Covalent cross-linking of fibronectin to fibrin is required for maximal cell adhesion to a fibronectin-fibrin matrix.

@article{Corbett1997CovalentCO,
  title={Covalent cross-linking of fibronectin to fibrin is required for maximal cell adhesion to a fibronectin-fibrin matrix.},
  author={Siobhan A. Corbett and Lihsueh Lee and Carole L. Wilson and Jean E. Schwarzbauer},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 40},
  pages={24999-5005}
}
In a blood clot, fibrin and plasma fibronectin (pFN) are covalently cross-linked by activated factor XIII (factor XIIIa) to form pFN-fibrin multimers. To determine the functional significance of covalent pFN-fibrin interactions, we have developed an in vitro model which allows the incorporation of recombinant FN (recFN) molecules into a covalently cross-linked recFN-fibrin matrix. Using the baculovirus expression system, we have expressed recFN monomers composed of the amino-terminal 70-kDa… CONTINUE READING

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