Modified amyloid beta protein ending at 42 or 40 with different solubility accumulates in the brain of Alzheimer's disease

Biochem Biophys Res Commun. 1995 Jun 26;211(3):1015-22. doi: 10.1006/bbrc.1995.1912.

Abstract

Serial extraction study of Alzheimer's disease (AD) and control brains revealed 4, 3.7 and 3 kD amyloid beta protein (A beta) species accumulated in AD brains. In the fractions extracted with TBS, 10% SDS and formic acid, considerable amounts of A beta species were recovered in SDS fractions besides TBS and formic acid fractions. Immunoblotting with several site-specific antibodies confirmed not only the presence of 4 kD A beta starting at the first amino acid of A beta but also 2 smaller A beta species with modification of their amino-termini in the highly resolutional Tris/Tricine gel system. A beta solubility using these solvents was associated with both modification of the amino-terminus and length of carboxyl-terminus of A beta. Especially, a large amount of modified A beta was found to be accumulated as forms with different solubility in AD brains.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aged
  • Aged, 80 and over
  • Alzheimer Disease*
  • Amyloid beta-Peptides / chemistry*
  • Amyloid beta-Peptides / immunology
  • Antibodies, Monoclonal
  • Antibody Specificity
  • Brain Chemistry
  • Fluoroimmunoassay
  • Humans
  • Immunoblotting

Substances

  • Amyloid beta-Peptides
  • Antibodies, Monoclonal