The interaction of human plasma glycosaminoglycans with plasma lipoproteins

Y. Nakashima, N. Di Ferrante, R. L. Jackson, Henry J. Pownall

Research output: Contribution to journalArticle

54 Scopus citations

Abstract

Modigications of existing methods have allowed for the isolation and purification of various species of plasma glycosaminoglycans on the basis of their sulfate content and molecular size. All of the preparations precipitated human plasma low density lipoproteins (LDL); maximal precipitation occurred with amounts of glycans corresponding to 50 μg of hexuronate and 12 mg of LDL. The interaction of glycans with pyrene labeled lipoproteins was also studied, measuring variations of the fluorescence emitted by the monomer (M) and excimer (E) species of the bound pyrene. The ratio I(E)/I(M) is proportional to C/eta, where c is the microscopic concentration of the pyrene confined to the hydrocarbon region of the lipoprotein and eta is the microviscosity of that region. To 0.12 mg of pyrene labeled LDL, very low density lipoproteins (VLDL) or high density lipoproteins (HDL) were added increasing amounts of the various glycan preparations. The sulfate rich species decreased the I(E)/I(M) ratio of LDL and HDL but not that of VLDL. This finding suggests that the glycan caused a change in liporotein conformation associated with either an increased volume or increased microscopic viscosity of the hydrocarbon region. The modification of LDL conformation could be prevented by proteolytic treatment of the sulfate rich species or by addition to the system of suitable amounts of sulfate poor species or of chondroitin 4 sulfate, but could not be prevented by increased ionic concentration. These results suggest that the two main species of plasma glycans are important in maintaining adequate rheological properties of plasma lipoproteins.

Original languageEnglish (US)
Pages (from-to)5386-5392
Number of pages7
JournalJournal of Biological Chemistry
Volume250
Issue number14
StatePublished - 1975

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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