J. Lipid Res.  Neurobiology of Lipids (ISSN1683-5506)
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The Journal of Lipid Research, Vol. 39, 2373-2386, December 1998
Copyright © 1998 by Lipid Research, Inc.


Original Article

Association of apolipoprotein E with {alpha}2-macroglobulin in human plasma

Larbi Krimboua, Michel Tremblaya, Jean Davignona, and Jeffrey S. Cohna
a Hyperlipidemia and Atherosclerosis Research Group, Clinical Research Institute of Montreal, 110 Pine Avenue West, Montreal, Quebec, Canada H2W 1R7

Correspondence to: Jeffrey S. Cohn.

Apolipoprotein (apo) E plays a central role in the transport of lipids among different organs and cell types, whereas {alpha}2-macroglobulin ({alpha}2M) is responsible for the binding and inactivation of plasma proteases, as well as the transport of various cytokines, growth factors, and hormones. In the present study, evidence is presented for direct binding of apoE with {alpha}2M in human plasma, based on the observation that two-dimensional non-denaturing gradient gel electrophoretic separation of plasma resulted in co-migration of apoE with {alpha}2M in a complex intermediate in size (18.5 nm in diameter) between low (LDL) and high density lipoproteins (HDL). ApoE associated with {alpha}2M could be immunoprecipitated from plasma with anti-human {alpha}2M antiserum. Purified apoE, labeled with 125I, bound to native and methylamine-activated {alpha}2M ({alpha}2M-MA) in vitro in a time- and concentration-dependent manner. ApoE bound to {alpha}2M-MA with greater affinity than {alpha}2M. The binding of apoE to both {alpha}2M and {alpha}2M-MA did not depend on the presence of lipid. Ingestion of an oral fat load resulted in a reduction in the amount of apoE associated with {alpha}2M. Sphingomyelin vesicles and very low density lipoproteins (VLDL), but not phosphatidylcholine vesicles or HDL3, inhibited the in vitro binding of 125I-labeled apoE3 to {alpha}2M and {alpha}2M-MA. Binding of 125I-labeled apoE3 was also partially inhibited by an excess of platelet-derived growth factor and ß-amyloid protein, but not interferon-{gamma}. Subjects with an apoE 4/4 phenotype had less apoE associated with {alpha}2M in plasma than subjects with an apoE 3/3 or 2/2 phenotype, corresponding to reduced in vitro binding of apoE4 with {alpha}2M or {alpha}2M-MA.

Although the functional significance of apoE binding to {alpha}2M remains to be determined, the present results demonstrate that: 1) apoE is non-covalently bound to {alpha}2M in human plasma, 2) {alpha}2M-MA has a greater capacity to bind apoE than {alpha}2M, 3) various proteins or lipoproteins known to bind apoE or {alpha}2M can potentially affect the interaction of apoE with {alpha}2M, and 4) association of apoE with {alpha}2M or {alpha}2M-MA is dependent on apoE phenotype.—Krimbou, L., M. Tremblay, J. Davignon, and J. S. Cohn. Association of apolipoprotein E with {alpha}2-macroglobulin in human plasma. J. Lipid Res. 1998. 39: 2373–2386.

Supplementary key words: atherosclerosis, Alzheimer's disease, high density lipoprotein, LRP


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