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Papers In Press, published online ahead of print May 1, 2005
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Surgery and Physiology, University of Maryland School of Medicine, Rockville, MD 20855
Corresponding Author: strickla{at}usa.redcross.org
Apolipoprotein E (apoE) associates with lipoproteins and mediates their interaction with members of the low density lipoprotein (LDL) receptor family. ApoE exists as three common isoforms that have important distinct functional and biological properties. Two apoE isoforms, apoE3 and apoE4, are recognized by the LDL receptor, whereas apoE2 binds poorly to this receptor and is associated with type III hyperlipidemia. In addition, the apoE4 isoform is associated with the common late onset familial and sporadic forms of Alzheimer’s disease. While the interaction of apoE with the LDL receptor is well characterized, the specificity of other members of this receptor family for apoE is poorly understood. In the current investigation, we have characterized the binding of apoE to the very low density lipoprotein (VLDL) receptor and the LDL receptor-related protein (LRP). Our results indicate that like the LDL receptor, LRP prefers lipid bound forms of apoE, but in contrast to the LDL receptor, both LRP and the VLDL receptor recognize all apoE isoforms. Interestingly, the VLDL receptor does not require the association of apoE with lipid for optimal recognition and avidly binds lipid-free apoE. Likely, this receptor-dependent specificity for various apoE isoforms and for lipid-free versus lipid-bound forms of apoE is physiologically significant and is connected to distinct functions for these receptors.
Accepted on April 27, 2005
Characterization of the apoE isoform binding properties of the VLDL receptor reveal marked differences from LRP and the LDL receptor
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