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Article: Differential effects of advanced glycation end-products on renal tubular cell inflammation

TitleDifferential effects of advanced glycation end-products on renal tubular cell inflammation
Authors
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
Citation
Nephrology, 2011, v. 16 n. 4, p. 417-425 How to Cite?
Abstract
Aim: 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.
Persistent Identifierhttp://hdl.handle.net/10722/137407
ISSN
2013 Impact Factor: 1.864
ISI Accession Number ID
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).

References

 

DC FieldValueLanguage
dc.contributor.authorTang, SCWen_HK
dc.contributor.authorChan, LYYen_HK
dc.contributor.authorLeung, JCKen_HK
dc.contributor.authorCheng, ASen_HK
dc.contributor.authorLin, Men_HK
dc.contributor.authorLan, HYen_HK
dc.contributor.authorLai, KNen_HK
dc.date.accessioned2011-08-26T14:24:30Z-
dc.date.available2011-08-26T14:24:30Z-
dc.date.issued2011en_HK
dc.identifier.citationNephrology, 2011, v. 16 n. 4, p. 417-425en_HK
dc.identifier.issn1320-5358en_HK
dc.identifier.urihttp://hdl.handle.net/10722/137407-
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.en_HK
dc.languageengen_US
dc.publisherBlackwell Publishing Asia. The Journal's web site is located at http://www.blackwellpublishing.com/journals/NEPen_HK
dc.relation.ispartofNephrologyen_HK
dc.rightsThe definitive version is available at www.blackwell-synergy.comen_US
dc.subjectadvanced glycation end-productsen_HK
dc.subjectcarboxymethyllysine albuminen_HK
dc.subjectchemokinesen_HK
dc.subjectdiabetic nephropathyen_HK
dc.subjectproximal tubular cellsen_HK
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.titleDifferential effects of advanced glycation end-products on renal tubular cell inflammationen_HK
dc.typeArticleen_HK
dc.identifier.emailTang, SCW: scwtang@hku.hken_HK
dc.identifier.emailLeung, JCK: jckleung@hku.hken_HK
dc.identifier.emailLai, KN: knlai@hku.hken_HK
dc.identifier.authorityTang, SCW=rp00480en_HK
dc.identifier.authorityLeung, JCK=rp00448en_HK
dc.identifier.authorityLai, KN=rp00324en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1111/j.1440-1797.2010.01437.xen_HK
dc.identifier.pmid21143336en_HK
dc.identifier.scopuseid_2-s2.0-79955420320en_HK
dc.identifier.hkuros190809en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-79955420320&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume16en_HK
dc.identifier.issue4en_HK
dc.identifier.spage417en_HK
dc.identifier.epage425en_HK
dc.identifier.isiWOS:000289899500010-
dc.publisher.placeAustraliaen_HK
dc.identifier.scopusauthoridTang, SCW=7403437082en_HK
dc.identifier.scopusauthoridChan, LYY=55182644100en_HK
dc.identifier.scopusauthoridLeung, JCK=7202180349en_HK
dc.identifier.scopusauthoridCheng, AS=21733421700en_HK
dc.identifier.scopusauthoridLin, M=55263956500en_HK
dc.identifier.scopusauthoridLan, HY=24544799000en_HK
dc.identifier.scopusauthoridLai, KN=7402135706en_HK
dc.identifier.citeulike8502227-

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