Lipoprotein receptors and cholesterol in APP trafficking and proteolytic processing, implications for Alzheimer's disease

Maria Paz Marzolo; Guojun Bu

doi:10.1016/j.semcdb.2008.10.005

Lipoprotein receptors and cholesterol in APP trafficking and proteolytic processing, implications for Alzheimer's disease

Maria Paz Marzolo, Guojun Bu

Neuroscience

Research output: Contribution to journal › Review article › peer-review

79 Scopus citations

Abstract

Amyloid-β (Aβ) peptide accumulation in the brain is central to the pathogenesis of Alzheimer's disease (AD). Aβ is produced through proteolytic processing of a transmembrane protein, β-amyloid precursor protein (APP), by β- and γ-secretases. Mounting evidence has demonstrated that alterations in APP cellular trafficking and localization directly impact its processing to Aβ. Members of the low-density lipoprotein receptor family, including LRP, LRP1B, SorLA/LR11, and apoER2, interact with APP and regulate its endocytic trafficking. Additionally, APP trafficking and processing are greatly affected by cellular cholesterol content. In this review, we summarize the current understanding of the roles of lipoprotein receptors and cholesterol in APP trafficking and processing and their implication for AD pathogenesis and therapy.

Original language	English (US)
Pages (from-to)	191-200
Number of pages	10
Journal	Seminars in Cell and Developmental Biology
Volume	20
Issue number	2
DOIs	https://doi.org/10.1016/j.semcdb.2008.10.005
State	Published - Apr 2009

Keywords

Alzheimer's disease
Amyloid precursor protein
Amyloid-β peptide
Cholesterol
Lipoprotein receptors

ASJC Scopus subject areas

Developmental Biology
Cell Biology

Access to Document

10.1016/j.semcdb.2008.10.005

Cite this

@article{25bfcce9575f433eaf86534b99c2b284,

title = "Lipoprotein receptors and cholesterol in APP trafficking and proteolytic processing, implications for Alzheimer's disease",

abstract = "Amyloid-β (Aβ) peptide accumulation in the brain is central to the pathogenesis of Alzheimer's disease (AD). Aβ is produced through proteolytic processing of a transmembrane protein, β-amyloid precursor protein (APP), by β- and γ-secretases. Mounting evidence has demonstrated that alterations in APP cellular trafficking and localization directly impact its processing to Aβ. Members of the low-density lipoprotein receptor family, including LRP, LRP1B, SorLA/LR11, and apoER2, interact with APP and regulate its endocytic trafficking. Additionally, APP trafficking and processing are greatly affected by cellular cholesterol content. In this review, we summarize the current understanding of the roles of lipoprotein receptors and cholesterol in APP trafficking and processing and their implication for AD pathogenesis and therapy.",

keywords = "Alzheimer's disease, Amyloid precursor protein, Amyloid-β peptide, Cholesterol, Lipoprotein receptors",

author = "Marzolo, {Maria Paz} and Guojun Bu",

year = "2009",

month = apr,

doi = "10.1016/j.semcdb.2008.10.005",

language = "English (US)",

volume = "20",

pages = "191--200",

journal = "Seminars in Cell and Developmental Biology",

issn = "1084-9521",

publisher = "Academic Press Inc.",

number = "2",

}

TY - JOUR

T1 - Lipoprotein receptors and cholesterol in APP trafficking and proteolytic processing, implications for Alzheimer's disease

AU - Marzolo, Maria Paz

AU - Bu, Guojun

PY - 2009/4

Y1 - 2009/4

N2 - Amyloid-β (Aβ) peptide accumulation in the brain is central to the pathogenesis of Alzheimer's disease (AD). Aβ is produced through proteolytic processing of a transmembrane protein, β-amyloid precursor protein (APP), by β- and γ-secretases. Mounting evidence has demonstrated that alterations in APP cellular trafficking and localization directly impact its processing to Aβ. Members of the low-density lipoprotein receptor family, including LRP, LRP1B, SorLA/LR11, and apoER2, interact with APP and regulate its endocytic trafficking. Additionally, APP trafficking and processing are greatly affected by cellular cholesterol content. In this review, we summarize the current understanding of the roles of lipoprotein receptors and cholesterol in APP trafficking and processing and their implication for AD pathogenesis and therapy.

AB - Amyloid-β (Aβ) peptide accumulation in the brain is central to the pathogenesis of Alzheimer's disease (AD). Aβ is produced through proteolytic processing of a transmembrane protein, β-amyloid precursor protein (APP), by β- and γ-secretases. Mounting evidence has demonstrated that alterations in APP cellular trafficking and localization directly impact its processing to Aβ. Members of the low-density lipoprotein receptor family, including LRP, LRP1B, SorLA/LR11, and apoER2, interact with APP and regulate its endocytic trafficking. Additionally, APP trafficking and processing are greatly affected by cellular cholesterol content. In this review, we summarize the current understanding of the roles of lipoprotein receptors and cholesterol in APP trafficking and processing and their implication for AD pathogenesis and therapy.

KW - Alzheimer's disease

KW - Amyloid precursor protein

KW - Amyloid-β peptide

KW - Cholesterol

KW - Lipoprotein receptors

UR - http://www.scopus.com/inward/record.url?scp=63949084694&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=63949084694&partnerID=8YFLogxK

U2 - 10.1016/j.semcdb.2008.10.005

DO - 10.1016/j.semcdb.2008.10.005

M3 - Review article

C2 - 19041409

AN - SCOPUS:63949084694

SN - 1084-9521

VL - 20

SP - 191

EP - 200

JO - Seminars in Cell and Developmental Biology

JF - Seminars in Cell and Developmental Biology

IS - 2

ER -

Lipoprotein receptors and cholesterol in APP trafficking and proteolytic processing, implications for Alzheimer's disease

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this