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Article: Advanced glycation end products inhibit the expression of collagens type i and iii by human gingival fibroblasts

TitleAdvanced glycation end products inhibit the expression of collagens type i and iii by human gingival fibroblasts
Authors
Issue Date2009
PublisherAmerican Academy of Periodontology. The Journal's web site is located at http://www.perio.org
Citation
Journal Of Periodontology, 2009, v. 80 n. 7, p. 1166-1173 How to Cite?
AbstractBackground: It is evident that diabetes and periodontal disease are closely interrelated. Accumulation of advanced glycation end products (AGEs), coupled with exaggerated host responses to bacterial infection, may account for the increased periodontal destruction observed in patients with uncontrolled diabetes. The present study investigated the effects of AGEs on the viability of human gingival fibroblasts (HGFs) and the expression of types I and III collagen in HGFs. Methods: The cell viability of HGFs was examined by methylthiazolet-etrazoliumassay, whereas the expression of types I and III collagen message and protein was detected by realtime quantitative reverse transcription-polymerase chain reaction and sandwich enzyme-linked immunosorbent assay, respectively. Results: AGEs significantly suppressed the cell viability of HGFs from 24 to 72 hours (P <0.01). A high concentration of glucose (25 mmol/l) in the culture media exaggerated the inhibition of the survival rate of HGFs (P <0.01). The expression of collagen types I and III messages and proteins was significantly downregulated at 72 hours by AGEs in a concentration-dependent manner (P <0.05). Moreover, the synthesis of intracellular types I and III collagen protein was markedly inhibited by AGEs (P <0.05).Conclusions: AGEs may suppress the cell viability of HGFs and downregulate the expression of types I and III collagen by the cells. Further investigations are warranted to clarify the molecular mechanisms of AGEs in the regulation of cell function and collagen metabolism in patients with diabetes and periodontitis. J Periodontol 2009;80:1166-1173.
Persistent Identifierhttp://hdl.handle.net/10722/66274
ISSN
2015 Impact Factor: 2.844
2015 SCImago Journal Rankings: 1.070
ISI Accession Number ID
Funding AgencyGrant Number
Guangdong Natural Science, Guangzhou, China8151008901000087
Funding Information:

The authors gratefully acknowledge the advice and suggestions of Prof. Hou Fanfan and Dr. Liu Zhiqiang, Institute of Kidney Diseases, South Medical University, Guangzhou, China. This study was funded by the Guangdong Natural Science fund committee 8151008901000087 (to Yun Fu), Guangzhou, China. The authors report no conflicts of interest related to this study.

References

 

DC FieldValueLanguage
dc.contributor.authorRen, Len_HK
dc.contributor.authorFu, Yen_HK
dc.contributor.authorDeng, Yen_HK
dc.contributor.authorQi, Len_HK
dc.contributor.authorJin, Len_HK
dc.date.accessioned2010-09-06T05:45:00Z-
dc.date.available2010-09-06T05:45:00Z-
dc.date.issued2009en_HK
dc.identifier.citationJournal Of Periodontology, 2009, v. 80 n. 7, p. 1166-1173en_HK
dc.identifier.issn0022-3492en_HK
dc.identifier.urihttp://hdl.handle.net/10722/66274-
dc.description.abstractBackground: It is evident that diabetes and periodontal disease are closely interrelated. Accumulation of advanced glycation end products (AGEs), coupled with exaggerated host responses to bacterial infection, may account for the increased periodontal destruction observed in patients with uncontrolled diabetes. The present study investigated the effects of AGEs on the viability of human gingival fibroblasts (HGFs) and the expression of types I and III collagen in HGFs. Methods: The cell viability of HGFs was examined by methylthiazolet-etrazoliumassay, whereas the expression of types I and III collagen message and protein was detected by realtime quantitative reverse transcription-polymerase chain reaction and sandwich enzyme-linked immunosorbent assay, respectively. Results: AGEs significantly suppressed the cell viability of HGFs from 24 to 72 hours (P <0.01). A high concentration of glucose (25 mmol/l) in the culture media exaggerated the inhibition of the survival rate of HGFs (P <0.01). The expression of collagen types I and III messages and proteins was significantly downregulated at 72 hours by AGEs in a concentration-dependent manner (P <0.05). Moreover, the synthesis of intracellular types I and III collagen protein was markedly inhibited by AGEs (P <0.05).Conclusions: AGEs may suppress the cell viability of HGFs and downregulate the expression of types I and III collagen by the cells. Further investigations are warranted to clarify the molecular mechanisms of AGEs in the regulation of cell function and collagen metabolism in patients with diabetes and periodontitis. J Periodontol 2009;80:1166-1173.en_HK
dc.languageengen_HK
dc.publisherAmerican Academy of Periodontology. The Journal's web site is located at http://www.perio.orgen_HK
dc.relation.ispartofJournal of Periodontologyen_HK
dc.subject.meshAdolescenten_HK
dc.subject.meshAdulten_HK
dc.subject.meshAnalysis of Varianceen_HK
dc.subject.meshCell Survival - drug effectsen_HK
dc.subject.meshCells, Cultureden_HK
dc.subject.meshCollagen Type I - drug effects - genetics - metabolismen_HK
dc.subject.meshCollagen Type III - drug effects - genetics - metabolismen_HK
dc.subject.meshFibroblasts - drug effects - metabolismen_HK
dc.subject.meshGingiva - cytology - drug effects - metabolismen_HK
dc.subject.meshGlycosylation End Products, Advanced - pharmacologyen_HK
dc.subject.meshHumansen_HK
dc.subject.meshRNA, Messenger - analysisen_HK
dc.subject.meshReference Valuesen_HK
dc.subject.meshYoung Adulten_HK
dc.titleAdvanced glycation end products inhibit the expression of collagens type i and iii by human gingival fibroblastsen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0022-3492&volume=80&spage=1166&epage=1173&date=2009&atitle=Advanced+glycation+end+products+inhibit+the+expression+of+collagens+type+I+and+III+by+human+gingival+fibroblastsen_HK
dc.identifier.emailJin, L:ljjin@hkucc.hku.hken_HK
dc.identifier.authorityJin, L=rp00028en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1902/jop.2009.080669en_HK
dc.identifier.pmid19563298-
dc.identifier.scopuseid_2-s2.0-68049121642en_HK
dc.identifier.hkuros157971en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-68049121642&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume80en_HK
dc.identifier.issue7en_HK
dc.identifier.spage1166en_HK
dc.identifier.epage1173en_HK
dc.identifier.isiWOS:000268042100022-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridRen, L=35216223200en_HK
dc.identifier.scopusauthoridFu, Y=15077896300en_HK
dc.identifier.scopusauthoridDeng, Y=7401531344en_HK
dc.identifier.scopusauthoridQi, L=35216093000en_HK
dc.identifier.scopusauthoridJin, L=7403328850en_HK

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