p. 3336-3344-
dc.identifier.issn0013-7227-
dc.identifier.urihttp://hdl.handle.net/10722/205861-
dc.description.abstractSeveral integral membrane proteins that constitute the blood-testis barrier (BTB) in mammalian testes, in particular rodents, are known to date. These include tight junction (TJ) proteins (e.g. occludin, junctional adhesion molecule-A, claudins), basal ectoplasmic specialization proteins (e.g. N-cadherin), and gap junction proteins (e.g. connexin43). However, the regulators (e.g. protein kinases and phosphatases) that affect these proteins, such as their interaction with the cytoskeletal actin, which in turn confer cell adhesion at the TJ, remain largely unknown. We report herein that focal adhesion kinase (FAK) is a putative interacting partner of occludin, but not claudin-11 or junctional adhesion molecule-A. Immunohistochemistry and fluorescence microscopy studies illustrated that the expression of FAK in the seminiferous epithelium of adult rat testes was stage specific. FAK colocalized with occludin at the BTB in virtually all stages of the seminiferous epithelial cycle but considerably diminished in stages VIII-IX, at the time of BTB restructuring to facilitate the transit of primary leptotene spermatocytes. Using Sertoli cells cultured in vitro with established TJ-permeability barrier and ultrastructures of TJ, basal ectoplasmic specialization and desmosome-like junction that mimicked the BTB in vivo, FAK was shown to colocalize with occludin and zonula occludens-1 (ZO-1) at the Sertoli-Sertoli cell interface. When these Sertoli cell cultures were treated with CdCl(2) to perturb the TJ-barrier function, occludin underwent endocytic-mediated internalization in parallel with FAK and ZO-1. Thus, these findings demonstrate that FAK is an integrated regulatory component of the occludin-ZO-1 protein complex, suggesting that functional studies can be performed to study the role of FAK in BTB dynamics.-
dc.languageeng-
dc.publisherThe Endocrine Society. The Journal's web site is located at http://endo.endojournals.org-
dc.relation.ispartofEndocrinology-
dc.subject.meshBlood-Testis Barrier - drug effects - physiology-
dc.subject.meshCadmium Chloride - pharmacology-
dc.subject.meshFocal Adhesion Kinase 1 - metabolism-
dc.subject.meshMembrane Proteins - metabolism-
dc.subject.meshPermeability - drug effects-
dc.titleAn Occludin-focal Adhesion Kinase Protein Complex At The Blood-testis Barrier: A Study Using The Cadmium Modelen_US
dc.typeArticleen_US
dc.identifier.emailSze, KL: szekl@hku.hk-
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1210/en.2008-1741-
dc.identifier.pmid19213829-
dc.identifier.pmcidPMC2703538-
dc.identifier.hkuros163172-
dc.identifier.volume150-
dc.identifier.issue7-
dc.identifier.spage3336-
dc.identifier.epage3344-
dc.identifier.isiWOS:000267781300045-
dc.publisher.placeUnited States-

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