A review of the unique features of HDL apoproteins |
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Authors: | Henry J Pownall Joel D Morrisett James T Sparrow Louis C Smith James Shepherd Richard L Jackson Antonio M Gotto Jr |
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Affiliation: | (1) Division of Atherosclerosis and Lipoprotein Research, Department of Medicine, Baylor College of Medicine and The Methodist Hospital, 77030 Houston, Texas |
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Abstract: | The human plasma high density lipoproteins (HDL) are a heterogeneous ensemble of five proteins associated with both neutral
and polar lipids. The sequences of all five proteins are known. ApoA-I and apoA-II are the major protein components; apoC-I,
apoC-II and apoC-III are the minor protein components. All these apoproteins spontaneously recombine with phospholipids to
give stable lipid-protein complexes and freely exchange between the two major HDL subclasses, HDL2 and HDL3. In addition, ApoC-I, apoC-II, and apoC-III exchange between HDL and very low density lipoproteins. Furthermore, certain
HDL apoproteins are activators for plasma enzymes that are important in lipid metabolism. ApoA-I and apoC-I activate lecithin/cholesterol
acyltransferase; apoC-II is an activator of lipoprotein lipase. The regions of apoC-I and apoC-II that are involved in the
activation of these enzymes have been localized with synthetic peptides. Studies of synthetic and native fragments of apoA-II,
apoC-I, apoC-II, and apoC-III as well as model lipid-binding peptides have identified specific regions with structural features
common to lipid-binding proteins. These special properties, which include helical potential, sequences with a critical amphipathic
length, and high hydrophobicity of the nonpolar side of the amphipathic helix, are the determinants of HDL structure and metabolism. |
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