Linked Life Data

15174104

Source:http://linkedlifedata.com/resource/pubmed/id/15174104

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2004-6-2
pubmed:abstractText
The covalent attachment of biomolecules onto surfaces represents a step toward the improvement of biomaterial properties by providing relevant biological signals of interest to the cell culture or tissue environment. The chemistries involved, however, often attach proteins to the surface in a random fashion, rather than the conformation or orientation most easily recognized by cells and other proteins both in vitro and in vivo. An alternative approach is to take advantage of natural interactions to both bind and orient a biomolecule "naturally," thereby enhancing its biological activity. Type 1 collagen has been shown to bind to osteopontin (OPN), a protein implicated in processes such as wound healing, endothelial cell survival, and angiogenesis. This study seeks to characterize, quantify, and exploit this interaction in order to present a more naturally recognized form of OPN to the environment surrounding a biomaterial. Binding of OPN to type 1 collagen was confirmed using Surface Plasmon Resonance (SPR). Radio-iodination of OPN showed that binding to collagen was dose-dependent and maximal in basic conditions. Principal component analysis of Time-of-Flight Secondary Ion Mass Spectrometry (ToF-SIMS) data identified differences in OPN immobilized via different techniques. Adhesion of bovine aortic endothelial cells on OPN immobilized using the affinity coating was also significantly enhanced compared to controls. Investigation into the in vivo relevance of this immobilization method is currently underway.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1549-3296
pubmed:author
pubmed:copyrightInfo
Copyright 2004 Wiley Periodicals, Inc.
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
70
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:15174104-Animals, pubmed-meshheading:15174104-Bicarbonates, pubmed-meshheading:15174104-Cattle, pubmed-meshheading:15174104-Cell Adhesion, pubmed-meshheading:15174104-Cells, Cultured, pubmed-meshheading:15174104-Coated Materials, Biocompatible, pubmed-meshheading:15174104-Collagen Type I, pubmed-meshheading:15174104-Endothelial Cells, pubmed-meshheading:15174104-Excipients, pubmed-meshheading:15174104-Imidazoles, pubmed-meshheading:15174104-Iodine Radioisotopes, pubmed-meshheading:15174104-Isotope Labeling, pubmed-meshheading:15174104-Mass Spectrometry, pubmed-meshheading:15174104-Osteopontin, pubmed-meshheading:15174104-Polyhydroxyethyl Methacrylate, pubmed-meshheading:15174104-Principal Component Analysis, pubmed-meshheading:15174104-Sialoglycoproteins, pubmed-meshheading:15174104-Surface Plasmon Resonance
pubmed:year
2004
pubmed:articleTitle
Enhancing the biological activity of immobilized osteopontin using a type-1 collagen affinity coating.
pubmed:affiliation
Department of Bioengineering, University of Washington, Seattle, Washington 98195, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.