Characterization of heparin and heparan sulfate domains binding to the long splice variant of platelet-derived growth factor A chain.

@article{Feyzi1997CharacterizationOH,
  title={Characterization of heparin and heparan sulfate domains binding to the long splice variant of platelet-derived growth factor A chain.},
  author={E. Feyzi and Florentyna Lustig and Gunnar Fager and Dorothe Spillmann and U lf Lindahl and Markku Salmivirta},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 9},
  pages={5518-24}
}
Platelet-derived growth factors (PDGFs) are homo- or heterodimers of two related polypeptides, known as A and B chains. The A chain exists as two splice variants due to the alternative usage of exons 6 (PDGF-AL, longer) and 7 (PDGF-AS, shorter). Exon 6 encodes an 18-amino acid sequence rich in basic amino acid residues, which has been implicated as a cell retention signal. Several lines of evidence indicate that the retention is due to binding of PDGF-AL to glycosaminoglycans, especially to… CONTINUE READING