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J Biol Chem, Vol. 273, Issue 22, 13395-13398, May 29, 1998

COMMUNICATION
Age-dependent Modulation of Heparan Sulfate Structure and Function

Emadoldin Feyzi, Tom Saldeen^§, Erik Larsson^¶, Ulf Lindahl, and Markku Salmivirta

From the Departments of  Medical Biochemistry and Microbiology, ^§ Surgery and ^¶ Genetics and Pathology, Uppsala University, S-75123 Uppsala, Sweden

Heparan sulfate interacts with growth factors, matrix components, effectors and modulators of enzymatic catalysis as well as with microbial proteins via sulfated oligosaccharide domains. Although a number of such domains have been characterized, little is known about the regulation of their formation in vivo. Here we show that the structure of human aorta heparan sulfate is gradually modulated during aging in a manner that gives rise to markedly enhanced binding to isoforms of platelet-derived growth factor A and B chains containing polybasic cell retention sequences. By contrast, the binding to fibroblast growth factor 2 is affected to a much lesser extent. The enhanced binding of aorta heparan sulfate to platelet-derived growth factor is suggested to be due to an age-dependent increase of GlcN 6-O-sulfation, resulting in increased abundance of the trisulfated L-iduronic acid (2-OSO₃)-GlcNSO₃(6-OSO₃) disaccharide unit. Such units have been shown to hallmark the platelet-derived growth factor A chain-binding site in heparan sulfate.

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Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.

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