Abstract B228: A hepatocyte growth factor antagonist engineered by targeted disruption of heparan sulfate binding

@inproceedings{Cecchi2009AbstractBA,
  title={Abstract B228: A hepatocyte growth factor antagonist engineered by targeted disruption of heparan sulfate binding},
  author={Fabiola Cecchi and Deborah Pajalunga and Daniel Christopher Rabe and Andrew Fowler and Nicholas J. Macdonald and Davida K. Blackman and Stephen J. Stahl and Andrew Byrd and Donald P Bottaro},
  year={2009}
}
Hepatocyte growth factor (HGF) stimulates cell proliferation, motility, and morphogenesis upon binding to the receptor tyrosine kinase Met and cell surface heparan sulfate (HS) glycans. NK1 is a truncated HGF isoform consisting of the N‐terminal (N) and first kringle (K1) domains of full‐length HGF that stimulates all major HGF biological activities. Within NK1, the N domain contains the HS binding site, while K1 contains the primary determinants of Met binding. To further define the role of HS… CONTINUE READING