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Article: Differential effects of advanced glycation end-products on renal tubular cell inflammation
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TitleDifferential effects of advanced glycation end-products on renal tubular cell inflammation
 
AuthorsTang, SCW1
Chan, LYY1
Leung, JCK1
Cheng, AS1
Lin, M1
Lan, HY1
Lai, KN1
 
Keywordsadvanced glycation end-products
carboxymethyllysine albumin
chemokines
diabetic nephropathy
proximal tubular cells
 
Issue Date2011
 
PublisherBlackwell Publishing Asia. The Journal's web site is located at http://www.blackwellpublishing.com/journals/NEP
 
CitationNephrology, 2011, v. 16 n. 4, p. 417-425 [How to Cite?]
DOI: http://dx.doi.org/10.1111/j.1440-1797.2010.01437.x
 
AbstractAim: The authors recently showed that advanced glycation end-products (AGE) in the form of glycated albumin (GA) upregulated renal tubular expression of interleukin (IL)-8 and soluble intercellular adhesion molecule-1 (sICAM-1), but not other important cytokines known to mediate diabetic nephropathy. This implies that other molecules such as the carbonyl intermediates of AGE or other modified protein lysine-albumin may participate in diabetic tubular injury. Methods: Human proximal tubular epithelial cells (PTEC) were growth-arrested and exposed to methylglyoxal (MG), MG-bovine serum albumin (BSA)-AGE, carboxymethyllysine (CML)-BSA, AGE-BSA or BSA with or without prior addition of rosiglitazone that was previously shown to attenuate the pro-inflammatory effect of GA alone. Results: MG-BSA-AGE and AGE-BSA upregulated tubular expression of connective tissue growth factor (CTGF), transforming growth factor (TGF)-β, and vascular endothelial growth factor (VEGF), whereas CML-BSA stimulated expression of IL-6, CCL-2, CTGF, TGF-β and VEGF. These AGE compounds also activated nuclear factor (NF)-ÎB and their effects were attenuated by pre-incubation with anti-RAGE antibody. MG and BSA did not affect the expression of any of these molecules. Rosiglitazone did not affect the in vitro biological effects of MG, MG-BSA-AGE, AGE-BSA or CML-BSA on PTEC. Conclusion: AGE exhibit differential inflammatory and fibrotic effects on PTEC via RAGE activation and NF-ÎB signal transduction. Rosiglitazone had no effect on these responses. Further investigations on compounds that nullify the downstream effects of these AGE are warranted. Tang and colleagues showed that various AGE formation (MG-BSA-AGE, AGE-BSA and CML-BSA are important AGE) have differential pro-inflammatory and profibrotic effects on cultured PTEC via RAGE activation and NF-ÎB signal transduction. © 2011 Asian Pacific Society of Nephrology.
 
ISSN1320-5358
2013 Impact Factor: 1.864
 
DOIhttp://dx.doi.org/10.1111/j.1440-1797.2010.01437.x
 
ISI Accession Number IDWOS:000289899500010
Funding AgencyGrant Number
Research Grants Council of Hong KongHKU 7764/07 M
Funding Information:

This work was supported by the Research Grants Council (General Research Fund number HKU 7764/07 M) of Hong Kong. Rosiglitazone was a kind gift from GlaxoSmithKline (Compound Management Division, Stevenage, Herts, UK).

