The function of multiple extracellular matrix receptors in mediating cell adhesion to extracellular matrix: preparation of monoclonal antibodies to the fibronectin receptor that specifically inhibit cell adhesion to fibronectin and react with platelet glycoproteins Ic-IIa

@article{Wayner1988TheFO,
  title={The function of multiple extracellular matrix receptors in mediating cell adhesion to extracellular matrix: preparation of monoclonal antibodies to the fibronectin receptor that specifically inhibit cell adhesion to fibronectin and react with platelet glycoproteins Ic-IIa},
  author={Elizabeth A. Wayner and William Gene Carter and Radoslaw Piotrowicz and Thomas J. Kunicki},
  journal={The Journal of Cell Biology},
  year={1988},
  volume={107},
  pages={1881 - 1891}
}
We have identified monoclonal antibodies that inhibit human cell adhesion to collagen (P1H5), fibronectin (P1F8 or P1D6), and collagen and fibronectin (P1B5) that react with a family of structurally similar glycoproteins referred to as extracellular matrix receptors (ECMRs) II, VI, and I, respectively. Each member of this family contains a unique alpha subunit, recognized by the antibodies, and a common beta subunit, each of approximately 140 kD. We show here that ECMR VI is identical to the… CONTINUE READING
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The role of intermolecular disulfide bonding in deposition of GP140 in the extracellular matrix

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