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Article: Serial changes in urinary proteome profile of membranous nephropathy: Implications for pathophysiology and biomarker discovery

TitleSerial changes in urinary proteome profile of membranous nephropathy: Implications for pathophysiology and biomarker discovery
Authors
KeywordsBiomarker
Glomerulus
Heymann nephritis
Kidney
Pathophysiology
Proteome
Proteomics
Urine
Issue Date2006
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jprobs
Citation
Journal Of Proteome Research, 2006, v. 5 n. 11, p. 3038-3047 How to Cite?
AbstractMembranous nephropathy is one of the most common causes of primary glomerular diseases worldwide. The present study adopted a gel-based proteomics approach to better understand the pathophysiology and define biomarker candidates of human membranous nephropathy using an animal model of passive Heymann nephritis (PHN). Clinical characteristics of Sprague-Dawley rats injected with rabbit anti-Fx1A antiserum mimicked those of human membranous nephropathy. Serial urine samples were collected at Days 0, 10, 20, 30, 40, and 50 after the injection with anti-Fx1 A (number of rats = 6; total number of gels = 36). Urinary proteome profiles were examined using 2D-PAGE and SYPRO Ruby staining. Quantitative intensity analysis and ANOVA with Tukey post-hoc multiple comparisons revealed 37 differentially expressed proteins among 6 different time-points. These altered proteins were successfully identified by MALDI-TOF MS and classified into 6 categories: (i) proteins with decreased urinary excretion during PHN; (ii) proteins with increased urinary excretion during PHN; (iii) proteins with increased urinary excretion during PHN, but which finally returned to basal levels; (iv) proteins with increased urinary excretion during PHN, but which finally declined below basal levels; (v) proteins with undetectable levels in the urine during PHN; and (vi) proteins that were detectable in the urine only during PHN. Most of these altered proteins have functional significance in signaling pathways, glomerular trafficking, and controlling the glomerular permeability. The ones in categories (v) and (vi) may serve as biomarkers for detecting or monitoring membranous nephropathy. After normalization of the data with 24-h urine creatinine excretion, changes in 34 of initially 37 differentially expressed proteins remained statistically significant. These data underscore the significant impact of urinary proteomics in unraveling disease pathophysiology and biomarker discovery. © 2006 American Chemical Society.
Persistent Identifierhttp://hdl.handle.net/10722/84957
ISSN
2015 Impact Factor: 4.173
2015 SCImago Journal Rankings: 1.962
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorNgai, HHYen_HK
dc.contributor.authorSit, WHen_HK
dc.contributor.authorJiang, PPen_HK
dc.contributor.authorXu, RJen_HK
dc.contributor.authorWan, JMFen_HK
dc.contributor.authorThongboonkerd, Ven_HK
dc.date.accessioned2010-09-06T08:59:05Z-
dc.date.available2010-09-06T08:59:05Z-
dc.date.issued2006en_HK
dc.identifier.citationJournal Of Proteome Research, 2006, v. 5 n. 11, p. 3038-3047en_HK
dc.identifier.issn1535-3893en_HK
dc.identifier.urihttp://hdl.handle.net/10722/84957-
dc.description.abstractMembranous nephropathy is one of the most common causes of primary glomerular diseases worldwide. The present study adopted a gel-based proteomics approach to better understand the pathophysiology and define biomarker candidates of human membranous nephropathy using an animal model of passive Heymann nephritis (PHN). Clinical characteristics of Sprague-Dawley rats injected with rabbit anti-Fx1A antiserum mimicked those of human membranous nephropathy. Serial urine samples were collected at Days 0, 10, 20, 30, 40, and 50 after the injection with anti-Fx1 A (number of rats = 6; total number of gels = 36). Urinary proteome profiles were examined using 2D-PAGE and SYPRO Ruby staining. Quantitative intensity analysis and ANOVA with Tukey post-hoc multiple comparisons revealed 37 differentially expressed proteins among 6 different time-points. These altered proteins were successfully identified by MALDI-TOF MS and classified into 6 categories: (i) proteins with decreased urinary excretion during PHN; (ii) proteins with increased urinary excretion during PHN; (iii) proteins with increased urinary excretion during PHN, but which finally returned to basal levels; (iv) proteins with increased urinary excretion during PHN, but which finally declined below basal levels; (v) proteins with undetectable levels in the urine during PHN; and (vi) proteins that were detectable in the urine only during PHN. Most of these altered proteins have functional significance in signaling pathways, glomerular trafficking, and controlling the glomerular permeability. The ones in categories (v) and (vi) may serve as biomarkers for detecting or monitoring membranous nephropathy. After normalization of the data with 24-h urine creatinine excretion, changes in 34 of initially 37 differentially expressed proteins remained statistically significant. These data underscore the significant impact of urinary proteomics in unraveling disease pathophysiology and biomarker discovery. © 2006 American Chemical Society.en_HK
dc.languageengen_HK
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jprobsen_HK
dc.relation.ispartofJournal of Proteome Researchen_HK
dc.subjectBiomarkeren_HK
dc.subjectGlomerulusen_HK
dc.subjectHeymann nephritisen_HK
dc.subjectKidneyen_HK
dc.subjectPathophysiologyen_HK
dc.subjectProteomeen_HK
dc.subjectProteomicsen_HK
dc.subjectUrineen_HK
dc.titleSerial changes in urinary proteome profile of membranous nephropathy: Implications for pathophysiology and biomarker discoveryen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1535-3893&volume=5&spage=3038&epage=3047&date=2006&atitle=Serial+Changes+in+Urinary+Proteome+Profile+of+Membranous+Nephropathy:+Implications+for+Pathophysiology+and+Biomarker+Discoveryen_HK
dc.identifier.emailXu, RJ: xuruojun@hkucc.hku.hken_HK
dc.identifier.emailWan, JMF: jmfwan@hku.hken_HK
dc.identifier.authorityXu, RJ=rp00820en_HK
dc.identifier.authorityWan, JMF=rp00798en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1021/pr060122ben_HK
dc.identifier.pmid17081055-
dc.identifier.scopuseid_2-s2.0-33751004998en_HK
dc.identifier.hkuros136116en_HK
dc.identifier.hkuros134690-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33751004998&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume5en_HK
dc.identifier.issue11en_HK
dc.identifier.spage3038en_HK
dc.identifier.epage3047en_HK
dc.identifier.isiWOS:000241755400017-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridNgai, HHY=8528923200en_HK
dc.identifier.scopusauthoridSit, WH=8528923000en_HK
dc.identifier.scopusauthoridJiang, PP=36147603700en_HK
dc.identifier.scopusauthoridXu, RJ=7402813973en_HK
dc.identifier.scopusauthoridWan, JMF=8930305000en_HK
dc.identifier.scopusauthoridThongboonkerd, V=6603472979en_HK
dc.identifier.citeulike1414718-

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