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Immunohistochemical evidence for amyloid beta in rat soleus muscle in chloroquine-induced myopathy.

Authors
  • Tsuzuki, K
  • Fukatsu, R
  • Takamaru, Y
  • Kimura, K
  • Abe, M
  • Shima, K
  • Fujii, N
  • Takahata, N
Type
Published Article
Journal
Neuroscience Letters
Publisher
Elsevier
Publication Date
Dec 05, 1994
Volume
182
Issue
2
Pages
151–154
Identifiers
PMID: 7715800
Source
Medline
License
Unknown

Abstract

Deposition of amyloid beta (A beta) is one of the pathological hallmarks of brains affected with Alzheimer's disease (AD). The accumulation of A beta have been observed in human myopathies with rimmed vacuoles (RVs) which might involve lysosomal function. Chloroquine, a potent lysosomotropic agent, induces muscle pathology in experimental animals similar to myopathy with RV. In this study, we demonstrate, for the first time, immunohistochemical evidence that A beta and cathepsin D, a lysosomal enzyme, accumulate in vacuolated rat soleus muscle due to chloroquine-induced myopathy. These data indicate that lysosomes are important in the metabolism of amyloid precursor protein to generate A beta. This experimental system seems to be useful not only to study basic mechanisms underlying RV myopathy but also to understand processing of amyloid precursor protein to A beta in AD.

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