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Conference Paper: Expression of multiple Na+/H+ exchanger isoforms in cultured epithelial cells from rat efferent duct and cauda epididymidis

TitleExpression of multiple Na+/H+ exchanger isoforms in cultured epithelial cells from rat efferent duct and cauda epididymidis
Authors
KeywordsEpididymis
Issue Date2001
PublisherSociety for the Study of Reproduction. The Journal's web site is located at http://www.biolreprod.org/
Citation
Biology Of Reproduction, 2001, v. 64 n. 2, p. 482-490 How to Cite?
AbstractAlthough earlier work has pointed to the presence of Na+/H+ exchangers (NHEs) in the rat epididymis, little is known about the regional distribution of various NHE isoforms and their functions. In the present work, expression of different isoforms of NHE in cultured epithelia of the efferent duct and cauda epdidymidis were studied. Reverse transcription-polymerase chain reaction revealed the presence of NHE1, NHE2, and NHE3, but not NHE4, message in both cultured epithelia. Western blot analysis detected the presence of NHE1 and NHE2 proteins in both cultured epithelia, but NHE3 protein was only detected in the cultured epithelial cells from the efferent duct. Immunohistochemical studies demonstrated that NHE2 was localized in the cytoplasm of the ciliated cells, whereas NHE3 was localized at the apical membrane of the principal cells of the efferent duct. The NHE activities in both cultured epithelia were inhibited by 10 μM HOE-694 (3-methylsulphonyl-4-piperidinobenzoyl guanidine methanesulphonate), a NHE1 inhibitor, by approximately 76%. The HOE-694-resistant NHE activities in the cultured epithelia of efferent duct and cauda epididymidis were completely inhibited by 20 μM S3226 (3-[2-(3-guanidino-2-methyl-3-oxo-propenyl)-5-methyl-phenyl]-N-isopropylidene -2-methyl-acrylamide dihydrochloride), a NHE3 inhibitor, and 300 μM HOE-694 (a dose that can completely block NHE2), respectively. These results indicated that NHE1, NHE2, and NHE3 were expressed in the cultured epithelial cells of the efferent duct, whereas only NHE1 and NHE2 were expressed in the cultured epithelial cells of the cauda epididymidis. It is suggested that NHE1 may provide "housekeeping" functions in both epithelia, whereas NHE2 in the cauda epididymidis and NHE3 in the efferent duct may be involved in Na+ reabsorption and regulation of pH of the luminal fluid.
Persistent Identifierhttp://hdl.handle.net/10722/173540
ISSN
2021 Impact Factor: 4.161
2020 SCImago Journal Rankings: 1.366
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLeung, GPHen_US
dc.contributor.authorTse, CMen_US
dc.contributor.authorCheng Chew, SBen_US
dc.contributor.authorWong, PYDen_US
dc.date.accessioned2012-10-30T06:32:34Z-
dc.date.available2012-10-30T06:32:34Z-
dc.date.issued2001en_US
dc.identifier.citationBiology Of Reproduction, 2001, v. 64 n. 2, p. 482-490en_US
dc.identifier.issn0006-3363en_US
dc.identifier.urihttp://hdl.handle.net/10722/173540-
dc.description.abstractAlthough earlier work has pointed to the presence of Na+/H+ exchangers (NHEs) in the rat epididymis, little is known about the regional distribution of various NHE isoforms and their functions. In the present work, expression of different isoforms of NHE in cultured epithelia of the efferent duct and cauda epdidymidis were studied. Reverse transcription-polymerase chain reaction revealed the presence of NHE1, NHE2, and NHE3, but not NHE4, message in both cultured epithelia. Western blot analysis detected the presence of NHE1 and NHE2 proteins in both cultured epithelia, but NHE3 protein was only detected in the cultured epithelial cells from the efferent duct. Immunohistochemical studies demonstrated that NHE2 was localized in the cytoplasm of the ciliated cells, whereas NHE3 was localized at the apical membrane of the principal cells of the efferent duct. The NHE activities in both cultured epithelia were inhibited by 10 μM HOE-694 (3-methylsulphonyl-4-piperidinobenzoyl guanidine methanesulphonate), a NHE1 inhibitor, by approximately 76%. The HOE-694-resistant NHE activities in the cultured epithelia of efferent duct and cauda epididymidis were completely inhibited by 20 μM S3226 (3-[2-(3-guanidino-2-methyl-3-oxo-propenyl)-5-methyl-phenyl]-N-isopropylidene -2-methyl-acrylamide dihydrochloride), a NHE3 inhibitor, and 300 μM HOE-694 (a dose that can completely block NHE2), respectively. These results indicated that NHE1, NHE2, and NHE3 were expressed in the cultured epithelial cells of the efferent duct, whereas only NHE1 and NHE2 were expressed in the cultured epithelial cells of the cauda epididymidis. It is suggested that NHE1 may provide "housekeeping" functions in both epithelia, whereas NHE2 in the cauda epididymidis and NHE3 in the efferent duct may be involved in Na+ reabsorption and regulation of pH of the luminal fluid.en_US
dc.languageengen_US
dc.publisherSociety for the Study of Reproduction. The Journal's web site is located at http://www.biolreprod.org/en_US
dc.relation.ispartofBiology of Reproductionen_US
dc.subjectEpididymis-
dc.subject.meshAmiloride - Pharmacologyen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBlotting, Westernen_US
dc.subject.meshCell Membrane - Enzymologyen_US
dc.subject.meshCells, Cultureden_US
dc.subject.meshDiuretics - Pharmacologyen_US
dc.subject.meshEpididymis - Cytology - Enzymologyen_US
dc.subject.meshEpithelial Cells - Enzymologyen_US
dc.subject.meshGuanidines - Pharmacologyen_US
dc.subject.meshImmunohistochemistryen_US
dc.subject.meshIsoenzymes - Biosynthesisen_US
dc.subject.meshMaleen_US
dc.subject.meshMethacrylates - Pharmacologyen_US
dc.subject.meshRna - Biosynthesis - Isolation & Purificationen_US
dc.subject.meshRatsen_US
dc.subject.meshRats, Sprague-Dawleyen_US
dc.subject.meshReverse Transcriptase Polymerase Chain Reactionen_US
dc.subject.meshSeminiferous Tubules - Cytology - Enzymologyen_US
dc.subject.meshSodium-Hydrogen Antiporter - Biosynthesis - Metabolismen_US
dc.subject.meshSulfones - Pharmacologyen_US
dc.titleExpression of multiple Na+/H+ exchanger isoforms in cultured epithelial cells from rat efferent duct and cauda epididymidisen_US
dc.typeConference_Paperen_US
dc.identifier.emailLeung, GPH:gphleung@hkucc.hku.hken_US
dc.identifier.authorityLeung, GPH=rp00234en_US
dc.description.naturelink_to_OA_fulltexten_US
dc.identifier.doi10.1095/biolreprod64.2.482-
dc.identifier.pmid11159350-
dc.identifier.scopuseid_2-s2.0-0035144522en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0035144522&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume64en_US
dc.identifier.issue2en_US
dc.identifier.spage482en_US
dc.identifier.epage490en_US
dc.identifier.isiWOS:000166650400011-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridLeung, GPH=35963668200en_US
dc.identifier.scopusauthoridTse, CM=7103295076en_US
dc.identifier.scopusauthoridCheng Chew, SB=6701358810en_US
dc.identifier.scopusauthoridWong, PYD=7403980262en_US
dc.customcontrol.immutablesml 170110 amended-
dc.identifier.issnl0006-3363-

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