Characterization of subpopulations of lipoprotein particles isolated from human cerebrospinal fluid

Biochim Biophys Acta. 1995 Mar 16;1255(2):192-200. doi: 10.1016/0005-2760(94)00232-n.

Abstract

The aim of the present study was to define lipoprotein complexes within cerebrospinal fluid (CSF) in terms of their apolipoprotein composition, using fractionation procedures considered optimal for maintaining lipoprotein structural integrity. Five apolipoproteins were identified, namely apolipoproteins A-I, A-IV, D, E and J. These were differentially distributed amongst lipoprotein particles of which three major subpopulations were identified. CSF-LpAI (20.1 +/- 3.8 nm) was enriched in apolipoprotein A-I and contained the major proportion (> 50%) of apolipoproteins D, E and J. CSF-LpE, of similar size to CSF-LpAI (20.2 +/- 3.1 nm), was composed principally of apolipoprotein E, with minor quantities of apolipoproteins A-I, A-IV, D and J. Elimination of these particles from cerebrospinal fluid by immunoabsorption revealed a third subpopulation of significantly greater diameter (32.0 +/- 6.8 nm). The majority (62%) of apolipoprotein A-IV was also present in this fraction. The study demonstrates the structural and size heterogeneity of lipoproteins in cerebrospinal fluid. This may reflect the lipid transport processes within the central nervous system.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Apolipoprotein A-I / chemistry
  • Apolipoproteins / cerebrospinal fluid*
  • Apolipoproteins / chemistry
  • Apolipoproteins D
  • Apolipoproteins E / chemistry
  • Blotting, Western
  • Clusterin
  • Electrophoresis, Gel, Two-Dimensional
  • Glycoproteins / chemistry
  • Humans
  • Lipoproteins / cerebrospinal fluid*
  • Microscopy, Electron
  • Molecular Chaperones*

Substances

  • Apolipoprotein A-I
  • Apolipoproteins
  • Apolipoproteins D
  • Apolipoproteins E
  • CLU protein, human
  • Clusterin
  • Glycoproteins
  • Lipoproteins
  • Molecular Chaperones