Biochemistry (Moscow)

, Volume 78, Issue 7, pp 726–735

Heparan sulfate-protein binding specificity

Review

DOI: 10.1134/S0006297913070055

Cite this article as:
Nugent, M.A., Zaia, J. & Spencer, J.L. Biochemistry Moscow (2013) 78: 726. doi:10.1134/S0006297913070055

Abstract

Heparan sulfate (HS) represents a large class of linear polysaccharides that are required for the function of all mammalian physiological systems. HS is characterized by a repeating disaccharide backbone that is subject to a wide range of modifications, making this class of macromolecules arguably the most information dense in all of biology. The majority of HS functions are associated with the ability to bind and regulate a wide range of proteins. Indeed, recent years have seen an explosion in the discovery of new activities for HS where it is now recognized that this class of glycans functions as co-receptors for growth factors and cytokines, modulates cellular uptake of lipoproteins, regulates protease activity, is critical to amyloid plaque formation, is used by opportunistic pathogens to enter cells, and may even participate in epigenetic regulation. This review will discuss the current state of understanding regarding the specificity of HS-protein binding and will describe the concept that protein binding to HS depends on the overall organization of domains within HS rather than fine structure.

Key words

heparinheparan sulfateglycosaminoglycansproteoglycansprotein bindingbioinformatics

Abbreviations

ECM

extracellular matrix

FGF

fibroblast growth factor

FGFR

fibroblast growth factor receptor

HS

heparan sulfate

HSPGs

heparan sulfate proteoglycans

Copyright information

© Pleiades Publishing, Ltd. 2013

Authors and Affiliations

  1. 1.Department of BiochemistryBoston University School of MedicineBostonUSA
  2. 2.Department of OphthalmologyBoston University School of MedicineBostonUSA
  3. 3.Department of Biomedical EngineeringBoston UniversityBostonUSA