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Journal of Lipid Research, Vol. 40, 1925-1930, October 1999
Copyright © 1999 by Lipid Research, Inc.

Rapid Communication

Identification and characterization of LRP8 (apoER2) in human blood platelets

David R. Riddella, Dimitri V. Vinogradova, Anita K. Stannarda, Nicholas Chadwicka, and James S. Owena
a Department of Medicine, Royal Free and University College Medical School, University College London, Royal Free Campus, London NW3 2PF, United Kingdom

Correspondence to: James S. Owen

Recently, we reported that apoE inhibits platelet reactivity by stimulating NO release and postulated apoE-receptor activation of intracellular NO synthase (eNOS). Here, we implicate a low density lipoprotein receptor (LDL-R) family member by studying ligand requirements using purified apoE isoforms, synthetic peptides, and the receptor antagonist, receptor-associated protein (RAP). Then, using a homology cloning approach and degenerate PCR primers to amplify the conserved Cys-rich binding domain of the LDL-R family, this receptor was identified as LRP8 (formerly termed, apoER2), a newly described brain protein with several splice variants. Immunoprecipitation of platelet membranes with anti-peptide antisera confirmed protein expression, while analysis of RNA from platelets and two megakaryocytic cell lines (Meg-01 and HEL) disclosed that the major LRP8 transcript lacked binding repeats 4;–6 (LRP8{Delta}4;–6) but contained the full-length cytoplasmic tail.

Sequence analysis of cytoplasmic LRP8 revealed several peptide motifs with potential for cellular signaling and we propose this as a rational mechanism through which apoE inhibits platelet aggregation.—Riddell, D. R., D. V. Vinogradov, A. K. Stannard, N. Chadwick, and J. S. Owen. Identification and characterization of LRP8 (apoER2) in human blood platelets. J. Lipid Res. 1999. 40: 1925;–1930.

Supplementary key words: apolipoprotein E, apolipoprotein E receptor 2, intracellular signalling, LDL-receptor family, nitric oxide, platelet aggregation


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