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Article: Markedly increased urinary preprohaptoglobin and haptoglobin in passive heymann nephritis: A differential proteomics approach

TitleMarkedly increased urinary preprohaptoglobin and haptoglobin in passive heymann nephritis: A differential proteomics approach
Authors
Keywords2D-DIGE
Glomeruli
Haptoglobin
Membranous nephropathy
Passive Heymann nephritis
Preprohaptoglobin
Proteomics
Urine
Issue Date2007
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jprobs
Citation
Journal Of Proteome Research, 2007, v. 6 n. 8, p. 3313-3320 How to Cite?
AbstractMembranous nephropathy (MN), a common cause of idiopathic nephrotic syndrome in adults, remains a potentially devastating problem worldwide. At present, there is no reliable noninvasive method for predicting and/or monitoring this glomerular disease, and its pathophysiology remains poorly understood. In the present study, the urinary proteome profile of rats after 10 days of an induction of passive Heymann nephritis (PHN), which resembles human MN, was compared to that of the baseline (control) urine prior to the induction of PHN by anti-Fx1 A injection. Each pool of PHN and control urine samples (n = 10 each) was labeled with different fluorescent dyes (Cy3 or Cy5), and equal amounts of the labeled proteins of both pools were resolved in the same 2D gel, together with an internal standard labeled with Cy2. Two-dimensional difference gel electrophoresis revealed a number of protein spots whose expression levels were altered during PHN. Eighteen protein spots with > 1.5-fold changes and p < 0.05 were selected for subsequent identification by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. They were successfully identified as serum albumin precursor, α-1-antitrypsin, preprohaptoglobin, liver-regeneration-related protein, and transthyretin (which increased during PHN) and E-cadherin, MPP7, tropomyosin β, kallikrein, and α-2u globulin (which decreased in the PHN urine). Among these proteins, the increase in urinary preprohaptoglobin has particularly drawn our attention because of its byproduct, haptoglobin (Hp), which is involved in the protection of tissue damage from hemoglobin-induced oxidative stress. Western blotting and enzyme-linked immunosorbent assay clearly showed a markedly increased level of Hp in the urine, but not in the serum, of the PHN animals. Our findings may lead to a significant advance in the attempt to define a new therapeutic target and/or novel biomarker for human MN. © 2007 American Chemical Society.
Persistent Identifierhttp://hdl.handle.net/10722/84807
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.authorThongboonkerd, Ven_HK
dc.contributor.authorWan, JMFen_HK
dc.date.accessioned2010-09-06T08:57:20Z-
dc.date.available2010-09-06T08:57:20Z-
dc.date.issued2007en_HK
dc.identifier.citationJournal Of Proteome Research, 2007, v. 6 n. 8, p. 3313-3320en_HK
dc.identifier.issn1535-3893en_HK
dc.identifier.urihttp://hdl.handle.net/10722/84807-
dc.description.abstractMembranous nephropathy (MN), a common cause of idiopathic nephrotic syndrome in adults, remains a potentially devastating problem worldwide. At present, there is no reliable noninvasive method for predicting and/or monitoring this glomerular disease, and its pathophysiology remains poorly understood. In the present study, the urinary proteome profile of rats after 10 days of an induction of passive Heymann nephritis (PHN), which resembles human MN, was compared to that of the baseline (control) urine prior to the induction of PHN by anti-Fx1 A injection. Each pool of PHN and control urine samples (n = 10 each) was labeled with different fluorescent dyes (Cy3 or Cy5), and equal amounts of the labeled proteins of both pools were resolved in the same 2D gel, together with an internal standard labeled with Cy2. Two-dimensional difference gel electrophoresis revealed a number of protein spots whose expression levels were altered during PHN. Eighteen protein spots with > 1.5-fold changes and p < 0.05 were selected for subsequent identification by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. They were successfully identified as serum albumin precursor, α-1-antitrypsin, preprohaptoglobin, liver-regeneration-related protein, and transthyretin (which increased during PHN) and E-cadherin, MPP7, tropomyosin β, kallikrein, and α-2u globulin (which decreased in the PHN urine). Among these proteins, the increase in urinary preprohaptoglobin has particularly drawn our attention because of its byproduct, haptoglobin (Hp), which is involved in the protection of tissue damage from hemoglobin-induced oxidative stress. Western blotting and enzyme-linked immunosorbent assay clearly showed a markedly increased level of Hp in the urine, but not in the serum, of the PHN animals. Our findings may lead to a significant advance in the attempt to define a new therapeutic target and/or novel biomarker for human MN. © 2007 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.subject2D-DIGEen_HK
dc.subjectGlomerulien_HK
dc.subjectHaptoglobinen_HK
dc.subjectMembranous nephropathyen_HK
dc.subjectPassive Heymann nephritisen_HK
dc.subjectPreprohaptoglobinen_HK
dc.subjectProteomicsen_HK
dc.subjectUrineen_HK
dc.titleMarkedly increased urinary preprohaptoglobin and haptoglobin in passive heymann nephritis: A differential proteomics approachen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1535-3893&volume=6&spage=3313&epage=3320&date=2007&atitle=Markedly+Increased+Urinary+Preprohaptoglobin+and+Haptoglobin+in+Passive+Heymann+Nephritis:+A+Differential+Proteomics+Approachen_HK
dc.identifier.emailWan, JMF: jmfwan@hku.hken_HK
dc.identifier.authorityWan, JMF=rp00798en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1021/pr070245ben_HK
dc.identifier.pmid17616219-
dc.identifier.scopuseid_2-s2.0-34548152121en_HK
dc.identifier.hkuros136115en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-34548152121&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume6en_HK
dc.identifier.issue8en_HK
dc.identifier.spage3313en_HK
dc.identifier.epage3320en_HK
dc.identifier.isiWOS:000248683200038-
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.scopusauthoridThongboonkerd, V=6603472979en_HK
dc.identifier.scopusauthoridWan, JMF=8930305000en_HK

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