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Sequence analysis of heparan sulfate epitopes with graded affinities for fibroblast growth factors 1 and 2 (Articolo in rivista)

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Sequence analysis of heparan sulfate epitopes with graded affinities for fibroblast growth factors 1 and 2 (Articolo in rivista) (literal)

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J.Kreuger, M.Salmivirta, L.Sturiale, G.Gimenez-Gallego, U.Lindahl (2001)
Sequence analysis of heparan sulfate epitopes with graded affinities for fibroblast growth factors 1 and 2
in The Journal of biological chemistry (Print); AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, BETHESDA (Stati Uniti d'America)
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Uppsala Univ, Dept Med Biochem & Micorbiol, S-75123 Uppsala, Sweden Abo Akad Univ, FIN-20521 Turku, Finland Univ Turku, Turku Ctr Biotechnol, FIN-20521 Turku, Finland BioTic Therapies Corp, FIN-20520 Turku, Finland G Ronzoni Inst Chem & Biochem Res, I-20133 Milan, Italy CSIC, Ctr Invest Biol, E-28006 Madrid, Spain (literal)

Titolo

Sequence analysis of heparan sulfate epitopes with graded affinities for fibroblast growth factors 1 and 2 (literal)

Abstract

Proteins that belong to the fibroblast growth factor (FGF) family regulate proliferation, migration, and differentiation of many cell types. Several FGFs, including the prototype factors FGF-1 and FGF-2, depend on interactions with heparan sulfate (HS) proteoglycans for activity. We have assessed tissue-derived HS fragments for binding to FGF-1 and FGF-2 to identify the authentic saccharide motifs required for interactions. Sequence information on a range of N-sulfated HS octasaccharides spanning from low to high affinity for FGF-1 was obtained. All octasaccharides with high affinity for FGF-1 (greater than or equal to0.5 m NaCl required for elution) contained an internal IdoUA(2-OSO3)-GlcNSO(3)(6-OSO3)-IdoUA(2-OSO3)-trisaccharide motif. Octasaccharides with a higher overall degree of sulfation but lacking the specific trisaccharide motif showed lower affinity for FGF-1. FGF-2 was shown to bind to a mono-O-sulfated HS 6-mer carrying a single internal IdoUA(2-OSO3)-unit. However, a di-O-sulfated -IdoUA(2-OSO3)-GlcNSO(3)-IdoUA(2-OSO3)-trisaccharide sequence within a HS 8-mer gave stronger binding. These findings show that not only the number but also the positions of individual sulfate groups determine affinity of HS for FGFs. Our findings support the notion that FGF-dependent processes can be modulated in vivo by regulated expression of distinct HS sequences. (literal)

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