Alternative splicing determines the binding of platelet-derived growth factor (PDGF-AA) to glycosaminoglycans.

@article{Lustig1996AlternativeSD,
  title={Alternative splicing determines the binding of platelet-derived growth factor (PDGF-AA) to glycosaminoglycans.},
  author={Florentyna Lustig and Johan Hoebeke and Gunnel Ostergren-Lund{\'e}n and Florence Velge-Roussel and G{\"o}ran Bondjers and Urban Olsson and U. J. R{\"u}etschi and Gunnar Fager},
  journal={Biochemistry},
  year={1996},
  volume={35 37},
  pages={12077-85}
}
We have shown previously that the platelet-derived growth factor (PDGF) and a synthetic oligopeptide, corresponding to the basic carboxyl-terminal amino acid extension of the long PDGF-A isoform, bind to heparin. Here, we have expressed the long (rA125) and the short (rA109) variants of PDGF A-chains in Escherichia coli and produced the functional homodimers. Surface plasmon resonance analyses showed that while the dimeric rA125 bound with high affinity to low molecular weight heparin, the… CONTINUE READING