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

TSUZUKI K FUKATSU R TAKAMARU Y YOSHIDA T HAYASHI Y YAMAGUCHI H FUJII N TAKAHATA N

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

26

INGLESE

Article

Neurosciences

Neuroscience letters → ACNP

0304-3940

202

1-2

1995

77 - 80

ISI

0304-3940(1995)202:1-2<77:APIRSM>2.0.ZU;2-2

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 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.