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(Arteriosclerosis, Thrombosis, and Vascular Biology. 1997;17:2721-2728.)
© 1997 American Heart Association, Inc.

Articles

In Vitro Interactions of Oxidatively Modified LDL With Type I, II, III, IV, and V Collagen, Laminin, Fibronectin, and Poly-D-Lysine

Joachim Greilberger; Otto Schmut; ; Günther Jürgens

From the Institute for Medical Biochemistry (J.G., G.J.) and the Department for Ophthalmology (O.S.), Medical School, Karl-Franzens Universität Graz, Austria.

Correspondence to Dr Günther Jürgens, Institute for Medical Biochemistry, Harrachgasse 21, A-8010 Graz, Austria. E-mail guenther.juergens{at}bkfug.kfunigraz.ac.at

Abstract The accumulation of LDL in the arterial intima is considered a key event in atherogenesis. We investigated the binding of oxidized LDL (ox-LDL) to microtiter plates coated with type I or II collagen, laminin, fibronectin, or poly-D-lysine. Oxidation of LDL, ¹²⁵I-LDL, or Eu³⁺-LDL was performed with CuCl₂, varying the time of oxidation. Bound lipoprotein was assessed by counting radioactivity or fluorescence in the wells. Binding of highly ox-LDL in PBS followed the order: type I collagen>poly-D-lysine>type II collagen>laminin>fibronectin. Comparing various collagen types, the binding of ox-LDL followed the order: type I>type V and, type III>type IV>type II collagen. Binding of ox-LDL in PBS was dependent on an increase in negative charge of ox-LDL. Testing certain amino acids as competitors for binding of highly ox-LDL to type I collagen put lysine first, followed by arginine and histidine. On laminin, histidine competed most, followed by lysine and arginine. When studying the influence of Na⁺, K⁺, Ca²⁺, Mg²⁺ (equivalent to their concentrations in the interstitial fluid), native LDL, moderately ox-LDL, and highly ox-LDL showed the same affinity to type I collagen. However, a fivefold dilution of the buffer increased the affinity of moderately and highly ox-LDL 3.9- and 10-fold compared with native LDL. Application of the F(ab')₂ from a monoclonal antibody to ox-LDL revealed a strong competition of the binding of highly ox-LDL to type II collagen (60%), laminin (35%), type I collagen (20%), and poly-D-lysine (15%), whereas the binding to fibronectin was not affected.

Key Words: low density lipoprotein • lipid peroxidation • matrix proteins • collagen phenotypes • atherosclerosis

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