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In order to understand how the HDL particles in the brain compartment are synthesized and remodeled, we investigated in human CSF the presence of minor lipoprotein subclasses such as preβ particles by bi-dimensional non-denaturing gel electrophoresis.
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Enzymatically active LCAT was present in human CSF as well as PLTP activity and mass; no CETP mass was detected. On the contrary, increasing cellular cholesterol concentrations by adding β-VLDL to Cos1 cells causes a decrease of the secretion of the soluble form of APP (s APP).
In CSF from AD patients, LCAT activity was 50% lower than in CSF from normal controls. These observations suggest that CSF lipoproteins may fulfill an important role in maintaining the neuronal cholesterol levels, thereby regulating indirectly the production of amyloidogenic peptides.
Several observations suggest a close relationship between the lipoprotein metabolism in the brain and the development of Alzheimer's disease (AD) (1, 2).
Characterization and functional studies of lipoproteins, lipid transfer proteins, and lecithin:cholesterol acyltransferase in CSF of normal individuals and patients with Alzheimer's disease.
It is not known in what form HDL precursors are synthesized in the brain and whether remodeling occurs within the CSF.