Cellular and Molecular Life Sciences CMLS

, Volume 56, Issue 9–10, pp 857–870

Cell surface heparan sulfate proteoglycans and lipoprotein metabolism

  • S. O. Kolset
  • M. Salmivirta

DOI: 10.1007/s000180050031

Cite this article as:
Kolset, S. & Salmivirta, M. CMLS, Cell. Mol. Life Sci. (1999) 56: 857. doi:10.1007/s000180050031

Abstract.

Cell surface heparan sulfate proteoglycans are involved in several aspects of the lipoprotein metabolism. Most of the biological activities of these proteoglycans are mediated via interactions of their heparan sulfate moieties with various protein ligands, including lipoproteins and lipases. The binding of lipoproteins to heparan sulfate is largely determined by their apoprotein composition, and apoproteins B and E display the highest affinity for heparan sulfate. Interactions of lipoproteins with heparan sulfate are important for the cellular uptake and turnover of lipoproteins, in part by enhancing the accessibility of lipoproteins to lipoprotein receptors and lipases. Apoprotein B may interact with receptors without involving heparan sulfate. Heparan sulfate has been further implicated in presentation and stabilization of lipoprotein lipase and hepatic lipase on cell surfaces and in the transport of lipoprotein lipase from extravascular cells to the luminal surface of the endothelia. In atherosclerosis, heparan sulfate is intimately involved in several events important to the pathophysiology of the disease. Heparan sulfate thus binds and regulates the activity of growth factors, cytokines, superoxide dismutase and antithrombin, which contribute to aberrant cell proliferation, migration and matrix production, scavenging of reactive oxygen radicals and thrombosis. In this review we discuss the various roles of heparan sulfate proteoglycans in vascular biology, with emphasis on interactions of heparan sulfate with lipoproteins and lipases and the molecular basis of such interactions.

Key words. Heparan sulfate; lipoproteins; atherosclerosis; lipases; apoproteins; proteoglycans. 

Copyright information

© Birkhäuser Verlag Basel, 1999

Authors and Affiliations

  • S. O. Kolset
    • 1
  • M. Salmivirta
    • 2
  1. 1.Institute for Nutrition Research, University of Oslo, Box 1046 Blindern, 0316 Oslo (Norway), Fax +47 22851512, e-mail: s.o.kolset@basalmed.uio.noNO
  2. 2.Department of Medical Biochemistry and Microbiology, Uppsala University, Biomedical Center, P.O. Box 575, S-75123 Uppsala (Sweden)SE

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