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Glycobiology Advance Access published online on January 12, 2004
Glycobiology, doi:10.1093/glycob/cwh051
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Submitted on July 3, 2003
Accepted on December 19, 2003

© 2004 Oxford University Press

REVIEW

Interactions of heparin/heparan sulfate with proteins: appraisal of structural factors and experimental approaches

Andrew K. Powell 1*, Edwin A. Yates 1, David G. Fernig 1, and Jeremy E. Turnbull 1

1 School of Biological Sciences, Biosciences Building, University of Liverpool, Crown Street, Liverpool, L69 7ZB, UK

* To whom correspondence should be addressed. E-mail: andrew_k_powell{at}yahoo.co.uk.

Abstract

Over the past decade the glycosaminoglycans heparin and heparan sulfate have been shown to bind and regulate the activities of many proteins. Established techniques have provided both qualitative and quantitative information regarding these interactions leading to a general view that proteins bind with a variety of affinities to particular sequences within heparin or heparan sulfate chains. The mechanism by which heparan sulfate regulates the activity of proteins through such interactions has, however, proved more elusive. Here, we survey some relevant details of the structural characteristics of heparin/heparan sulfate and the approaches used to investigate their interactions with proteins. For the latter, the interactions of heparin/heparan sulfate with fibroblast growth factors and their receptors will be emphasised, since these proteins have been the subject of many studies. We reflect upon the information that various techniques have provided, points regarding their use and some relevant theoretical considerations regarding the study of protein-heparin/heparan sulfate interactions. A perspective of new and developing approaches, which may aid advances in this field, is also provided.


interaction, protein, heparan sulfate, heparin, FGF
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