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Characterization and functional studies of lipoproteins, lipid transfer proteins, and lecithin: cholesterol acyltransferase in CSF of normal individuals and patients with Alzheimer's disease.

(2000) JOURNAL OF LIPID RESEARCH. 41(6). p.963-974
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Abstract
We investigated the lipoprotein distribution and composition in cerebrospinal fluid (CSF) in a group of patients with Alzheimer's disease (AD) or affected by other types of dementia in comparison to non-demented controls. We found slightly decreased apolipoprotein (apo)E and cholesterol concentrations in CSF of AD patients and moderately increased apoA-I concentrations, while in patients suffering from other types of dementia the apoA-I CSF concentration was increased. ApoA-IV concentrations varied widely in human CSF, but were not associated with any clinical condition. HDL2-like apoE-containing lipoproteins represent the major lipoprotein fraction. In CSF of normal controls, only a minor HDL3-like apoA-I-containing lipoprotein fraction was observed; this fraction was more prevalent in AD patients. ApoA-II was recovered mostly in the HDL3 density range, while apoA-IV was not associated with lipoproteins but appeared in a lipid-free form, co-localizing with LCAT immunoreactivity Bi-dimensional analysis demonstrated pre-beta and alpha apoA-I-containing particles; apoE and apoA-II: were detected only in alpha-migrating particles. ApoA-IV distributed both to pre-P and gamma-migrating particles; the LCAT signal was co-localized in this gamma-migrating fraction. Enzymatically active LCAT tvas present in human CSF as well as PLTP activity and mass; no CETP mass was detected. In CSF from AD patients, LCAT activity was 50% lower than in CSF from normal controls. CSF lipoproteins induced a significant cholesterol efflux from cultured rat astrocytes, suggesting that they play an active role in maintaining the cholesterol homeostasis in brain cells.
Keywords
cerebrospinal fluid, lipoproteins, Alzheimer's disease, cholesterol, efflux, HUMAN CEREBROSPINAL-FLUID, AMYLOID PRECURSOR PROTEIN, HIGH-DENSITY-LIPOPROTEIN, ESTER TRANSFER PROTEIN, APOLIPOPROTEIN-A-IV, IN-VITRO, CODON-360 MUTATION, E POLYMORPHISM, BETA-PROTEIN, HUMAN BRAIN

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Citation

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Chicago
Demeester, Nathalie, G Castro, C Desrumaux, C De Geitere, JC Fruchart, Patrick Santens, E Mulleners, et al. 2000. “Characterization and Functional Studies of Lipoproteins, Lipid Transfer Proteins, and Lecithin: Cholesterol Acyltransferase in CSF of Normal Individuals and Patients with Alzheimer’s Disease.” Journal of Lipid Research 41 (6): 963–974.
APA
Demeester, N., Castro, G., Desrumaux, C., De Geitere, C., Fruchart, J., Santens, P., Mulleners, E., et al. (2000). Characterization and functional studies of lipoproteins, lipid transfer proteins, and lecithin: cholesterol acyltransferase in CSF of normal individuals and patients with Alzheimer’s disease. JOURNAL OF LIPID RESEARCH, 41(6), 963–974.
Vancouver
1.
Demeester N, Castro G, Desrumaux C, De Geitere C, Fruchart J, Santens P, et al. Characterization and functional studies of lipoproteins, lipid transfer proteins, and lecithin: cholesterol acyltransferase in CSF of normal individuals and patients with Alzheimer’s disease. JOURNAL OF LIPID RESEARCH. 2000;41(6):963–74.
MLA
Demeester, Nathalie, G Castro, C Desrumaux, et al. “Characterization and Functional Studies of Lipoproteins, Lipid Transfer Proteins, and Lecithin: Cholesterol Acyltransferase in CSF of Normal Individuals and Patients with Alzheimer’s Disease.” JOURNAL OF LIPID RESEARCH 41.6 (2000): 963–974. Print.
@article{127640,
  abstract     = {We investigated the lipoprotein distribution and composition in cerebrospinal fluid (CSF) in a group of patients with Alzheimer's disease (AD) or affected by other types of dementia in comparison to non-demented controls. We found slightly decreased apolipoprotein (apo)E and cholesterol concentrations in CSF of AD patients and moderately increased apoA-I concentrations, while in patients suffering from other types of dementia the apoA-I CSF concentration was increased. ApoA-IV concentrations varied widely in human CSF, but were not associated with any clinical condition. HDL2-like apoE-containing lipoproteins represent the major lipoprotein fraction. In CSF of normal controls, only a minor HDL3-like apoA-I-containing lipoprotein fraction was observed; this fraction was more prevalent in AD patients. ApoA-II was recovered mostly in the HDL3 density range, while apoA-IV was not associated with lipoproteins but appeared in a lipid-free form, co-localizing with LCAT immunoreactivity Bi-dimensional analysis demonstrated pre-beta and alpha apoA-I-containing particles; apoE and apoA-II: were detected only in alpha-migrating particles. ApoA-IV distributed both to pre-P and gamma-migrating particles; the LCAT signal was co-localized in this gamma-migrating fraction. Enzymatically active LCAT tvas present in human CSF as well as PLTP activity and mass; no CETP mass was detected. In CSF from AD patients, LCAT activity was 50\% lower than in CSF from normal controls. CSF lipoproteins induced a significant cholesterol efflux from cultured rat astrocytes, suggesting that they play an active role in maintaining the cholesterol homeostasis in brain cells.},
  author       = {Demeester, Nathalie and Castro, G and Desrumaux, C and De Geitere, C and Fruchart, JC and Santens, Patrick and Mulleners, E and Engelborghs, S and De Deyn, PP and Vandekerckhove, Jo{\"e}l and Rosseneu, Maryvonne and Labeur, Christine},
  issn         = {0022-2275},
  journal      = {JOURNAL OF LIPID RESEARCH},
  keyword      = {cerebrospinal fluid,lipoproteins,Alzheimer's disease,cholesterol,efflux,HUMAN CEREBROSPINAL-FLUID,AMYLOID PRECURSOR PROTEIN,HIGH-DENSITY-LIPOPROTEIN,ESTER TRANSFER PROTEIN,APOLIPOPROTEIN-A-IV,IN-VITRO,CODON-360 MUTATION,E POLYMORPHISM,BETA-PROTEIN,HUMAN BRAIN},
  language     = {eng},
  number       = {6},
  pages        = {963--974},
  title        = {Characterization and functional studies of lipoproteins, lipid transfer proteins, and lecithin: cholesterol acyltransferase in CSF of normal individuals and patients with Alzheimer's disease.},
  volume       = {41},
  year         = {2000},
}

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