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The synergy site of fibronectin is required for strong interaction with the platelet integrin alphaIIbbeta3. | LitMetric

The synergy site of fibronectin is required for strong interaction with the platelet integrin alphaIIbbeta3.

Ann Biomed Eng

Department of Chemical, Biological, and Materials Engineering, University of Oklahoma, Norman, 73019-1004, USA.

Published: October 2006

AI Article Synopsis

  • Integrins are important cell adhesion molecules that typically bind to ligands with the RGD peptide sequence, but other nearby sites also play a crucial role in this binding.
  • Researchers used site-directed mutagenesis to investigate which specific amino acids in the protein fibronectin affect its binding to the platelet integrin alphaIIbbeta3.
  • They found that changes to certain amino acids, including the one in the RGD sequence, significantly reduced platelet adhesion, indicating that optimal binding requires both the RGD region and additional amino acids that are located further away.

Article Abstract

Integrins are a class of cell adhesion molecules that bind to ligands containing the RGD peptide sequence. There is increasing evidence that peptide sites other than the RGD site are required for optimal binding of integrins with their ligands. We have examined the sites on the protein fibronectin that are needed for optimal binding to the platelet integrin alphaIIbbeta3 using a strategy of site directed mutagenesis. Single amino acids near the RGD site or near the synergy site of fibronectin were mutated and the resultant proteins were expressed in a bacterial expression system. The purified protein was coated onto glass cover slips. Platelets, expressing alphaIIbbeta3 were perfused over the surface at physiologically relevant shear rates and the extent of adhesion was quantified. We found that the single amino acid substitution of the aspartic acid in the RGD sequence, D1495A, completely abolished adhesion. Surprisingly, the mutants R1445A and R1448Q that are near the RGD site also abolished adhesion of platelets under flow. Additionally, the synergy site mutants R1371A, R1374Q, or R1379A displayed only minimal adhesion of platelets. These results show that the binding site for alphaIIbbeta3 on fibronectin extends over a considerable distance from the RGD site and that these distant sites are required for optimal attachment of cells in the presence of physiologically relevant shear stress.

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Source
http://dx.doi.org/10.1007/s10439-006-9161-1DOI Listing

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