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Article: Coxsackie and adenovirus receptor (CAR) is a product of Sertoli and germ cells in rat testes which is localized at the Sertoli-Sertoli and Sertoli-germ cell interface

TitleCoxsackie and adenovirus receptor (CAR) is a product of Sertoli and germ cells in rat testes which is localized at the Sertoli-Sertoli and Sertoli-germ cell interface
Authors
KeywordsTestis; Spermatogenesis
Sertoli-germ cell interaction
Blood–testis barri
Tight junction
Adherens junction
Issue Date2007
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yexcr
Citation
Experimental Cell Research, 2007, v. 313 n. 7, p. 1373-1392 How to Cite?
AbstractThe coxsackie and adenovirus receptor (CAR), a putative cell-cell adhesion molecule, has attracted wide interest due to its importance in viral pathogenesis and in mediating adenoviral gene delivery. However, the distribution pattern and physiological function of CAR in the testis is still not clear. Here, we identified CAR in Sertoli cells and germ cells of rats. In vivo studies have shown that CAR resides at the blood-testis barrier as well as at the ectoplasmic specialization. The persistent expression of CAR in rat testes from neonatal period throughout adulthood implicates its role in spermatogenesis. Using primary Sertoli cell cultures, we observed a significant induction of CAR during the formation of Sertoli cell epithelium. Furthermore, CAR was seen to be concentrated at inter-Sertoli cell junctions, co-localizing with tight junction protein marker ZO-1 and adherens junction protein N-cadherin. CAR was also found to be associated with proteins of Src kinase family and its protein level declined after TNFalpha treatment in Sertoli cell cultures. Immunofluorescent staining of isolated germ cells has revealed the presence of CAR on spermatogonia, spermatocytes, round spermatids and elongate spermatids. Taken together, we propose that CAR functions as an adhesion molecule in maintaining the inter-Sertoli cell junctions at the basal compartment of the seminiferous epithelium. In addition, CAR may confer adhesion between Sertoli and germ cells at the Sertoli-germ cell interface. It is possible that the receptor utilized by viral pathogens to breakthrough the epithelial barrier was also employed by developing germ cells to migrate through the inter-Sertoli cell junctions.
Persistent Identifierhttp://hdl.handle.net/10722/48723
ISSN
2015 Impact Factor: 3.378
2015 SCImago Journal Rankings: 1.900
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorWang, CQFen_HK
dc.contributor.authorMruk, DDen_HK
dc.contributor.authorLee, WWMen_HK
dc.contributor.authorCheng, CYen_HK
dc.date.accessioned2008-05-22T04:22:26Z-
dc.date.available2008-05-22T04:22:26Z-
dc.date.issued2007en_HK
dc.identifier.citationExperimental Cell Research, 2007, v. 313 n. 7, p. 1373-1392en_HK
dc.identifier.issn0014-4827en_HK
dc.identifier.urihttp://hdl.handle.net/10722/48723-
dc.description.abstractThe coxsackie and adenovirus receptor (CAR), a putative cell-cell adhesion molecule, has attracted wide interest due to its importance in viral pathogenesis and in mediating adenoviral gene delivery. However, the distribution pattern and physiological function of CAR in the testis is still not clear. Here, we identified CAR in Sertoli cells and germ cells of rats. In vivo studies have shown that CAR resides at the blood-testis barrier as well as at the ectoplasmic specialization. The persistent expression of CAR in rat testes from neonatal period throughout adulthood implicates its role in spermatogenesis. Using primary Sertoli cell cultures, we observed a significant induction of CAR during the formation of Sertoli cell epithelium. Furthermore, CAR was seen to be concentrated at inter-Sertoli cell junctions, co-localizing with tight junction protein marker ZO-1 and adherens junction protein N-cadherin. CAR was also found to be associated with proteins of Src kinase family and its protein level declined after TNFalpha treatment in Sertoli cell cultures. Immunofluorescent staining of isolated germ cells has revealed the presence of CAR on spermatogonia, spermatocytes, round spermatids and elongate spermatids. Taken together, we propose that CAR functions as an adhesion molecule in maintaining the inter-Sertoli cell junctions at the basal compartment of the seminiferous epithelium. In addition, CAR may confer adhesion between Sertoli and germ cells at the Sertoli-germ cell interface. It is possible that the receptor utilized by viral pathogens to breakthrough the epithelial barrier was also employed by developing germ cells to migrate through the inter-Sertoli cell junctions.en_HK
dc.format.extent3452315 bytes-
dc.format.extent902 bytes-
dc.format.mimetypeapplication/pdf-
dc.format.mimetypetext/plain-
dc.languageengen_HK
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yexcren_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subjectTestis; Spermatogenesisen_HK
dc.subjectSertoli-germ cell interactionen_HK
dc.subjectBlood–testis barrien_HK
dc.subjectTight junctionen_HK
dc.subjectAdherens junctionen_HK
dc.titleCoxsackie and adenovirus receptor (CAR) is a product of Sertoli and germ cells in rat testes which is localized at the Sertoli-Sertoli and Sertoli-germ cell interfaceen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0014-4827&volume=313&issue=7&spage=1373&epage=1392&date=2007&atitle=Coxsackie+and+adenovirus+receptor+(CAR)+is+a+product+of+Sertoli+and+germ+cells+in+rat+testes+which+is+localized+at+the+Sertoli-Sertoli+and+Sertoli-germ+cell+interfaceen_HK
dc.identifier.emailLee, WWM: hrszlwm@hku.hken_HK
dc.description.naturepostprinten_HK
dc.identifier.doi10.1016/j.yexcr.2007.01.017en_HK
dc.identifier.pmid17359973-
dc.identifier.pmcidPMC2095131-
dc.identifier.scopuseid_2-s2.0-33947720531-
dc.identifier.hkuros132221-
dc.identifier.isiWOS:000245681800009-
dc.identifier.scopusauthoridWang, CQF=14319463500-
dc.identifier.scopusauthoridMruk, DD=6701823934-
dc.identifier.scopusauthoridLee, WM=24799156600-
dc.identifier.scopusauthoridCheng, CY=7404797787-
dc.identifier.citeulike2521822-

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