Interactions between heparan sulfate and proteins: the concept of specificity

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...

Full description

Saved in:
Bibliographic Details
Published inThe Journal of cell biology Vol. 174; no. 3; pp. 323 - 327
Main Authors Kreuger, Johan, Spillmann, Dorothe, Li, Jin-ping, Lindahl, Ulf
Format Journal Article
LanguageEnglish
Published United States The Rockefeller University Press 31.07.2006
Rockefeller University Press
Subjects
Animals
Binding Sites
Biochemistry
Biopolymers
Biosynthesis
Cells
Endothelial cells
Enzymes
Genetics
Heparin
Heparitin Sulfate - biosynthesis
Heparitin Sulfate - chemistry
Heparitin Sulfate - metabolism
Ligands
MEDICIN
MEDICINE
Mini-Review
Phenotypes
Physiological regulation
Polymers
Protein Binding
Protein folding
Proteins - metabolism
Receptors
Reviews
Substrate Specificity
Sulfates
Online AccessGet full text

Cover

More Information
Summary: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.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
content type line 23
ObjectType-Review-1
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.
Correspondence to Ulf Lindahl: Ulf.Lindahl@imbim.uu.se
ISSN:0021-9525
1540-8140
1540-8140
DOI:10.1083/jcb.200604035