File Download
 
Links for fulltext
(May Require Subscription)
 
Supplementary

Article: Biochemical characterization of the cell-biomaterial interface by quantitative proteomics
  • Basic View
  • Metadata View
  • XML View
TitleBiochemical characterization of the cell-biomaterial interface by quantitative proteomics
 
AuthorsTong, WY2
Liang, YM3
Tam, V2
Yip, HK4
Kao, YT1
Cheung, KMC2
Yeung, KWK2
Lam, YW3
 
Issue Date2010
 
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc.. The Journal's web site is located at http://www.mcponline.org/
 
CitationMolecular And Cellular Proteomics, 2010, v. 9 n. 10, p. 2089-2098 [How to Cite?]
DOI: http://dx.doi.org/10.1074/mcp.M110.001966
 
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.
 
ISSN1535-9476
2012 Impact Factor: 7.251
2012 SCImago Journal Rankings: 2.352
 
DOIhttp://dx.doi.org/10.1074/mcp.M110.001966
 
PubMed Central IDPMC2953907
 
ISI Accession Number IDWOS:000282368900001
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorTong, WY
 
dc.contributor.authorLiang, YM
 
dc.contributor.authorTam, V
 
dc.contributor.authorYip, HK
 
dc.contributor.authorKao, YT
 
dc.contributor.authorCheung, KMC
 
dc.contributor.authorYeung, KWK
 
dc.contributor.authorLam, YW
 
dc.date.accessioned2010-10-31T11:16:28Z
 
dc.date.available2010-10-31T11:16:28Z
 
dc.date.issued2010
 
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.
 
dc.description.natureLink_to_OA_fulltext
 
dc.identifier.citationMolecular And Cellular Proteomics, 2010, v. 9 n. 10, p. 2089-2098 [How to Cite?]
DOI: http://dx.doi.org/10.1074/mcp.M110.001966
 
dc.identifier.doihttp://dx.doi.org/10.1074/mcp.M110.001966
 
dc.identifier.eissn1535-9484
 
dc.identifier.epage2098
 
dc.identifier.hkuros178904
 
dc.identifier.isiWOS:000282368900001
 
dc.identifier.issn1535-9476
2012 Impact Factor: 7.251
2012 SCImago Journal Rankings: 2.352
 
dc.identifier.issue10
 
dc.identifier.openurl
 
dc.identifier.pmcidPMC2953907
 
dc.identifier.pmid20562470
 
dc.identifier.scopuseid_2-s2.0-77957977633
 
dc.identifier.spage2089
 
dc.identifier.urihttp://hdl.handle.net/10722/125188
 
dc.identifier.volume9
 
dc.languageeng
 
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc.. The Journal's web site is located at http://www.mcponline.org/
 
dc.publisher.placeUnited States
 
dc.relation.ispartofMolecular and Cellular Proteomics
 
dc.relation.referencesReferences in Scopus
 
dc.titleBiochemical characterization of the cell-biomaterial interface by quantitative proteomics
 
dc.typeArticle
 
<?xml encoding="utf-8" version="1.0"?>
<item><contributor.author>Tong, WY</contributor.author>
<contributor.author>Liang, YM</contributor.author>
<contributor.author>Tam, V</contributor.author>
<contributor.author>Yip, HK</contributor.author>
<contributor.author>Kao, YT</contributor.author>
<contributor.author>Cheung, KMC</contributor.author>
<contributor.author>Yeung, KWK</contributor.author>
<contributor.author>Lam, YW</contributor.author>
<date.accessioned>2010-10-31T11:16:28Z</date.accessioned>
<date.available>2010-10-31T11:16:28Z</date.available>
<date.issued>2010</date.issued>
<identifier.citation>Molecular And Cellular Proteomics, 2010, v. 9 n. 10, p. 2089-2098</identifier.citation>
<identifier.issn>1535-9476</identifier.issn>
<identifier.uri>http://hdl.handle.net/10722/125188</identifier.uri>
<description.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. &#169; 2010 by The American Society for Biochemistry and Molecular Biology, Inc.</description.abstract>
<language>eng</language>
<publisher>American Society for Biochemistry and Molecular Biology, Inc.. The Journal&apos;s web site is located at http://www.mcponline.org/</publisher>
<relation.ispartof>Molecular and Cellular Proteomics</relation.ispartof>
<title>Biochemical characterization of the cell-biomaterial interface by quantitative proteomics</title>
<type>Article</type>
<identifier.openurl>http://library.hku.hk:4550/resserv?sid=HKU:IR&amp;issn=1535-9484 (Electronic) 1535-9476 (Linkin&amp;volume=&amp;spage=&amp;epage=&amp;date=2010&amp;atitle=Biochemical+characterization+of+the+cell-biomaterial+interface+by+quantitative+proteomics</identifier.openurl>
<description.nature>Link_to_OA_fulltext</description.nature>
<identifier.doi>10.1074/mcp.M110.001966</identifier.doi>
<identifier.pmid>20562470</identifier.pmid>
<identifier.pmcid>PMC2953907</identifier.pmcid>
<identifier.scopus>eid_2-s2.0-77957977633</identifier.scopus>
<identifier.hkuros>178904</identifier.hkuros>
<relation.references>http://www.scopus.com/mlt/select.url?eid=2-s2.0-77957977633&amp;selection=ref&amp;src=s&amp;origin=recordpage</relation.references>
<identifier.volume>9</identifier.volume>
<identifier.issue>10</identifier.issue>
<identifier.spage>2089</identifier.spage>
<identifier.epage>2098</identifier.epage>
<identifier.eissn>1535-9484</identifier.eissn>
<identifier.isi>WOS:000282368900001</identifier.isi>
<publisher.place>United States</publisher.place>
<bitstream.url>http://hub.hku.hk/bitstream/10722/125188/1/re01.htm</bitstream.url>
</item>
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