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Article: Kidney claudin-19: Localization in distal tubules and collecting ducts and dysregulation in polycystic renal disease

TitleKidney claudin-19: Localization in distal tubules and collecting ducts and dysregulation in polycystic renal disease
Authors
KeywordsAquaporins
Claudin-19
Kidney
Polycystic disease
Tight junction
Issue Date2006
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febslet
Citation
Febs Letters, 2006, v. 580 n. 3, p. 923-931 How to Cite?
AbstractTight junction (TJ) constitutes the barrier by controlling the passage of ions and molecules via paracellular pathway and the movement of proteins and lipids between apical and basolateral domains of the plasma membrane. Claudins, occludin, and junctional adhesion molecules are the major three transmembrane proteins at TJ. This study focuses a newly identified mammalian TJ gene, claudin-19, in kidneys. Mouse claudin-19 composes of 224 amino acids and shares 98.2% and 95% amino acid homology with rat and human, respectively; the most evolutionary-related claudins are claudin-1 and -7, which share ∼75% DNA sequence homology with claudin-19. Claudin-19 is abundantly expressed in the mouse and rat kidneys among the organs examined by Northern blots, and to a much less extent, also found in brain by RT-PCR. Claudin-19 and zonula occludens-1 (ZO-1) are localized at junctional regions of Madin-Darby canine kidney (MDCK) cells by immunofluorescent microscopy. In addition, ZO-1 is found in the claudin-19-associated protein complexes in MDCK cells by co-immunoprecipitation. Using aquaporin-1 and aquaporin-2 antibodies as markers for different renal segment, strong expression of claudin-19 was observed in distal tubules of the cortex as well as in the collecting ducts of the medulla. To less extent, claudin-19 is also present in the proximal tubules (cortex) and in the loop of Henle (medulla). Furthermore, intense claudin-19 immunoreactivity is found co-localized with the ZO-1 in kidneys from postnatal day 15, day 45, and adult rats and mice. Similar localizations of claudin-19 and ZO-1 are also observed in human kidneys. Since these renal segments are mainly for controlling the paracellular cation transport, it is suggested that claudin-19 may participate in these processes. In human polycystic kidneys, decreased expression and dyslocalization of claudin-19 are noticed, suggesting a possible correlation between claudin-19 and renal disorders. Taken together, claudin-19 is a claudin isoform that is highly and specifically expressed in renal tubules with a putative role in TJ homeostasis in renal physiology. © 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/87373
ISSN
2015 Impact Factor: 3.519
2015 SCImago Journal Rankings: 2.026
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLee, NPYen_HK
dc.contributor.authorTong, MKen_HK
dc.contributor.authorLeung, PPen_HK
dc.contributor.authorChan, VWen_HK
dc.contributor.authorLeung, Sen_HK
dc.contributor.authorTam, PCen_HK
dc.contributor.authorChan, KWen_HK
dc.contributor.authorLee, KFen_HK
dc.contributor.authorYeung, WSBen_HK
dc.contributor.authorLuk, JMen_HK
dc.date.accessioned2010-09-06T09:28:50Z-
dc.date.available2010-09-06T09:28:50Z-
dc.date.issued2006en_HK
dc.identifier.citationFebs Letters, 2006, v. 580 n. 3, p. 923-931en_HK
dc.identifier.issn0014-5793en_HK
dc.identifier.urihttp://hdl.handle.net/10722/87373-
dc.description.abstractTight junction (TJ) constitutes the barrier by controlling the passage of ions and molecules via paracellular pathway and the movement of proteins and lipids between apical and basolateral domains of the plasma membrane. Claudins, occludin, and junctional adhesion molecules are the major three transmembrane proteins at TJ. This study focuses a newly identified mammalian TJ gene, claudin-19, in kidneys. Mouse claudin-19 composes of 224 amino acids and shares 98.2% and 95% amino acid homology with rat and human, respectively; the most evolutionary-related claudins are claudin-1 and -7, which share ∼75% DNA sequence homology with claudin-19. Claudin-19 is abundantly expressed in the mouse and rat kidneys among the organs examined by Northern blots, and to a much less extent, also found in brain by RT-PCR. Claudin-19 and zonula occludens-1 (ZO-1) are localized at junctional regions of Madin-Darby canine kidney (MDCK) cells by immunofluorescent microscopy. In addition, ZO-1 is found in the claudin-19-associated protein complexes in MDCK cells by co-immunoprecipitation. Using aquaporin-1 and aquaporin-2 antibodies as markers for different renal segment, strong expression of claudin-19 was observed in distal tubules of the cortex as well as in the collecting ducts of the medulla. To less extent, claudin-19 is also present in the proximal tubules (cortex) and in the loop of Henle (medulla). Furthermore, intense claudin-19 immunoreactivity is found co-localized with the ZO-1 in kidneys from postnatal day 15, day 45, and adult rats and mice. Similar localizations of claudin-19 and ZO-1 are also observed in human kidneys. Since these renal segments are mainly for controlling the paracellular cation transport, it is suggested that claudin-19 may participate in these processes. In human polycystic kidneys, decreased expression and dyslocalization of claudin-19 are noticed, suggesting a possible correlation between claudin-19 and renal disorders. Taken together, claudin-19 is a claudin isoform that is highly and specifically expressed in renal tubules with a putative role in TJ homeostasis in renal physiology. © 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febsleten_HK
dc.relation.ispartofFEBS Lettersen_HK
dc.rightsF E B S Letters. Copyright © Elsevier BV.en_HK
dc.subjectAquaporinsen_HK
dc.subjectClaudin-19en_HK
dc.subjectKidneyen_HK
dc.subjectPolycystic diseaseen_HK
dc.subjectTight junctionen_HK
dc.subject.meshAnimalsen_HK
dc.subject.meshAquaporin 1 - metabolismen_HK
dc.subject.meshAquaporin 2 - metabolismen_HK
dc.subject.meshBase Sequenceen_HK
dc.subject.meshCell Lineen_HK
dc.subject.meshDogsen_HK
dc.subject.meshGene Expression Regulationen_HK
dc.subject.meshHumansen_HK
dc.subject.meshIon Transporten_HK
dc.subject.meshKidney Tubules, Collecting - metabolism - pathologyen_HK
dc.subject.meshKidney Tubules, Distal - metabolism - pathologyen_HK
dc.subject.meshLoop of Henle - metabolism - pathologyen_HK
dc.subject.meshMembrane Proteins - metabolismen_HK
dc.subject.meshMolecular Sequence Dataen_HK
dc.subject.meshOrgan Specificityen_HK
dc.subject.meshPhosphoproteins - metabolismen_HK
dc.subject.meshPolycystic Kidney Diseases - metabolism - pathologyen_HK
dc.subject.meshRatsen_HK
dc.subject.meshRats, Sprague-Dawleyen_HK
dc.subject.meshTight Junctions - metabolism - pathologyen_HK
dc.titleKidney claudin-19: Localization in distal tubules and collecting ducts and dysregulation in polycystic renal diseaseen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0014-5793&volume=580&issue=3&spage=923&epage=31&date=2006&atitle=Kidney+claudin-19:+Localization+in+distal+tubules+and+collecting+ducts+and+dysregulation+in+polycystic+renal+diseaseen_HK
dc.identifier.emailLee, NPY: nikkilee@hku.hken_HK
dc.identifier.emailChan, KW: hrmtckw@hku.hken_HK
dc.identifier.emailLee, KF: ckflee@hku.hken_HK
dc.identifier.emailYeung, WSB: wsbyeung@hkucc.hku.hken_HK
dc.identifier.emailLuk, JM: jmluk@hkucc.hku.hken_HK
dc.identifier.authorityLee, NPY=rp00263en_HK
dc.identifier.authorityChan, KW=rp00330en_HK
dc.identifier.authorityLee, KF=rp00458en_HK
dc.identifier.authorityYeung, WSB=rp00331en_HK
dc.identifier.authorityLuk, JM=rp00349en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.febslet.2006.01.019en_HK
dc.identifier.pmid16427635en_HK
dc.identifier.scopuseid_2-s2.0-31444455224en_HK
dc.identifier.hkuros113961en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-31444455224&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume580en_HK
dc.identifier.issue3en_HK
dc.identifier.spage923en_HK
dc.identifier.epage931en_HK
dc.identifier.isiWOS:000235222500032-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridLee, NPY=7402722690en_HK
dc.identifier.scopusauthoridTong, MK=36880476300en_HK
dc.identifier.scopusauthoridLeung, PP=7401749062en_HK
dc.identifier.scopusauthoridChan, VW=36005663800en_HK
dc.identifier.scopusauthoridLeung, S=35228353200en_HK
dc.identifier.scopusauthoridTam, PC=7202539419en_HK
dc.identifier.scopusauthoridChan, KW=16444133100en_HK
dc.identifier.scopusauthoridLee, KF=26643097500en_HK
dc.identifier.scopusauthoridYeung, WSB=7102370745en_HK
dc.identifier.scopusauthoridLuk, JM=7006777791en_HK

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