Binding of fibronectin to human lipoproteins

Karoly Cseh, Istvan Karadi, Katalin Rischak, Lajos Szollar, Gyozo Janoki, Lajos Jakab, Laszlo Romics

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

High molecular mass adhesive glycoprotein plasma fibronectin binds to isolated HDL and LDL lipoprotein fractions in a solid phase radioimmunoassay. Mean dissociation constants of interaction of fibronectin and immobilized HDL and LDL lipoproteins isolated from eight patients with type IIa and type IV hyperlipoproteinemia are 7.8 ± 3.2 × 10-7 mol/l and 6.8 ± 2.6 × 10-7 mol/l, respectively. Fibronectin can also bind to HDL and LDL isolated from six healthy subjects with mean dissociation constants of 2.07 ± 0.45 × 10-6 mol/l and 2.25 ± 0.48 × 10-6 mol/l, respectively. The binding is not dependent on the presence of divalent cations. Fibronectinlipoprotein interaction is inhibited by soluble lipoproteins. There is no observable interaction between fibronectin and VLDL fraction. Binding of fibronectin to HDL and LDL lipoproteins can have an in vivo significance, since the interaction may play a role in the metabolism, deposition of lipoproteins into the vessel wall and in atherogenesis.

Original languageEnglish
Pages (from-to)75-85
Number of pages11
JournalClinica Chimica Acta
Volume182
Issue number1
DOIs
Publication statusPublished - Jun 15 1989

Keywords

  • Atherosclerosis
  • Fibronectin
  • Lipoprotein
  • Radioimmunoassay

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry
  • Biochemistry, medical

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    Cseh, K., Karadi, I., Rischak, K., Szollar, L., Janoki, G., Jakab, L., & Romics, L. (1989). Binding of fibronectin to human lipoproteins. Clinica Chimica Acta, 182(1), 75-85. https://doi.org/10.1016/0009-8981(89)90151-4