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LDL receptor-related protein, a multifunctional ApoE receptor, binds secreted β-amyloid precursor protein and mediates its degradation

Kounnas, Maria Z, Moir, Robert D, Rebeck, G.William, Bush, Ashley I, Argraves, W.Scott, Tanzi, Rudolph E, Hyman, Bradley T, Strickland, Dudley K·1995·Cell
DOI 10.1016/0092-8674(95)90320-8
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Abstract

The secreted form of beta-amyloid precursor protein (APP) containing the Kunitz proteinase inhibitor (KPI) domain, also called protease nexin II, is internalized and degraded by cells. We show that the low density lipoprotein (LDL) receptor-related protein (LRP) is responsible for the endocytosis of secreted APP. APPs770 degradation is inhibited by an LRP antagonist called the receptor-associated protein (RAP) and by LRP antibodies and is greatly diminished in fibroblasts genetically deficient in LRP. APPs695, which lacks the KPI domain, is a poor LRP ligand. Since LRP also binds apolipoprotein E (apoE)-enriched lipoproteins and inheritance of the epsilon 4 allele of the apoE gene is a risk factor for Alzheimer's disease (AD), these data link in a single metabolic pathway two molecules strongly implicated in the pathophysiology of AD.

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Metadata

Authors
Kounnas, M. Z., Moir, R. D., Rebeck, G. W., Bush, A. I., Argraves, W. S., Tanzi, R. E., Hyman, B. T., & Strickland, D. K.
Venue
Cell
Publisher
Elsevier BV
Published
1995-07
Volume
82
Issue
2
Pages
331-340
ISSN
0092-8674
DOI
10.1016/0092-8674(95)90320-8
Cited by
401
References
3
Language
en
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