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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2009-2-16
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pubmed:abstractText |
Poly-N-acetyllactosamine (poly-LacNAc) structures have been identified as important ligands for galectin-mediated cell adhesion to extra-cellular matrix (ECM) proteins. We here present the biofunctionalization of surfaces with poly-LacNAc structures and subsequent binding of ECM glycoproteins. First, we synthesized beta-GlcNAc glycosides carrying a linker for controlled coupling onto chemically functionalized surfaces. Then we produced poly-LacNAc structures with defined lengths using human beta1,4-galactosyltransferase-1 and beta1,3-N-acetylglucosaminyltransferase from Helicobacter pylori. These compounds were also used for kinetic characterization of glycosyltransferases and lectin binding assays. A mixture of poly-LacNAc-structures covalently coupled to functionalized microtiter plates were identified for best binding to our model galectin His(6)CGL2. We further demonstrate for the first time that these poly-LacNAc surfaces are suitable for further galectin-mediated binding of the ECM glycoproteins laminin and fibronectin. This new technology should facilitate cell adhesion to biofunctionalized surfaces by imitating the natural ECM microenvironment.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetylglucosamine,
http://linkedlifedata.com/resource/pubmed/chemical/Biocompatible Materials,
http://linkedlifedata.com/resource/pubmed/chemical/CGL2 protein, Coprinus cinereus,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Galactosyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Galectin 2,
http://linkedlifedata.com/resource/pubmed/chemical/Galectins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosides,
http://linkedlifedata.com/resource/pubmed/chemical/N-Acetylglucosaminyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/beta1,4-galactosyltransferase ...,
http://linkedlifedata.com/resource/pubmed/chemical/poly-N-acetyllactosamine
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1573-4986
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
26
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
141-59
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pubmed:meshHeading |
pubmed-meshheading:18758940-Acetylglucosamine,
pubmed-meshheading:18758940-Biocompatible Materials,
pubmed-meshheading:18758940-Extracellular Matrix,
pubmed-meshheading:18758940-Fungal Proteins,
pubmed-meshheading:18758940-Galactosyltransferases,
pubmed-meshheading:18758940-Galectin 2,
pubmed-meshheading:18758940-Galectins,
pubmed-meshheading:18758940-Glycoproteins,
pubmed-meshheading:18758940-Glycosides,
pubmed-meshheading:18758940-Humans,
pubmed-meshheading:18758940-N-Acetylglucosaminyltransferases,
pubmed-meshheading:18758940-Polysaccharides
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pubmed:year |
2009
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pubmed:articleTitle |
Chemo-enzymatic synthesis of poly-N-acetyllactosamine (poly-LacNAc) structures and their characterization for CGL2-galectin-mediated binding of ECM glycoproteins to biomaterial surfaces.
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pubmed:affiliation |
Institute of Biotechnology and Helmholtz-Institute for Biomedical Engineering, RWTH Aachen University, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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