Enzymatic and chemical modifications of lipoprotein(a) selectively alter its lysine-binding functions

The pathogenicity of lipoprotein(a) [Lp(a)] as a risk factor for cardiovascular disease may depend upon its lysine binding sites (LBS) which impart unique functions to Lp(a) not shared with low density lipoprotein. Biologically relevant modifications of Lp(a) were tested for alterations of LBS activ...

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Bibliographic Details
Published in:Biochimica et biophysica acta 1998-05, Vol.1392 (1), p.73-84
Main Authors: Hoover-Plow, Jane, Skocir, Pamela
Format: Article
Language:English
Subjects:
Acetylcysteine - pharmacology
Amidines - pharmacology
Binding Sites
Chromatography, Affinity
Copper Sulfate - pharmacology
Homocysteine
Homocysteine - pharmacology
Immunoassay
Lipoprotein(a)
Lipoprotein(a) - drug effects
Lipoprotein(a) - metabolism
Lysine - metabolism
Lysine-binding activity
N-Acetylcysteine
Oxidation
Oxidation-Reduction
Phospholipase A 2
Phospholipases A - pharmacology
Phospholipases A2
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Summary:The pathogenicity of lipoprotein(a) [Lp(a)] as a risk factor for cardiovascular disease may depend upon its lysine binding sites (LBS) which impart unique functions to Lp(a) not shared with low density lipoprotein. Biologically relevant modifications of Lp(a) were tested for alterations of LBS activity using two previously described functional assays, a LBS-Lp(a) immunoassay and a lysine–Sepharose bead assay. In the LBS-Lp(a) immunoassay, minimal changes in the LBS activity of Lp(a) were observed after modification with lipoprotein lipase, sphingomyelinase, or phospholipase C. In contrast, a significant ( p
ISSN:0005-2760
0006-3002
1879-145X
DOI:10.1016/S0005-2760(98)00022-8