 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorTang, SCW
 
dc.contributor.authorChan, LYY
 
dc.contributor.authorLeung, JCK
 
dc.contributor.authorCheng, AS
 
dc.contributor.authorLin, M
 
dc.contributor.authorLan, HY
 
dc.contributor.authorLai, KN
 
dc.date.accessioned2011-08-26T14:24:30Z
 
dc.date.available2011-08-26T14:24:30Z
 
dc.date.issued2011
 
dc.description.abstractAim: The authors recently showed that advanced glycation end-products (AGE) in the form of glycated albumin (GA) upregulated renal tubular expression of interleukin (IL)-8 and soluble intercellular adhesion molecule-1 (sICAM-1), but not other important cytokines known to mediate diabetic nephropathy. This implies that other molecules such as the carbonyl intermediates of AGE or other modified protein lysine-albumin may participate in diabetic tubular injury. Methods: Human proximal tubular epithelial cells (PTEC) were growth-arrested and exposed to methylglyoxal (MG), MG-bovine serum albumin (BSA)-AGE, carboxymethyllysine (CML)-BSA, AGE-BSA or BSA with or without prior addition of rosiglitazone that was previously shown to attenuate the pro-inflammatory effect of GA alone. Results: MG-BSA-AGE and AGE-BSA upregulated tubular expression of connective tissue growth factor (CTGF), transforming growth factor (TGF)-β, and vascular endothelial growth factor (VEGF), whereas CML-BSA stimulated expression of IL-6, CCL-2, CTGF, TGF-β and VEGF. These AGE compounds also activated nuclear factor (NF)-ÎB and their effects were attenuated by pre-incubation with anti-RAGE antibody. MG and BSA did not affect the expression of any of these molecules. Rosiglitazone did not affect the in vitro biological effects of MG, MG-BSA-AGE, AGE-BSA or CML-BSA on PTEC. Conclusion: AGE exhibit differential inflammatory and fibrotic effects on PTEC via RAGE activation and NF-ÎB signal transduction. Rosiglitazone had no effect on these responses. Further investigations on compounds that nullify the downstream effects of these AGE are warranted. Tang and colleagues showed that various AGE formation (MG-BSA-AGE, AGE-BSA and CML-BSA are important AGE) have differential pro-inflammatory and profibrotic effects on cultured PTEC via RAGE activation and NF-ÎB signal transduction. © 2011 Asian Pacific Society of Nephrology.
 
dc.description.naturelink_to_subscribed_fulltext
 
dc.identifier.citationNephrology, 2011, v. 16 n. 4, p. 417-425 [How to Cite?]
DOI: http://dx.doi.org/10.1111/j.1440-1797.2010.01437.x
 
dc.identifier.citeulike8502227
 
dc.identifier.doihttp://dx.doi.org/10.1111/j.1440-1797.2010.01437.x
 
dc.identifier.epage425
 
dc.identifier.hkuros190809
 
dc.identifier.isiWOS:000289899500010
Funding AgencyGrant Number
Research Grants Council of Hong KongHKU 7764/07 M
Funding Information:

This work was supported by the Research Grants Council (General Research Fund number HKU 7764/07 M) of Hong Kong. Rosiglitazone was a kind gift from GlaxoSmithKline (Compound Management Division, Stevenage, Herts, UK).

 
dc.identifier.issn1320-5358
2013 Impact Factor: 1.864
 
dc.identifier.issue4
 
dc.identifier.pmid21143336
 
dc.identifier.scopuseid_2-s2.0-79955420320
 
dc.identifier.spage417
 
dc.identifier.urihttp://hdl.handle.net/10722/137407
 
dc.identifier.volume16
 
dc.languageeng
 
dc.publisherBlackwell Publishing Asia. The Journal's web site is located at http://www.blackwellpublishing.com/journals/NEP
 
dc.publisher.placeAustralia
 
dc.relation.ispartofNephrology
 
dc.relation.referencesReferences in Scopus
 
dc.rightsThe definitive version is available at www.blackwell-synergy.com
 
dc.subject.meshEpithelial Cells - drug effects - immunology - metabolism - pathology
 
dc.subject.meshGlycosylation End Products, Advanced - metabolism
 
dc.subject.meshInflammation Mediators - metabolism
 
dc.subject.meshKidney Tubules, Proximal - drug effects - immunology - metabolism - pathology
 
dc.subject.meshNephritis, Interstitial - immunology - metabolism - pathology - prevention and control
 
dc.subjectadvanced glycation end-products
 
dc.subjectcarboxymethyllysine albumin
 
dc.subjectchemokines
 
dc.subjectdiabetic nephropathy
 
dc.subjectproximal tubular cells
 
dc.titleDifferential effects of advanced glycation end-products on renal tubular cell inflammation
 
dc.typeArticle
 
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Author Affiliations
  1. The University of Hong Kong