File Download
  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Collagen degradation by host-derived enzymes during aging

TitleCollagen degradation by host-derived enzymes during aging
Authors
KeywordsDentin matrix
Gelatinase
Matrix metalloproteinases (MMPs)
Issue Date2004
PublisherSage Publications, Inc.. The Journal's web site is located at http://www.sagepub.com/journalsProdDesc.nav?prodId=Journal201925
Citation
Journal Of Dental Research, 2004, v. 83 n. 3, p. 216-221 How to Cite?
AbstractIncompletely infiltrated collagen fibrils in acid-etched dentin are susceptible to degradation. We hypothesize that degradation can occur in the absence of bacteria. Partially demineralized collagen matrices (DCMs) prepared from human dentin were stored in artificial saliva. Control specimens were stored in artificial saliva containing proteolytic enzyme inhibitors, or pure mineral oil. We retrieved them at 24 hrs, 90 and 250 days to examine the extent of degradation of DCM. In the 24-hour experimental and 90- and 250-day control specimens, we observed 5- to 6-μm-thick layers of DCM containing banded collagen fibrils. DCMs were almost completely destroyed in the 250-day experimental specimens, but not when incubated with enzyme inhibitors or mineral oil. Functional enzyme analysis of dentin powder revealed low levels of collagenolytic activity that was inhibited by protease inhibitors or 0.2% chlorhexidine. We hypothesize that collagen degradation occurred over time, via host-derived matrix metalloproteinases that are released slowly over time.
Persistent Identifierhttp://hdl.handle.net/10722/53303
ISSN
2015 Impact Factor: 4.602
2015 SCImago Journal Rankings: 1.714
References

 

DC FieldValueLanguage
dc.contributor.authorPashley, DHen_HK
dc.contributor.authorTay, FRen_HK
dc.contributor.authorYiu, Cen_HK
dc.contributor.authorHashimoto, Men_HK
dc.contributor.authorBreschi, Len_HK
dc.contributor.authorCarvalho, RMen_HK
dc.contributor.authorIto, Sen_HK
dc.date.accessioned2009-04-03T07:06:21Z-
dc.date.available2009-04-03T07:06:21Z-
dc.date.issued2004en_HK
dc.identifier.citationJournal Of Dental Research, 2004, v. 83 n. 3, p. 216-221en_HK
dc.identifier.issn0022-0345en_HK
dc.identifier.urihttp://hdl.handle.net/10722/53303-
dc.description.abstractIncompletely infiltrated collagen fibrils in acid-etched dentin are susceptible to degradation. We hypothesize that degradation can occur in the absence of bacteria. Partially demineralized collagen matrices (DCMs) prepared from human dentin were stored in artificial saliva. Control specimens were stored in artificial saliva containing proteolytic enzyme inhibitors, or pure mineral oil. We retrieved them at 24 hrs, 90 and 250 days to examine the extent of degradation of DCM. In the 24-hour experimental and 90- and 250-day control specimens, we observed 5- to 6-μm-thick layers of DCM containing banded collagen fibrils. DCMs were almost completely destroyed in the 250-day experimental specimens, but not when incubated with enzyme inhibitors or mineral oil. Functional enzyme analysis of dentin powder revealed low levels of collagenolytic activity that was inhibited by protease inhibitors or 0.2% chlorhexidine. We hypothesize that collagen degradation occurred over time, via host-derived matrix metalloproteinases that are released slowly over time.en_HK
dc.languageengen_HK
dc.publisherSage Publications, Inc.. The Journal's web site is located at http://www.sagepub.com/journalsProdDesc.nav?prodId=Journal201925en_HK
dc.relation.ispartofJournal of Dental Researchen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subjectDentin matrixen_HK
dc.subjectGelatinaseen_HK
dc.subjectMatrix metalloproteinases (MMPs)en_HK
dc.titleCollagen degradation by host-derived enzymes during agingen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0022-0345&volume=83&issue=3&spage=216&epage=221&date=2004&atitle=Collagen+degradation+by+host-derived+enzymes+during+agingen_HK
dc.identifier.emailYiu, C:ckyyiu@hkucc.hku.hken_HK
dc.identifier.authorityYiu, C=rp00018en_HK
dc.description.naturepublished_or_final_versionen_HK
dc.identifier.scopuseid_2-s2.0-1642618268en_HK
dc.identifier.hkuros108255-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-1642618268&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume83en_HK
dc.identifier.issue3en_HK
dc.identifier.spage216en_HK
dc.identifier.epage221en_HK
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridPashley, DH=35448600800en_HK
dc.identifier.scopusauthoridTay, FR=7102091962en_HK
dc.identifier.scopusauthoridYiu, C=7007115156en_HK
dc.identifier.scopusauthoridHashimoto, M=35380578400en_HK
dc.identifier.scopusauthoridBreschi, L=7003933670en_HK
dc.identifier.scopusauthoridCarvalho, RM=7103357029en_HK
dc.identifier.scopusauthoridIto, S=35414429700en_HK

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats