Amyloid beta protein in rat soleus muscle in chloroquine-induced myopathy using end-specific antibodies for A beta 40 and A beta 42: immunohistochemical evidence for amyloid beta protein

Neurosci Lett. 1995 Dec 29;202(1-2):77-80. doi: 10.1016/0304-3940(95)12205-2.


Previous immunohistochemical studies from this laboratory demonstrated that monoclonal antibodies raised against various regions of amyloid precursor protein (APP) (i.e., N-terminus, amyloid beta protein (A beta), and C-terminus) strongly labeled vacuoles in chloroquine-induced myopathy-affected muscle in rats. In this study, we used antibodies end specific for the A beta 40 and A beta 42 species, and a monoclonal antibody to A beta 1-9 which reacts with APP and A beta. Most vacuoles clearly reacted with anti-A beta 1-9, while about half reacted with anti-A beta 42, and only a few reacted with anti-A beta 40. These results demonstrate that vacuoles in chloroquine-induced myopathy-affected muscle contain cleaved A beta, and that distribution of the two major A beta species is similar to what is observed in A beta deposition in Alzheimer's disease (AD)-affected brain. This provides further evidence that chloroquine-induced myopathy in rats provides a suitable model to understand APP processing into A beta, and the role of APP in terms of the pathogenesis of AD.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid beta-Peptides / analysis*
  • Amyloid beta-Peptides / immunology
  • Amyloid beta-Protein Precursor / immunology
  • Amyloid beta-Protein Precursor / ultrastructure
  • Animals
  • Antibodies, Monoclonal
  • Antibody Specificity
  • Antimalarials / adverse effects
  • Chloroquine / adverse effects
  • Disease Models, Animal
  • Immunohistochemistry
  • Male
  • Muscle, Skeletal / chemistry*
  • Muscular Diseases / chemically induced
  • Muscular Diseases / pathology
  • Rats
  • Rats, Wistar


  • Amyloid beta-Peptides
  • Amyloid beta-Protein Precursor
  • Antibodies, Monoclonal
  • Antimalarials
  • Chloroquine