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• W2000452941 abstract "The atherogenicity of Lp(a) is attributable to the binding of its apolipoprotein(a) component to fibrin and other plasminogen substrates. It can attenuate the activation of plasminogen, diminishing plasmin-dependent fibrinolysis and transforming growth factor-beta activation. Apolipoprotein(a) contains a major lysine-binding site in one of its kringle domains. Destroying this site by site-directed mutagenesis greatly reduces the binding of apolipoprotein(a) to lysine and fibrin. Transgenic mice expressing wild-type apolipoprotein(a) have a 5-fold increase in the development of lipid lesions, as well as a large increase in the focal deposition of apolipoprotein(a) in the aorta, compared to the lysine-binding site mutant strain and to non-transgenic litter mates. Although the adaptive function of apolipoprotein(a) remains obscure, a gene with similar structure has evolved by independent remodeling of the plasminogen twice during the course of mammalian evolution." @default.
• W2000452941 created "2016-06-24" @default.
• W2000452941 creator A5087092637 @default.
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• W2000452941 date "2008-04-23" @default.
• W2000452941 modified "2023-09-26" @default.
• W2000452941 title "The lysine-binding function of Lp(a)" @default.
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• W2000452941 doi "https://doi.org/10.1111/j.1399-0004.1997.tb04353.x" @default.
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