Isoform‐Specific Effects of Apolipoproteins E2, E3, and E4 on Cerebral Capillary Sequestration and Blood‐Brain Barrier Transport of Circulating Alzheimer's Amyloid β

Martel, Cynthia L.; Mackic, Jasmina B.; Matsubara, Etsuro; Governale, Samuel; Miguel, Calero; Miao, Wesley; McComb, J. Gordon; Frangione, Blas; Ghiso, Jorge; Zlokovic, Berislav V.

doi:10.1046/j.1471-4159.1997.69051995.x

Cited by 149Barrier Structure and Function StudiesAlzheimer's disease research and treatmentsDrug Transport and Resistance Mechanisms

Isoform‐Specific Effects of Apolipoproteins E2, E3, and E4 on Cerebral Capillary Sequestration and Blood‐Brain Barrier Transport of Circulating Alzheimer's Amyloid β

Martel, Cynthia L., Mackic, Jasmina B., Matsubara, Etsuro, Governale, Samuel, Miguel, Calero, Miao, Wesley, McComb, J. Gordon, Frangione, Blas +2 more·1997·Journal of Neurochemistry

DOI 10.1046/j.1471-4159.1997.69051995.x

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Abstract

Abstract: Cerebral capillary sequestration and blood‐brain barrier (BBB) permeability to apolipoproteins E2 (apoE2), E3 (apoE3), and E4 (apoE4) and to their complexes with sAβ 1–40, a peptide homologous to the major form of soluble Alzheimer's amyloid β, were studied in perfused guinea pig brain. Cerebrovascular uptake of three apoE isoforms was low, their blood‐to‐brain transport undetectable, but uptake by the choroid plexus significant. Binding of all three isoforms to sAβ 1–40 in vitro was similar with a KD between 11.8 and 12.9 n M. Transport into brain parenchyma and sequestration by BBB and choroid plexus were negligible for sAβ 1–40‐apoE2 and sAβ 1–40‐apoE3, but significant for sAβ 1–40‐apoE4. After 10 min, 85% of sAβ 1–40‐apoE4 taken up at the BBB remained as intact complex, whereas free sAβ 1–40 was 51% degraded. Circulating apoE isoforms have contrasting effects on cerebral capillary uptake of and BBB permeability of sAβ. ApoE2 and apoE3 completely prevent cerebral capillary sequestration and blood‐to‐brain transport of sAβ 1–40. Conversely, apoE4, by entering brain microvessels and parenchyma as a stable complex with sAβ, reduces peptide degradation and may predispose to cerebrovascular and possibly enhance parenchymal amyloid formation under pathological conditions.

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Limited blood-brain barrier permeability to circulating lipid-poor apoE2, apoE3, and apoE4 supports that apoE in blood and brain are regulated independently.
“A limited blood brain barrier permeability to circulating lipidpoor apoE2, apoE3, and apoE4 supports that apoE in blood and brain are regulated independently [72,107,108].”
From Plasma levels of apolipoprotein E, APOE genotype and risk of dementia and ischemic heart disease: A review (2016) · cites this paper as [107]
Previous work suggests a limited blood-brain barrier permeability to circulating lipid-poor apoE.
“Further, previous work suggest a limited blood–brain barrier permeability to circulating lipid-poor apoE,62”
From Plasma levels of apolipoprotein E, <i>APOE</i> genotype, and all-cause and cause-specific mortality in 105 949 individuals from a white general population cohort (2019) · cites this paper as [62]
An apoE4-Aβ complex present in the periphery is sequestered into brain capillaries to a greater extent than Aβ bound to apoE2 or apoE3, demonstrating that apoE4-mediated blood to brain transport of Aβ may play a role in amyloid accumulation in the brain.
“Finally, an apoE4-Aβ complex present in the periphery is sequestered into brain capillaries to a greater extent than Aβ bound to apoE2 or apoE3, demonstrating that apoE4-mediated blood to brain transport of Aβ may play a role in amyloid accumulation in the brain (Martel et al., 1997).”
From The role of apolipoprotein E in Alzheimer's disease (2009) · cites this paper as Martel et al., 1997

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Blood-Brain Barrier Transport of Circulating Alzheimer′s Amyloid β
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Authors: Martel, C. L., Mackic, J. B., Matsubara, E., Governale, S., Miguel, C., Miao, W., McComb, J. G., Frangione, B., Ghiso, J., & Zlokovic, B. V.
Affiliations: University of Southern California (US)
NYU Langone Health (US)
ORCID: Matsubara, Etsuro
McComb, J. Gordon
Ghiso, Jorge
Venue: Journal of Neurochemistry
Publisher: Wiley
Published: 1997-11
Volume: 69
Issue: 5
Pages: 1995-2004
ISSN: 0022-3042 (ISSN-L)
1471-4159
DOI: 10.1046/j.1471-4159.1997.69051995.x
OpenAlex: W1974008457
Cited by: 149
References: 21
Citations by year: 2026: 1 · 2025: 1 · 2024: 4 · 2023: 1 · 2022: 4 · 2021: 3 · 2020: 6 · 2019: 5 · 2018: 4 · 2017: 3 · 2016: 6 · 2015: 2 · 2014: 8 · 2013: 3 · 2012: 7
FWCI: 4.76
Type: journal article
Language: en
Open access: closed
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor, 1843 d)
Locations: Journal of Neurochemistry (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute of Neurological Disorders and Stroke (NS34467)
Topics: Life Sciences › Neuroscience › Neurology › Barrier Structure and Function Studies
Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
Keywords: apolipoprotein E isoforms, APOE2, APOE3, APOE ε4, blood-brain barrier permeability, amyloid beta degradation, amyloid deposition
MeSH terms: Amino Acid Sequence, Animals, Apolipoproteins E, Blood-Brain Barrier, Capillary Permeability, Cerebrovascular Circulation, Female, Guinea Pigs, Humans, Kinetics, Male, Molecular Sequence Data, Peptide Fragments, Perfusion, Recombinant Proteins, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Apolipoprotein E3, Apolipoprotein E4, Apolipoprotein E2

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Isoform‐Specific Effects of Apolipoproteins E2, E3, and E4 on Cerebral Capillary Sequestration and Blood‐Brain Barrier Transport of Circulating Alzheimer's Amyloid β

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