LDL Receptor-Related Protein 1: Unique Tissue-Specific Functions Revealed by Selective Gene Knockout Studies

Lillis, Anna P.; Van Duyn, Lauren B.; Murphy-Ullrich, Joanne E.; Strickland, Dudley K.

doi:10.1152/physrev.00033.2007

Cited by 669

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LDL Receptor-Related Protein 1: Unique Tissue-Specific Functions Revealed by Selective Gene Knockout Studies

Lillis, Anna P., Van Duyn, Lauren B., Murphy-Ullrich, Joanne E., Strickland, Dudley K.·2008·Physiological Reviews

DOI 10.1152/physrev.00033.2007PMC PMC2744109

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Abstract

The LDL receptor-related protein (originally called LRP, but now referred to as LRP1) is a large endocytic receptor that is widely expressed in several tissues. LRP1 is a member of the LDL receptor family that plays diverse roles in various biological processes including lipoprotein metabolism, degradation of proteases, activation of lysosomal enzymes, and cellular entry of bacterial toxins and viruses. Deletion of the LRP1 gene leads to lethality in mice, revealing a critical, but as of yet, undefined role in development. Tissue-specific gene deletion studies reveal an important contribution of LRP1 in the vasculature, central nervous system, macrophages, and adipocytes. Three important properties of LRP1 dictate its diverse role in physiology: 1) its ability to recognize more than 30 distinct ligands, 2) its ability to bind a large number of cytoplasmic adaptor proteins via determinants located on its cytoplasmic domain in a phosphorylation-specific manner, and 3) its ability to associate with and modulate the activity of other transmembrane receptors such as integrins and receptor tyrosine kinases.

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LRP1 belongs to the same family as LRP5 and is known to regulate crucial processes that help maintain synaptic integrity and cholesterol homeostasis in the brain.
“LRP1 belongs to the same family as LRP5 and is known to regulate crucial processes that help maintain synaptic integrity and cholesterol homeostasis in the brain.[44][45][46]”
From Canonical Wnt pathway and the LDL receptor superfamily in neuronal cholesterol homeostasis and function (2024) · cites this paper as [46]
Section II (Structural organization of LRP1; page unavailable) identifies LRP1 and LRP5 as members of the LDL receptor family. Section IX.F (Role of LRP1 in neurons, Summary; page unavailable) says a role in brain synaptic transmission is possible but not established. The paper discusses cholesterol-rich lipoprotein clearance in the liver (Section V.D), not LRP1 maintaining cholesterol homeostasis in the brain; it also does not establish that LRP1 maintains synaptic integrity. (LLM, conf=0.88)
Experimental — accuracy not yet measured
NeuN-positive neurons showed strong LRP1 expression in the soma of neurons.
“NeuNpositive neurons showed strong LRP1 expression in the soma of neurons (Figure 3A), validating high LRP1 expression in neuronal cell bodies as reported previously (28,29).”
From Endothelial LRP1 transports amyloid-β1–42 across the blood-brain barrier (2015) · cites this paper as [28]
LRP1 binds many ligands and functions in a context-dependent manner.
“LRP1 binds many ligands and is known to function in a context‐dependent manner. 40 , 41”
From Inhibition of Acyl‐CoenzymeA: Cholesterol Acyltransferase 1 promotes shedding of soluble triggering receptor on myeloid cells 2 (TREM2) and low‐density lipoprotein receptor 1 (LRP1)‐dependent phagocytosis of amyloid beta protein in microglia (2025) · cites this paper as [40]
The aspartic acid residues in each complement-type repeat can form an acidic pocket responsible for docking lysine residues on ligands.
“The aspartic acid residues in each repeat can form acidic pocket responsible for docking the lysine residues on ligands [37].”
From LRP1 is a neuronal receptor for α-synuclein uptake and spread (2022) · cites this paper as [37]

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“LRP1 is expressed in a variety of cell types in the brain and the periphery including abundant expression levels in the liver [16], largely responsible for the rapid endocytosis and subsequent elimination of peripheral Aβ [17–19].”
Background
Endothelium-specific depletion of LRP1 improves glucose homeostasis through inducing osteocalcin
Mao, H., Li, L., Fan, Q., Angelini, A., Saha, P. K., Coarfa, C., Rajapakshe, K., Perera, D., Cheng, J., Wu, H., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25673-6 · Cited by 30
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“Receptors of the LDL receptor family share a modular domain organization through the use of repetitive characteristic substructures, and are divided into a cytoplasmic and extracellular section of variable length, connected by a single-pass transmembrane domain [61].”
Background
Inhibition of Acyl‐CoenzymeA: Cholesterol Acyltransferase 1 promotes shedding of soluble triggering receptor on myeloid cells 2 (TREM2) and low‐density lipoprotein receptor 1 (LRP1)‐dependent phagocytosis of amyloid beta protein in microglia
Hovde, M. J., Maaser‐Hecker, A., Bae, J., & Tanzi, R. E. (2025) · Alzheimer's & Dementia · doi:10.1002/alz.70879 · Cited by 8

Authors: Lillis, A. P., Van Duyn, L. B., Murphy-Ullrich, J. E., & Strickland, D. K.
Venue: Physiological Reviews
Publisher: American Physiological Society
Published: 2008-07
Volume: 88
Issue: 3
Pages: 887-918
ISSN: 0031-9333
1522-1210
DOI: 10.1152/physrev.00033.2007
PMC: PMC2744109
Cited by: 669
References: 17
Language: en

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LDL Receptor-Related Protein 1: Unique Tissue-Specific Functions Revealed by Selective Gene Knockout Studies

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