Binding of fibronectin to human lipoproteins

Clinica Chimica Acta; International Journal of Clinical Chemistry
K CsehL Romics

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 X 10(-7) mol/l and 6.8 +/- 2.6 X 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 X 10(-6) mol/l and 2.25 +/- 0.48 X 10(-6) mol/l, respectively. The binding is not dependent on the presence of divalent cations. Fibronectin-lipoprotein 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.

References

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Citations

May 1, 1995·Arteriosclerosis, Thrombosis, and Vascular Biology·K J Williams, I Tabas
Jun 19, 2012·Cellular & Molecular Biology Letters·Shigeki KamitaniKohji Hanasaki
Mar 1, 1991·Arteriosclerosis and Thrombosis : a Journal of Vascular Biology·H RobenekN J Severs
Nov 6, 1998·The Journal of Experimental Medicine·H ChenH Metzger

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