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Cited by 126

The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.

Production and characterization of astrocyte-derived human apolipoprotein E isoforms from immortalized astrocytes and their interactions with amyloid-β

Morikawa, Masayuki, Fryer, John D., Sullivan, Patrick M., Christopher, Erin A., Wahrle, Suzanne E., DeMattos, Ronald B., O'Dell, Mark A., Fagan, Anne M., Lashuel, Hilal A., Walz, Thomas, Asai, Kiyofumi, Holtzman, David M.·2005·Neurobiology of Disease
DOI 10.1016/j.nbd.2004.11.005
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Crossref · 10.1016/j.nbd.2004.11.005

Cites

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  • ApoE2 lipoproteins secreted from astrocytes form slightly larger particles than ApoE3 and ApoE4 lipoproteins.

    “However, ApoE2 lipoproteins secreted from astrocytes form slightly larger particles than ApoE3 and ApoE4 lipoproteins [17–20].”

    From ApoE lipoproteins in the central nervous system under homeostasis and role in Alzheimer’s disease and related disorders (2026) · cites this paper as [18]

    In “Purification and size analysis of apoE-containing lipoproteins secreted by immortalized astrocytes” (page unavailable), the authors report no consistent particle-size difference between apoE isoforms or cell lines. This is contrary to the claim that astrocyte-secreted ApoE2 particles are slightly larger than ApoE3 and ApoE4 particles. (LLM, conf=0.88)

    Checked by a reasoning model — may be wrong.

    Experimental — accuracy not yet measured

  • In the central nervous system under homeostatic conditions, ApoE is primarily secreted by astrocytes, while microglia upregulate ApoE secretion under multiple disease conditions.

    “In the central nervous system (CNS), ApoE is primarily secreted by astrocytes under homeostatic conditions with microglia upregulating ApoE secretion under multiple disease conditions [18–20, 93–95].”

    From ApoE lipoproteins in the central nervous system under homeostasis and role in Alzheimer’s disease and related disorders (2026) · cites this paper as [18]

    The Introduction (page not provided) says that CNS apoE is secreted predominantly by astrocytes, supporting the first part of the claim. It identifies microglia as apoE-producing cells but does not say that they upregulate apoE secretion under disease conditions; the searched passages on microglia and disease do not establish that part. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

  • Under homeostatic conditions, ApoE is primarily produced by astrocytes which secrete lipidated ApoE.

    “Under homeostatic conditions, ApoE is primarily produced by astrocytes which secrete lipidated ApoE [17–20].”

    From ApoE lipoproteins in the central nervous system under homeostasis and role in Alzheimer’s disease and related disorders (2026) · cites this paper as [18]

  • Larger LpE secreted by astrocytes, those with a diameter of 10-17 nm, were found to associate with Aβ.

    “Larger LpE secreted by astrocytes, those with a diameter of 10–17 nm, were found to associate with Aβ [18].”

    From ApoE lipoproteins in the central nervous system under homeostasis and role in Alzheimer’s disease and related disorders (2026) · cites this paper as [18]

  • Astrocytes with human APOE isoforms knocked into the endogenous mouse Apoe allele secrete discoidal particles of overlapping size.

    “Astrocytes with human APOE isoforms knocked into the endogenous mouse Apoe allele secrete discoidal particles of overlapping size.”

    From ApoE lipoproteins in the central nervous system under homeostasis and role in Alzheimer’s disease and related disorders (2026) · cites this paper as [18]

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Citations

Cites

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Research works printed but not linked: 39

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  2. Aleshkov, 1997, Interaction of nascent apoE2, apoE3, and apoE4 isoforms expressed in mammalian cells with amyloid peptide β (1–40). Relevance to Alzheimer's disease, Biochemistry, 36, 10571, 10.1021/bi9626362 · DOI · Paper page
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  9. DeMattos, 2001, Biochemical analysis of cell-derived apoE3 particles active in stimulating neurite outgrowth, J. Lipid Res., 42, 976, 10.1016/S0022-2275(20)31622-9 · DOI
  10. DeMattos, 2004, ApoE and clusterin cooperatively suppress abeta levels and deposition: evidence that apoE regulates extracellular abeta metabolism in vivo, Neuron, 22, 193, 10.1016/S0896-6273(03)00850-X · DOI · Paper page
  11. Elshourbagy, 1985, Apolipoprotein E mRNA is abundant in the brain and adrenals, as well as in the liver, and is present in other peripheral tissues of rats and marmosets, Proc. Natl. Acad. Sci. U. S. A., 82, 203, 10.1073/pnas.82.1.203 · DOI · Paper page
  12. Evans, 1994, Apolipoprotein E is a kinetic but not a thermodynamic inhibitor of amyloid formation: implications for the pathogenesis and treatment of Alzheimer's disease, Proc. Natl. Acad. Sci. U. S. A., 92, 763, 10.1073/pnas.92.3.763 · DOI · Paper page
  13. Fagan, 2000, Differences in Aβ 40/42 ratio associated with CSF lipoproteins as a function of apoE genotype, Ann. Neurol., 48, 201, 10.1002/1531-8249(200008)48:2<201::AID-ANA10>3.0.CO;2-X · DOI
  14. Greenberg, 1995, Apolipoprotein E ɛ4 and cerebral hemorrhage associated with amyloid angiopathy, Ann. Neurol., 38, 254, 10.1002/ana.410380219 · DOI
  15. Hirsch-Reinshagen, 2004, Deficiency of ABCA1 impairs apolipoprotein E metabolism in brain, J. Biol. Chem., 279, 41197, 10.1074/jbc.M407962200 · DOI · Paper page
  16. Holtzman, 2001, Role of apoE/Aβ interactions in the pathogenesis of Alzheimer's disease and cerebral amyloid angiopathy, J. Mol. Neurosci., 17, 147, 10.1385/JMN:17:2:147 · DOI · Paper page
  17. Holtzman, 2000, Apolipoprotein E isoform-dependent amyloid deposition and neuritic degeneration in a mouse model of Alzheimer's disease, Proc. Natl. Acad. Sci. U. S. A., 97, 2892, 10.1073/pnas.050004797 · DOI · Paper page
  18. Knouff, 1999, Apo E structure determines VLDL clearance and atherosclerosis risk in mice, J. Clin. Invest., 103, 1579, 10.1172/JCI6172 · DOI · Paper page
  19. Krul, 1988, Heterogeneity of apolipoprotein E epitope expression on human lipoproteins: importance for apolipoprotein E function, J. Lipid Res., 29, 1309, 10.1016/S0022-2275(20)38434-0 · DOI · Paper page
  20. LaDu, 1995, Purification of apolipoprotein E attenuates isoform-specific binding to β-amyloid, J. Biol. Chem., 270, 9030, 10.1074/jbc.270.16.9039 · DOI · Paper page
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Metadata

Authors
Morikawa, M., Fryer, J. D., Sullivan, P. M., Christopher, E. A., Wahrle, S. E., DeMattos, R. B., O'Dell, M. A., Fagan, A. M., Lashuel, H. A., Walz, T., Asai, K., & Holtzman, D. M.
Venue
Neurobiology of Disease
Publisher
Elsevier BV
Published
2005-06
Volume
19
Issue
1-2
Pages
66-76
ISSN
0969-9961
DOI
10.1016/j.nbd.2004.11.005
Cited by
126
References
19
Language
en
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)

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