Human-like rodent amyloid-beta-peptide determines Alzheimer pathology in aged wild-type Octodon degu

Neurobiol Aging. 2005 Jul;26(7):1023-8. doi: 10.1016/j.neurobiolaging.2004.09.016. Epub 2004 Dec 10.

Abstract

It is generally accepted that human Alzheimer's disease (AD) neuropathology markers are completely absent in rodent brains. We report here that an aged wild-type South American rodent, Octodon degu, expresses neuronal beta-amyloid precursor protein (beta-APP695) displaying both intracellular and extracellular deposits of amyloid-beta-peptide (Abeta), intracellular accumulations of tau-protein and ubiquitin, a strong astrocytic response and acetylcholinesterase (AChE)-rich pyramidal neurons. The high amino acid homology (97.5%) between deguAbeta and humanAbeta sequences is probably a major factor in the appearance of AD markers in this aged rodent. Our results indicate that aged O. degu constitutes the first wild-type rodent model for neurodegenerative processes associated to AD.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylcholinesterase / metabolism
  • Aging / physiology*
  • Alzheimer Disease / metabolism*
  • Alzheimer Disease / pathology
  • Amino Acid Sequence
  • Amyloid beta-Peptides / genetics
  • Amyloid beta-Peptides / metabolism*
  • Animals
  • Astrocytes / metabolism
  • Blotting, Northern / methods
  • Brain / cytology
  • Brain / metabolism
  • Disease Models, Animal
  • Gene Expression Regulation / physiology
  • Glial Fibrillary Acidic Protein / metabolism
  • Humans
  • Immunohistochemistry / methods
  • Neurons / metabolism
  • Octodon / metabolism*
  • RNA, Messenger / biosynthesis
  • Rats
  • Reverse Transcriptase Polymerase Chain Reaction / methods
  • Ubiquitin / metabolism
  • tau Proteins / metabolism

Substances

  • Amyloid beta-Peptides
  • Glial Fibrillary Acidic Protein
  • RNA, Messenger
  • Ubiquitin
  • tau Proteins
  • Acetylcholinesterase