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
K. Tsuzuki et al., 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, Neuroscience letters, 202(1-2), 1995, pp. 77-80
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 bet
a), and C-terminus) strongly labeled vacuoles in chloroquine-induced m
yopathy-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 an
tibody to A beta 1-9 which reacts with APP and A beta. Most vacuoles c
learly reacted with anti-A beta 1-9, while about half reacted with ant
i-A beta 42, and only a few reacted with anti-A beta 40. These results
demonstrate that vacuoles in chloroquine-induced myopathy-affected mu
scle 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 Al
zheimer'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 o
f the pathogenesis of AD.