| pubmed-article:12220083 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12220083 | lifeskim:mentions | umls-concept:C0069676 | lld:lifeskim |
| pubmed-article:12220083 | lifeskim:mentions | umls-concept:C1749467 | lld:lifeskim |
| pubmed-article:12220083 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:12220083 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:12220083 | pubmed:dateCreated | 2002-9-10 | lld:pubmed |
| pubmed-article:12220083 | pubmed:abstractText | Osteopontin (OPN) is an extracellular matrix protein found in bones and teeth, where it accumulates at matrix-matrix interfaces. We postulate that OPN interacts homotypically and heterotypically in the adhesion of apposing matrices. Using suspensions of OPN-coupled aldehyde/sulfate latex spheres, we measured the strength of homotypic OPN-OPN binding in vitro. Doublets formed through shear-induced collisions in a cone and plate rheoscope were subjected to shear stresses >0.6 Nm(-2) and the fraction broken up determined over 60 s. Rapid initial breakup of 35% of doublets was followed by very slow breakup of the remaining 65%. Monte Carlo simulation of the breakup kinetics pointed to the existence of low and high bond strength populations of doublets. Dynamic light scattering spectroscopy of soluble OPN showed that 27% by mass existed as dimers. We postulate that OPN dimers binding to monomers account for the low strength bonds since a strong bond has already formed between the molecules of the dimer. In contrast, OPN-OPN monomer bonds had higher tensile strength than bonds between the high-affinity interaction of IgG and protein G, previously studied. Antibody blocking studies showed that the self-binding region of OPN resides in the C-terminus. These data suggest that homotypic OPN-OPN bonds have physiologically significant strength, supporting the hypothesis that OPN-OPN binding and self-assembly participate in adhesion within mineralized tissues. | lld:pubmed |
| pubmed-article:12220083 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12220083 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12220083 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12220083 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12220083 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12220083 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12220083 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12220083 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12220083 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:12220083 | pubmed:issn | 0090-6964 | lld:pubmed |
| pubmed-article:12220083 | pubmed:author | pubmed-author:GoldsmithH... | lld:pubmed |
| pubmed-article:12220083 | pubmed:author | pubmed-author:MäenpääP HPH | lld:pubmed |
| pubmed-article:12220083 | pubmed:author | pubmed-author:McKeeM DMD | lld:pubmed |
| pubmed-article:12220083 | pubmed:author | pubmed-author:McIntoshF AFA | lld:pubmed |
| pubmed-article:12220083 | pubmed:author | pubmed-author:KaartinenM... | lld:pubmed |
| pubmed-article:12220083 | pubmed:author | pubmed-author:LabrosseJ MJM | lld:pubmed |
| pubmed-article:12220083 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12220083 | pubmed:volume | 30 | lld:pubmed |
| pubmed-article:12220083 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12220083 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12220083 | pubmed:pagination | 840-50 | lld:pubmed |
| pubmed-article:12220083 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:12220083 | pubmed:meshHeading | pubmed-meshheading:12220083... | lld:pubmed |
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| pubmed-article:12220083 | pubmed:meshHeading | pubmed-meshheading:12220083... | lld:pubmed |
| pubmed-article:12220083 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12220083 | pubmed:articleTitle | Homotypic interactions of soluble and immobilized osteopontin. | lld:pubmed |
| pubmed-article:12220083 | pubmed:affiliation | Department of Medicine, Montreal General Hospital, Montreal, QC, Canada. | lld:pubmed |
| pubmed-article:12220083 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12220083 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:12220083 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
