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. 2009 Jun 5;58(9):2018–2026. doi: 10.2337/db09-0206

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© 2009 by the American Diabetes Association.

Readers may use this article as long as the work is properly cited, the use is educational and not for profit, and the work is not altered. See http://creativecommons.org/licenses/by-nc-nd/3.0/ for details.

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FIG. 1. — Effect of apoCIII content on binding of LDL to biglycan in vitro. A: The binding of LDL isolated from patients with type 2 diabetes was analyzed using solid-phase assays for biglycan in vitro. Twelve pairs of LDL with low (●) or high (▾) LDL-apoCIII were analyzed. The low– LDL-apoCIII samples were also enriched in vitro with human apoCIII (○) so they contained approximately as much apoCIII as the high LDL-apoCIII samples, and their binding was analyzed. The dissociation constants (K_d) of the corresponding samples in each matched pair are shown. *P = 0.005, **P < 0.001. B: LDL with no apoCIII was isolated from subjects with type 2 diabetes and enriched in vitro with increasing amounts of human purified apoCIII, and LDL binding was analyzed by solid-phase assays for biglycan. C: Recombinant wild-type LDL (○) and site A mutant LDL (□) were isolated from human apoB100 transgenic mice and enriched with increasing amounts of human purified apoCIII. The LDL binding was analyzed by solid-phase assays for biglycan and is expressed as a percentage of apoCIII-free LDL binding to biglycan (means ± SD, n = 4–5). *P < 0.05 versus apoCIII-free LDL.