File Download
  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Biochemical characterization of the cell-biomaterial interface by quantitative proteomics

TitleBiochemical characterization of the cell-biomaterial interface by quantitative proteomics
Authors
Issue Date2010
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc.. The Journal's web site is located at http://www.mcponline.org/
Citation
Molecular And Cellular Proteomics, 2010, v. 9 n. 10, p. 2089-2098 How to Cite?
Abstract
Surface topography and texture of cell culture substrata can affect the differentiation and growth of adherent cells. The biochemical basis of the transduction of the physical and mechanical signals to cellular responses is not well understood. The lack of a systematic characterization of cell-biomaterial interaction is the major bottleneck. This study demonstrated the use of a novel subcellular fractionation method combined with quantitative MS-based proteomics to enable the robust and high-throughput analysis of proteins at the adherence interface of Madin-Darby canine kidney cells. This method revealed the enrichment of extracellular matrix proteins and membrane and stress fibers proteins at the adherence surface, whereas it shows depletion of extracellular matrix belonging to the cytoplasmic, nucleus, and lateral and apical membranes. The asymmetric distribution of proteins between apical and adherence sides was also profiled. Apart from classical proteins with clear involvement in cell-material interactions, proteins previously not known to be involved in cell attachment were also discovered. © 2010 by The American Society for Biochemistry and Molecular Biology, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/125188
ISSN
2013 Impact Factor: 7.254
PubMed Central ID
ISI Accession Number ID
References

 

Author Affiliations
  1. The University of Hong Kong Li Ka Shing Faculty of Medicine
  2. The University of Hong Kong
  3. City University of Hong Kong
  4. James Cook University
DC FieldValueLanguage
dc.contributor.authorTong, WYen_HK
dc.contributor.authorLiang, YMen_HK
dc.contributor.authorTam, Ven_HK
dc.contributor.authorYip, HKen_HK
dc.contributor.authorKao, YTen_HK
dc.contributor.authorCheung, KMCen_HK
dc.contributor.authorYeung, KWKen_HK
dc.contributor.authorLam, YWen_HK
dc.date.accessioned2010-10-31T11:16:28Z-
dc.date.available2010-10-31T11:16:28Z-
dc.date.issued2010en_HK
dc.identifier.citationMolecular And Cellular Proteomics, 2010, v. 9 n. 10, p. 2089-2098en_HK
dc.identifier.issn1535-9476en_HK
dc.identifier.urihttp://hdl.handle.net/10722/125188-
dc.description.abstractSurface topography and texture of cell culture substrata can affect the differentiation and growth of adherent cells. The biochemical basis of the transduction of the physical and mechanical signals to cellular responses is not well understood. The lack of a systematic characterization of cell-biomaterial interaction is the major bottleneck. This study demonstrated the use of a novel subcellular fractionation method combined with quantitative MS-based proteomics to enable the robust and high-throughput analysis of proteins at the adherence interface of Madin-Darby canine kidney cells. This method revealed the enrichment of extracellular matrix proteins and membrane and stress fibers proteins at the adherence surface, whereas it shows depletion of extracellular matrix belonging to the cytoplasmic, nucleus, and lateral and apical membranes. The asymmetric distribution of proteins between apical and adherence sides was also profiled. Apart from classical proteins with clear involvement in cell-material interactions, proteins previously not known to be involved in cell attachment were also discovered. © 2010 by The American Society for Biochemistry and Molecular Biology, Inc.en_HK
dc.languageengen_HK
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc.. The Journal's web site is located at http://www.mcponline.org/en_HK
dc.relation.ispartofMolecular and Cellular Proteomicsen_HK
dc.titleBiochemical characterization of the cell-biomaterial interface by quantitative proteomicsen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1535-9484 (Electronic) 1535-9476 (Linkin&volume=&spage=&epage=&date=2010&atitle=Biochemical+characterization+of+the+cell-biomaterial+interface+by+quantitative+proteomicsen_HK
dc.identifier.emailCheung, KMC:cheungmc@hku.hken_HK
dc.identifier.emailYeung, KWK:wkkyeung@hkucc.hku.hken_HK
dc.identifier.authorityCheung, KMC=rp00387en_HK
dc.identifier.authorityYeung, KWK=rp00309en_HK
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1074/mcp.M110.001966en_HK
dc.identifier.pmid20562470en_HK
dc.identifier.pmcidPMC2953907-
dc.identifier.scopuseid_2-s2.0-77957977633en_HK
dc.identifier.hkuros178904en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-77957977633&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume9en_HK
dc.identifier.issue10en_HK
dc.identifier.spage2089en_HK
dc.identifier.epage2098en_HK
dc.identifier.eissn1535-9484-
dc.identifier.isiWOS:000282368900001-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridTong, WY=37035246400en_HK
dc.identifier.scopusauthoridLiang, YM=35277087500en_HK
dc.identifier.scopusauthoridTam, V=35977084900en_HK
dc.identifier.scopusauthoridYip, HK=37035540600en_HK
dc.identifier.scopusauthoridKao, YT=37034292800en_HK
dc.identifier.scopusauthoridCheung, KMC=7402406754en_HK
dc.identifier.scopusauthoridYeung, KWK=13309584700en_HK
dc.identifier.scopusauthoridLam, YW=35290612300en_HK

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats