Comparison of the reaction of methylglyoxal (MGO) with murine and human amyloid beta (Aβ): Insights into a mechanism of Alzheimer's disease (AD)

Biochem Biophys Res Commun. 2020 Dec 17;533(4):1298-1302. doi: 10.1016/j.bbrc.2020.10.008. Epub 2020 Oct 10.

Abstract

Reacted with methylglyoxal (MGO), murine Aβ(1-40) (mAβ) produced significantly less superoxide anion (O2•-) compared to human Aβ(1-40) (hAβ). The reactions of MGO with mAβ(R13H), hAβ(H13F), Nα-acetyl-l-lysine, and Nα-acetyl-l-arginine implied that the lack of His13 in mAβ prohibits its Lys16 residue from reacting to produce cross-linked reaction products and O2•-. Our results suggest that murine brains are under less oxidative stress than human brains, which may be one of the reasons why rodents do not develop AD-like symptoms, and which provides further insight into a chemical mechanism for the development of AD in humans.

Keywords: Alzheimer’s disease; Glycation; Human amyloid beta (hAβ); Methylglyoxal (MGO); Murine amyloid beta (mAβ); Oxidative stress.

Publication types

  • Comparative Study

MeSH terms

  • Alzheimer Disease / etiology
  • Amyloid beta-Peptides / chemistry*
  • Amyloid beta-Peptides / metabolism
  • Animals
  • Arginine / analogs & derivatives
  • Arginine / metabolism
  • Humans
  • Lysine / analogs & derivatives
  • Lysine / metabolism
  • Mice
  • Peptide Fragments / chemistry*
  • Peptide Fragments / metabolism
  • Pyruvaldehyde / chemistry*
  • Pyruvaldehyde / metabolism
  • Superoxides / metabolism

Substances

  • Amyloid beta-Peptides
  • Peptide Fragments
  • amyloid beta-protein (1-40)
  • Superoxides
  • N(alpha)-acetyllysine
  • Pyruvaldehyde
  • Arginine
  • Lysine
  • N-acetyl-L-arginine