Human Apolipoprotein A-I

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Opposite regulation of human versus mouse apolipoprotein A-I by fibrates in human apolipoprotein A-I transgenic mice.

The regulation of liver apolipoprotein (apo) A-I gene expression by fibrates was studied in human apo A-I transgenic mice containing a human genomic DNA fragment driving apo A-I expression in liver. Treatment with fenofibrate (0.5% wt/wt) for 7 d increased plasma human apo A-I levels up to 750% and HDL-cholesterol levels up to 200% with a shift to larger particles. The increase in human apo A-I...

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Apolipoprotein A-I Therapy

Since 1988, with the release of the National Cholesterol Education Panel (NCEP) Adult Treatment Panel I, lowdensity lipoprotein cholesterol (LDL-C) has been the primary focus of therapy (1). Although the total cholesterol to high-density lipoprotein cholesterol (HDL-C) ratio is a better cardiovascular risk predictor (2), the consensus at the time was that the clinical evidence only supported LD...

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Human apolipoprotein A-I prevents atherosclerosis associated with apolipoprotein[a] in transgenic mice.

Elevated levels of apolipoprotein[a] (apo[a]) and apolipoprotein A-I (apoA-I) are associated, respectively, with increased and decreased atherosclerosis risk, in both humans and transgenic mice. To investigate the interactions of these two important lipid-associated proteins, we assessed the effect of expression of human apoA-I and apo[a] transgenes, both singularly and together, on murine athe...

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Human apolipoprotein A-I. Post-translational modification by covalent phosphorylation.

In vitro phosphorylation of purified human plasma apolipoprotein A-I (apoA-I) by a recently characterized Ca2+/calmodulin-dependent kinase (Beg, Z. H., Stonik, J. A., and Brewer, H. B., Jr. (1987) J. Biol. Chem. 262, 13228-13240) was time-, Ca2+-, and calmodulin-dependent. Maximal phosphorylation of human apoA-I revealed a stoichiometry of approximately 1 mol of PO4/mol of apoA-I. Phosphorylati...

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Human Apolipoprotein A-I-Derived Amyloid: Its Association with Atherosclerosis

Amyloidoses constitute a group of diseases in which soluble proteins aggregate and deposit extracellularly in tissues. Nonhereditary apolipoprotein A-I (apoA-I) amyloid is characterized by deposits of nonvariant protein in atherosclerotic arteries. Despite being common, little is known about the pathogenesis and significance of apoA-I deposition. In this work we investigated by fluorescence and...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1989

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)83518-9