Source:http://linkedlifedata.com/resource/pubmed/id/15299021
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
43
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pubmed:dateCreated |
2004-10-18
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pubmed:abstractText |
Surface presentation of adhesion receptors influences cell adhesion, although the mechanisms underlying these effects are not well understood. We used a micropipette adhesion frequency assay to quantify how the molecular orientation and length of adhesion receptors on the cell membrane affected two-dimensional kinetic rates of interactions with surface ligands. Interactions of P-selectin, E-selectin, and CD16A with their respective ligands or antibody were used to demonstrate such effects. Randomizing the orientation of the adhesion receptor or lowering its ligand- and antibody-binding domain above the cell membrane lowered two-dimensional affinities of the molecular interactions by reducing the forward rates but not the reverse rates. In contrast, the soluble antibody bound with similar three-dimensional affinities to cell-bound P-selectin constructs regardless of their orientation and length. These results demonstrate that the orientation and length of an adhesion receptor influences its rate of encountering and binding a surface ligand but does not subsequently affect the stability of binding.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/E-Selectin,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/P-Selectin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, IgG
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
22
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pubmed:volume |
279
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
44915-23
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:15299021-Animals,
pubmed-meshheading:15299021-Antibodies, Monoclonal,
pubmed-meshheading:15299021-CHO Cells,
pubmed-meshheading:15299021-Cell Adhesion,
pubmed-meshheading:15299021-Cell Line, Tumor,
pubmed-meshheading:15299021-Cricetinae,
pubmed-meshheading:15299021-Dose-Response Relationship, Drug,
pubmed-meshheading:15299021-E-Selectin,
pubmed-meshheading:15299021-Erythrocytes,
pubmed-meshheading:15299021-HL-60 Cells,
pubmed-meshheading:15299021-Humans,
pubmed-meshheading:15299021-Kinetics,
pubmed-meshheading:15299021-Ligands,
pubmed-meshheading:15299021-Models, Biological,
pubmed-meshheading:15299021-Models, Chemical,
pubmed-meshheading:15299021-P-Selectin,
pubmed-meshheading:15299021-Protein Binding,
pubmed-meshheading:15299021-Protein Structure, Tertiary,
pubmed-meshheading:15299021-Receptors, IgG,
pubmed-meshheading:15299021-Time Factors
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pubmed:year |
2004
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pubmed:articleTitle |
Quantifying the effects of molecular orientation and length on two-dimensional receptor-ligand binding kinetics.
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pubmed:affiliation |
National Microgravity Laboratory, Institute of Mechanics, Chinese Academy of Sciences, Beijing 100080, China.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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