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Conference Paper: Lipopolysaccharide and hypoxia modulate collagen metabolism in human gingival fibroblasts

TitleLipopolysaccharide and hypoxia modulate collagen metabolism in human gingival fibroblasts
Authors
KeywordsCollagen
Fibroblasts
Host-microbial interactions
Infection and Periodontics
Issue Date2011
PublisherInternational Association for Dental Research.
Citation
The 25th IADR-SEA Division Annual Scientific Meeting, Singapore, 28-30 October 2011. How to Cite?
AbstractOBJECTIVES: Collagens are key structural components of connective tissues. Biochemical alternation of collagen metabolism during periodontal bacterial infection leads to tissue breakdown. We examined collagen I metabolism in human gingival fibroblasts (HGF) and systemically studied the impact of hypoxia and lipopolysaccharides (LPS), which are both intimately involved in the pathogenesis of periodontal disease. METHODS: Primary HGF were treated with Escherichia coli LPS, Toll-like receptor (TLR) 4-neutralizing antibody, and/or hypoxia-inducible factor α (HIF-α) inhibitor 3-(5'-hydroxymethyl-2'-furyl)-1-benzyl indazole (YC-1) under different oxygen concentrations. The transcript levels of 35 genes directly related to collagen I synthesis and degradation were examined using Real-Time PCR. The concentrations of collagen I and tissue inhibitor of metalloproteinase (TIMP)-3 from cultured cells were measured by ELISA. The activities of matrix metalloproteinase (MMP) -2 and -9 were examined using gelatin zymography. RESULTS: Although the transcript and protein production of collagen I propeptide remained unchanged, hypoxia and/or LPS enhanced the transcription of several enzymes related to collagen assembly and crosslinking, including prolyl 4-hydroxylases, lysyl hydroxylases and lysyl oxidases. The mRNA levels of MMP-1, 2, 8, 9, 13 and 14 remained stable, as did the enzymatic activity of MMP-2 and -9. However, levels of TIMP-1 and -3 were increased by hypoxia. The observed cellular reactions under hypoxic conditions could be reversed by YC-1 treatment. CONCLUSIONS: Hypoxia and LPS appeared to alter cellular reactions in HGF by maintaining or upregulating signals involved in collagen I matrix homeostasis possibly mediated through HIF-α.
DescriptionPoster Discussion Session - Senior Researcher Division Travel Award: abstract no. 80
Persistent Identifierhttp://hdl.handle.net/10722/164990

 

DC FieldValueLanguage
dc.contributor.authorLi, JPen_US
dc.contributor.authorFung, MLen_US
dc.contributor.authorLeung, WKen_US
dc.date.accessioned2012-09-20T08:13:16Z-
dc.date.available2012-09-20T08:13:16Z-
dc.date.issued2011en_US
dc.identifier.citationThe 25th IADR-SEA Division Annual Scientific Meeting, Singapore, 28-30 October 2011.en_US
dc.identifier.urihttp://hdl.handle.net/10722/164990-
dc.descriptionPoster Discussion Session - Senior Researcher Division Travel Award: abstract no. 80-
dc.description.abstractOBJECTIVES: Collagens are key structural components of connective tissues. Biochemical alternation of collagen metabolism during periodontal bacterial infection leads to tissue breakdown. We examined collagen I metabolism in human gingival fibroblasts (HGF) and systemically studied the impact of hypoxia and lipopolysaccharides (LPS), which are both intimately involved in the pathogenesis of periodontal disease. METHODS: Primary HGF were treated with Escherichia coli LPS, Toll-like receptor (TLR) 4-neutralizing antibody, and/or hypoxia-inducible factor α (HIF-α) inhibitor 3-(5'-hydroxymethyl-2'-furyl)-1-benzyl indazole (YC-1) under different oxygen concentrations. The transcript levels of 35 genes directly related to collagen I synthesis and degradation were examined using Real-Time PCR. The concentrations of collagen I and tissue inhibitor of metalloproteinase (TIMP)-3 from cultured cells were measured by ELISA. The activities of matrix metalloproteinase (MMP) -2 and -9 were examined using gelatin zymography. RESULTS: Although the transcript and protein production of collagen I propeptide remained unchanged, hypoxia and/or LPS enhanced the transcription of several enzymes related to collagen assembly and crosslinking, including prolyl 4-hydroxylases, lysyl hydroxylases and lysyl oxidases. The mRNA levels of MMP-1, 2, 8, 9, 13 and 14 remained stable, as did the enzymatic activity of MMP-2 and -9. However, levels of TIMP-1 and -3 were increased by hypoxia. The observed cellular reactions under hypoxic conditions could be reversed by YC-1 treatment. CONCLUSIONS: Hypoxia and LPS appeared to alter cellular reactions in HGF by maintaining or upregulating signals involved in collagen I matrix homeostasis possibly mediated through HIF-α.-
dc.languageengen_US
dc.publisherInternational Association for Dental Research.-
dc.relation.ispartofIADR-SEA Division Annual Scientific Meeting, 2011en_US
dc.subjectCollagen-
dc.subjectFibroblasts-
dc.subjectHost-microbial interactions-
dc.subjectInfection and Periodontics-
dc.titleLipopolysaccharide and hypoxia modulate collagen metabolism in human gingival fibroblastsen_US
dc.typeConference_Paperen_US
dc.identifier.emailFung, ML: fungml@hkucc.hku.hken_US
dc.identifier.emailLeung, WK: ewkleung@hkucc.hku.hken_US
dc.identifier.authorityFung, ML=rp00433en_US
dc.identifier.authorityLeung, WK=rp00019en_US
dc.description.naturelink_to_OA_fulltext-
dc.identifier.hkuros209843en_US
dc.description.otherThe 25th IADR-SEA Division Annual Scientific Meeting, Singapore, 28-30 October 2011.-

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