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Article: Nitric Oxide/Nitric Oxide Synthase, Spermatogenesis, and Tight Junction Dynamics

TitleNitric Oxide/Nitric Oxide Synthase, Spermatogenesis, and Tight Junction Dynamics
Authors
KeywordsCyclic adenosine monophosphate
Cyclic guanosine monophosphate
Nitric oxide
Signal transduction
Spermatogenesis
Issue Date2004
PublisherSociety for the Study of Reproduction. The Journal's web site is located at http://www.biolreprod.org/
Citation
Biology Of Reproduction, 2004, v. 70 n. 2, p. 267-276 How to Cite?
AbstractDuring spermatogenesis, preleptotene and leptotene spermatocytes, residing in the basal compartment of the seminiferous epithelium, must traverse the blood-testis barrier (BTB) to gain entry to the adluminal compartment for further development at late stage VIII and early stage IX of the epithelial cycle. As such, the timely opening and closing of the BTB is crucial to spermatogenesis. A compromise in this process can lead to infertility. Moreover, the BTB is unique in its relative localization in the seminiferous epithelium compared to the tight junctions (TJs) found in other epithelia. Sertoli cell TJs are situated near the basal lamina in the testis, closest to the basement membrane (a modified form of extracellular matrix [ECM]), unlike TJs found in other epithelia, which are found nearest the apical portion of an epithelium, farthest away from ECM. Needless to say, BTB function in the testis is maintained by intricate regulatory mechanisms. In addition to hormones and cytokines, nitric oxide (NO) was recently shown to be a putative TJ regulator in the testis. Perhaps equally important, TJ dynamics in the testis were shown to be regulated, at least in part, by occludin, a TJ -integral membrane protein, via the NO/soluble guanylate cyclase/cGMP/protein kinase G signaling pathway. This minireview summarizes recent advances in the field regarding the role of NO in testicular function, with special emphasis regarding its role in TJ dynamics and the likely implications of these studies for male contraceptive development.
Persistent Identifierhttp://hdl.handle.net/10722/143479
ISSN
2015 Impact Factor: 3.471
2015 SCImago Journal Rankings: 1.646
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLee, NPYen_HK
dc.contributor.authorCheng, CYen_HK
dc.date.accessioned2011-12-02T05:22:11Z-
dc.date.available2011-12-02T05:22:11Z-
dc.date.issued2004en_HK
dc.identifier.citationBiology Of Reproduction, 2004, v. 70 n. 2, p. 267-276en_HK
dc.identifier.issn0006-3363en_HK
dc.identifier.urihttp://hdl.handle.net/10722/143479-
dc.description.abstractDuring spermatogenesis, preleptotene and leptotene spermatocytes, residing in the basal compartment of the seminiferous epithelium, must traverse the blood-testis barrier (BTB) to gain entry to the adluminal compartment for further development at late stage VIII and early stage IX of the epithelial cycle. As such, the timely opening and closing of the BTB is crucial to spermatogenesis. A compromise in this process can lead to infertility. Moreover, the BTB is unique in its relative localization in the seminiferous epithelium compared to the tight junctions (TJs) found in other epithelia. Sertoli cell TJs are situated near the basal lamina in the testis, closest to the basement membrane (a modified form of extracellular matrix [ECM]), unlike TJs found in other epithelia, which are found nearest the apical portion of an epithelium, farthest away from ECM. Needless to say, BTB function in the testis is maintained by intricate regulatory mechanisms. In addition to hormones and cytokines, nitric oxide (NO) was recently shown to be a putative TJ regulator in the testis. Perhaps equally important, TJ dynamics in the testis were shown to be regulated, at least in part, by occludin, a TJ -integral membrane protein, via the NO/soluble guanylate cyclase/cGMP/protein kinase G signaling pathway. This minireview summarizes recent advances in the field regarding the role of NO in testicular function, with special emphasis regarding its role in TJ dynamics and the likely implications of these studies for male contraceptive development.en_HK
dc.languageengen_US
dc.publisherSociety for the Study of Reproduction. The Journal's web site is located at http://www.biolreprod.org/en_HK
dc.relation.ispartofBiology of Reproductionen_HK
dc.subjectCyclic adenosine monophosphateen_HK
dc.subjectCyclic guanosine monophosphateen_HK
dc.subjectNitric oxideen_HK
dc.subjectSignal transductionen_HK
dc.subjectSpermatogenesisen_HK
dc.subject.meshAnimalsen_US
dc.subject.meshHumansen_US
dc.subject.meshMaleen_US
dc.subject.meshNitric Oxideen_US
dc.subject.meshNitric Oxide Synthaseen_US
dc.subject.meshSpermatogenesisen_US
dc.subject.meshTight Junctionsen_US
dc.titleNitric Oxide/Nitric Oxide Synthase, Spermatogenesis, and Tight Junction Dynamicsen_HK
dc.typeArticleen_HK
dc.identifier.emailLee, NPY: nikkilee@hku.hken_HK
dc.identifier.authorityLee, NPY=rp00263en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1095/biolreprod.103.021329en_HK
dc.identifier.pmid14522829-
dc.identifier.scopuseid_2-s2.0-0742306236en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0742306236&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume70en_HK
dc.identifier.issue2en_HK
dc.identifier.spage267en_HK
dc.identifier.epage276en_HK
dc.identifier.isiWOS:000188395400001-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLee, NPY=7402722690en_HK
dc.identifier.scopusauthoridCheng, CY=7404797787en_HK

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