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Article: Regulation of blood-testis barrier dynamics by desmosome, gap junction, hemidesmosome and polarity protein: an unexpected turn of events

TitleRegulation of blood-testis barrier dynamics by desmosome, gap junction, hemidesmosome and polarity protein: an unexpected turn of events
Authors
KeywordsTestis
Spermatogenesis
Seminiferous epithelial cycle
Blood-testis barrier
Sertoli cell
Issue Date2011
PublisherLandes Bioscience. The Journal's web site is located at http://www.landesbioscience.com/journals/spermatogenesis/
Citation
Spermatogenesis, 2011, v. 1 n. 2, p. 105-115 How to Cite?
AbstractThe blood-testis barrier (BTB) is a unique ultrastructure in the mammalian testis. Unlike other blood-tissue barriers, such as the blood-brain barrier and the blood-ocular (or blood-retina) barrier which formed by tight junctions (TJ) between endothelial cells of the microvessels, the BTB is constituted by coexisting TJ, basal ectoplasmic specialization (basal ES), desmosomes and gap junctions between adjacent Sertoli cells near the basement membrane of the seminiferous tubule. The BTB also divides the seminiferous epithelium into the apical (or adluminal) and basal compartments so that meiosis I and II and post-meiotic germ cell development can all take place in a specialized microenvironment in the apical compartment behind the BTB. While the unusual anatomical features of the BTB have been known for decades, the physiological function of the coexisting junctions, in particular the desmosome and gap junction, that constitute the BTB was unknown until recently. Based on recently published findings, we critically evaluate the role of the desmosome and gap junction that serve as a signaling platform to coordinate the 'opening' and 'closing' of the TJ-permeability barrier conferred by TJ and basal ES during the seminiferous epithelial cycle of spermatogenesis. This is made possible by polarity proteins working in concert with nonreceptor protein tyrosine kinases, such as focal adhesion kinase (FAK) and c-Src, at the site to regulate endosome-mediated protein trafficking events (e.g., endocytosis, transcytosis, recycling or protein degradation). These events not only serve to destabilize the existing 'old' BTB above preleptotene spermatocytes in transit in 'clones' at the BTB, but also contribute to the assembly of 'new' BTB below the transiting spermatocytes. Furthermore, hemidesmosomes at the Sertoli cell-basement membrane interface also contribute to the BTB restructuring events at stage VIII of the epithelial cycle. Additionally, the findings that a gap junction at the BTB provides a possible route for the passage of toxicants [e.g., bisphenol A (BPA)] and potential male contraceptives (e.g., adjudin) across the BTB also illustrate that these coexisting junctions, while helpful to maintain the immunological barrier integrity during the transit of spermatocytes, can be the 'gateway' to making the BTB so vulnerable to toxicants and/or chemicals, causing male reproductive dysfunction.
Persistent Identifierhttp://hdl.handle.net/10722/138079
ISSN
PubMed Central ID

 

DC FieldValueLanguage
dc.contributor.authorCheng, CYen_US
dc.contributor.authorWong, EWPen_US
dc.contributor.authorLie, PYPen_US
dc.contributor.authorLi, MWMen_US
dc.contributor.authorMruk, DDen_US
dc.contributor.authorYan, HHNen_US
dc.contributor.authorMok, KWen_US
dc.contributor.authorMannu, Jen_US
dc.contributor.authorMathur, PPen_US
dc.contributor.authorLui, WYen_US
dc.contributor.authorLee, WWMen_US
dc.contributor.authorBonanomi, Men_US
dc.contributor.authorSilvestrini, Ben_US
dc.date.accessioned2011-08-26T14:39:43Z-
dc.date.available2011-08-26T14:39:43Z-
dc.date.issued2011en_US
dc.identifier.citationSpermatogenesis, 2011, v. 1 n. 2, p. 105-115en_US
dc.identifier.issn2156-5554-
dc.identifier.urihttp://hdl.handle.net/10722/138079-
dc.description.abstractThe blood-testis barrier (BTB) is a unique ultrastructure in the mammalian testis. Unlike other blood-tissue barriers, such as the blood-brain barrier and the blood-ocular (or blood-retina) barrier which formed by tight junctions (TJ) between endothelial cells of the microvessels, the BTB is constituted by coexisting TJ, basal ectoplasmic specialization (basal ES), desmosomes and gap junctions between adjacent Sertoli cells near the basement membrane of the seminiferous tubule. The BTB also divides the seminiferous epithelium into the apical (or adluminal) and basal compartments so that meiosis I and II and post-meiotic germ cell development can all take place in a specialized microenvironment in the apical compartment behind the BTB. While the unusual anatomical features of the BTB have been known for decades, the physiological function of the coexisting junctions, in particular the desmosome and gap junction, that constitute the BTB was unknown until recently. Based on recently published findings, we critically evaluate the role of the desmosome and gap junction that serve as a signaling platform to coordinate the 'opening' and 'closing' of the TJ-permeability barrier conferred by TJ and basal ES during the seminiferous epithelial cycle of spermatogenesis. This is made possible by polarity proteins working in concert with nonreceptor protein tyrosine kinases, such as focal adhesion kinase (FAK) and c-Src, at the site to regulate endosome-mediated protein trafficking events (e.g., endocytosis, transcytosis, recycling or protein degradation). These events not only serve to destabilize the existing 'old' BTB above preleptotene spermatocytes in transit in 'clones' at the BTB, but also contribute to the assembly of 'new' BTB below the transiting spermatocytes. Furthermore, hemidesmosomes at the Sertoli cell-basement membrane interface also contribute to the BTB restructuring events at stage VIII of the epithelial cycle. Additionally, the findings that a gap junction at the BTB provides a possible route for the passage of toxicants [e.g., bisphenol A (BPA)] and potential male contraceptives (e.g., adjudin) across the BTB also illustrate that these coexisting junctions, while helpful to maintain the immunological barrier integrity during the transit of spermatocytes, can be the 'gateway' to making the BTB so vulnerable to toxicants and/or chemicals, causing male reproductive dysfunction.-
dc.languageengen_US
dc.publisherLandes Bioscience. The Journal's web site is located at http://www.landesbioscience.com/journals/spermatogenesis/-
dc.relation.ispartofSpermatogenesisen_US
dc.subjectTestis-
dc.subjectSpermatogenesis-
dc.subjectSeminiferous epithelial cycle-
dc.subjectBlood-testis barrier-
dc.subjectSertoli cell-
dc.titleRegulation of blood-testis barrier dynamics by desmosome, gap junction, hemidesmosome and polarity protein: an unexpected turn of eventsen_US
dc.typeArticleen_US
dc.identifier.emailWong, EWP: ewong1@hku.hken_US
dc.identifier.emailYan, HHN: helenyan@graduate.hku.hken_US
dc.identifier.emailLui, WY: wylui@hku.hken_US
dc.identifier.emailLee, WWM: hrszlwm@hku.hken_US
dc.identifier.authorityLui, WY=rp00756en_US
dc.identifier.authorityLee, WWM=rp00728en_US
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.4161/spmg.1.2.15745-
dc.identifier.pmid22319658-
dc.identifier.pmcidPMC3271652-
dc.identifier.hkuros191903en_US
dc.identifier.volume1en_US
dc.identifier.issue2en_US
dc.identifier.spage105en_US
dc.identifier.epage115en_US
dc.publisher.placeUnited States-

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