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Distinct patterns of apolipoprotein C-I, C-II, and C-III isoforms are associated with markers of Alzheimer’s disease
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Aβ42 levels are negatively correlated with truncated ApoC1/ApoC2 forms, suggesting greater plaque deposition.
“Aβ42 levels are negatively correlated to these truncated forms suggesting greater plaque deposition [134].”
From ApoE lipoproteins in the central nervous system under homeostasis and role in Alzheimer’s disease and related disorders (2026) · cites this paper as [134]
The proportion of truncated proteolytic fragments of ApoC1 and ApoC2 is elevated in the CSF of human APOE ε4 carriers.
“In contrast to total ApoC1 protein levels, the proportion of truncated proteolytic fragments of ApoC1 and ApoC2 were elevated in the CSF of human APOE ε4 carriers [134].”
From ApoE lipoproteins in the central nervous system under homeostasis and role in Alzheimer’s disease and related disorders (2026) · cites this paper as [134]
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Apolipoprotein E controls cerebrovascular integrity via cyclophilin A
Bell, R. D., Winkler, E. A., Singh, I., Sagare, A. P., Deane, R., Wu, Z., Holtzman, D. M., Betsholtz, C., Armulik, A., Sallstrom, J., et al. (2012) · Nature · doi:10.1038/nature11087 · Cited by 1,293 · cited 1×
“It has been shown that lipoprotein bound apoE4 does not preferentially bind to LRP1 like the other two apoE isoforms (E2 and E3), which was suggested to affect Aβ clearance (75, 76).”
BackgroundApolipoprotein E in Alzheimer’s disease and other neurological disorders
Verghese, P. B., Castellano, J. M., & Holtzman, D. M. (2011) · The Lancet Neurology · doi:10.1016/s1474-4422(10)70325-2 · Cited by 857 · cited 1×
“731 Median (IQR) 106 (57) 96 (64) 153 (115) 169 (120) 200 (50) 158 (115) CSF ApoC-II (ng/ml) 0.”
apoE isoform–specific disruption of amyloid β peptide clearance from mouse brain
Deane, R., Sagare, A., Hamm, K., Parisi, M., Lane, S., Finn, M. B., Holtzman, D. M., & Zlokovic, B. V. (2008) · Journal of Clinical Investigation · doi:10.1172/jci36663 · Cited by 771
ApoC-III inhibits clearance of triglyceride-rich lipoproteins through LDL family receptors
Gordts, P. L. S. M., Nock, R., Son, N.-H., Ramms, B., Lew, I., Gonzales, J. C., Thacker, B. E., Basu, D., Lee, R. G., Mullick, A. E., et al. (2016) · Journal of Clinical Investigation · doi:10.1172/jci86610 · Cited by 274 · cited 1×
“This could allow the lipoproteins with an affinity for these receptors, such as apoA-I and apoE, to readily bind to them (51, 52).”
BackgroundWhat are lipoproteins doing in the brain?
Wang, H., & Eckel, R. H. (2014) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2013.10.003 · Cited by 234
Wolska, A., Dunbar, R. L., Freeman, L. A., Ueda, M., Amar, M. J., Sviridov, D. O., & Remaley, A. T. (2017) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2017.10.025 · Cited by 231
Fung, K. Y., Wang, C., Nyegaard, S., Heit, B., Fairn, G. D., & Lee, W. L. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00841 · Cited by 129
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Cited by
Sorted by citations
Strickland, M. R., & Holtzman, D. M. (2026) · Molecular Neurodegeneration · doi:10.1186/s13024-026-00970-0
Metadata
- Authors
- Hu, Y., Meuret, C., Martinez, A., Yassine, H. N., & Nedelkov, D.
- Venue
- Journal of Lipid Research
- Publisher
- Elsevier BV
- Published
- 2021
- Volume
- 62
- Pages
- 100014
- ISSN
- 0022-2275
- PMC
- PMC7859854
- Cited by
- 18
- References
- 7
- Language
- en
- Funders
- National Institutes of Health (R01AG054434, R01AG055770, R01AG067063, R21AG056518)
- National Institute on Aging (P50AG05142)
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