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Comparative Study
. 1994 Apr 15;269(15):11216-23.

Interaction of hepatocyte growth factor with heparan sulfate. Elucidation of the major heparan sulfate structural determinants

M Lyon  1 , J A Deakin, K Mizuno, T Nakamura, J T Gallagher
Affiliations
  • PMID: 8157651
Free article
Comparative Study

Interaction of hepatocyte growth factor with heparan sulfate. Elucidation of the major heparan sulfate structural determinants

M Lyon et al. J Biol Chem. .
Free article

Abstract

We have demonstrated by affinity chromatography that hepatocyte growth factor (HGF) binds strongly to heparan sulfate (HS). This substantiates previous suggestions that cell-surface heparan sulfate proteoglycans constitute the so-called low affinity cellular binding sites for HGF. Using a recombinant human HGF affinity column, we have analyzed the effects of various specific chemical and enzymatic modifications/depolymerizations of HS on its affinity in order to elucidate the polysaccharide structural determinants. Interaction is shown to be only slightly affected by digestion with heparinase I or III or by replacement of N-sulfates with N-acetyl groups. This suggests a specific role for sulfated domains containing nonsulfated IdceA residues, with only a small contribution from N-sulfates and IdceA(2-OSO3) residues. In addition, disaccharide analyses of various HGF-binding oligosaccharides indicate that affinity is more closely associated with 6-O-sulfation of GlcNSO3 residues than with sulfation at any other position. Although interaction can be demonstrated with heparinase III-resistant oligosaccharides as small as hexasaccharides, the highest affinity was found with oligosaccharides containing a minimum of 10-12 monosaccharides. The structural specificity of the HGF-HS interaction is thus shown to be radically different from that previously described for the basic fibroblast growth factor-HS interaction.

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