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. 2015 Jul 15;7:136. doi: 10.3389/fnagi.2015.00136

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Copyright © 2015 Ramanathan, Nelson, Sagare and Zlokovic.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution and reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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(A) The structure of LRP1. The extracellular domain consists of a heavy α-chain (515 kDa) with four ligand-binding domains. The light chain or the β-chain (85 kDa) extends into the intracellular compartment where it has two characteristic NPxY motifs involved in endocytosis and cell signaling. Proteolytic cleavage of surface-bound LRP1 yields the soluble sLRP1. (B) The three steps of LRP1-mediated Aβ clearance from brain (step 1), from blood (step 2) and from the body (step 3). For description of these three steps please see panel (B). See “Role of LRP1 in Aβ Clearance” Section for a more detailed explanation.