Amyloid beta binding proteins in vitro and in normal human cerebrospinal fluid

Neurosci Lett. 1995 May 19;191(1-2):79-82. doi: 10.1016/0304-3940(95)11565-7.

Abstract

A major neuropathological feature of Alzheimer's disease (AD) is the deposition of amyloid beta (A beta) in the form of senile plaques. The A beta peptide exists both in a beta-pleated sheet fibrillar form in amyloid deposits and as a normal soluble protein in biological fluids. Numerous proteins have been identified immunohistochemically to be associated with senile plaques, where A beta is the major constituent. Some of the latter have also been suggested to be carriers of the normal soluble A beta (sA beta) including apolipoprotein J (apoJ), apolipoprotein E (apoE) and transthyretin (TTR). We have found, using several different methods, that numerous proteins can bind synthetic A beta peptides when high concentrations are used; however, using an affinity anti-sA beta column we confirm that apoJ is the major binding protein in pooled human cerebrospinal fluid. On the other hand it is known that apoE co-purifies with A beta biochemically extracted from senile plaques. In AD tissue there may be a change in the major apolipoprotein binding A beta from apoJ to apoE.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Amyloid beta-Peptides / cerebrospinal fluid*
  • Animals
  • Antibodies, Monoclonal
  • Apolipoproteins E / metabolism
  • Blotting, Western
  • Cattle
  • Clusterin
  • Glycoproteins / metabolism
  • Humans
  • Immunohistochemistry
  • Iodine Radioisotopes
  • Molecular Chaperones*
  • Molecular Sequence Data
  • Nerve Tissue Proteins / metabolism
  • Prealbumin / metabolism
  • Precipitin Tests
  • Protein Binding

Substances

  • Amyloid beta-Peptides
  • Antibodies, Monoclonal
  • Apolipoproteins E
  • CLU protein, human
  • Clusterin
  • Glycoproteins
  • Iodine Radioisotopes
  • Molecular Chaperones
  • Nerve Tissue Proteins
  • Prealbumin