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Published 31 July 2006. doi:10.1083/jcb.200604035
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 174, Number 3, 323-327
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Interactions between heparan sulfate and proteins: the concept of specificity



Johan Kreuger1, Dorothe Spillmann2, Jin-ping Li2, and Ulf Lindahl2

1 Rudbeck Laboratory, Department of Genetics and Pathology, and 2 Department of Medical Biochemistry and Microbiology, Biomedical Center, Uppsala University, SE-75185 Uppsala, Sweden

Correspondence to Ulf Lindahl: Ulf.Lindahl{at}imbim.uu.se

Proteoglycan (PG) coreceptors carry heparan sulfate (HS) chains that mediate interactions with growth factors, morphogens, and receptors. Thus, PGs modulate fundamental processes such as cell survival, division, adhesion, migration, and differentiation. This review summarizes recent biochemical and genetic information that sheds new light on the nature of HS–protein binding. Unexpectedly, many interactions appear to depend more on the overall organization of HS domains than on their fine structure.

Abbreviations used in this paper: EXT, GlcA/GlcNAc transferase; GlcA, glucuronic acid; GlcNAc, N-acetylglucosamine; HS, heparan sulfate; IdoA, iduronic acid; NS, N-sulfated; PG, proteoglycan; SAS, N-sulfated/acetylated/sulfated.


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