AMYLOID PRECURSOR PROTEIN, A-BETA AND AMYLOID-ASSOCIATED PROTEINS INVOLVED IN CHLOROQUINE RETINOPATHY IN RATS - IMMUNOPATHOLOGICAL STUDIES

Citation
T. Yoshida et al., AMYLOID PRECURSOR PROTEIN, A-BETA AND AMYLOID-ASSOCIATED PROTEINS INVOLVED IN CHLOROQUINE RETINOPATHY IN RATS - IMMUNOPATHOLOGICAL STUDIES, Brain research, 764(1-2), 1997, pp. 283-288
Citations number
23
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Neurosciences
Journal title
ISSN journal
0006-8993
Volume
764
Issue
1-2
Year of publication
1997
Pages
283 - 288
Database
ISI
SICI code
0006-8993(1997)764:1-2<283:APPAAA>2.0.ZU;2-K
Abstract
To understand the retinal changes in Alzheimer disease (AD) patients, pathological and immunocytochemical studies were performed on retinal cells in the chloroquine-treated rats at 0, 4, 8, 12, 16, 20, and 24 w eeks after the initial injection, using anti-amyloid precursor protein (APP), -amyloid beta protein (A beta), -apolipoprotein E (apoE), -ubi quitin, and -cathepsin D antibodies. Pathological alterations consiste nt with chloroquine retinopathy were recognized in the ganglion cells of the ganglion cell layer (GCL) and the inner plexiform layer (IPL) 4 weeks after initial chloroquine injection. Rat retinal changes appear to have a direct relationship to the duration of chloroquine administ ration. Intense immunoreactivities for anti-APP, A beta, apoE (an asso ciated protein), and ubiquitin co-localized in the swollen ganglion ce lls and Muller cells by 20-24 weeks together with the lysosomal enzyme cathepsin D. The present data indicate that the endosomal/lysosomal p athway plays an important role in the processing of APP in rat retina. This experimental model is considered to be a suitable neural model t o understand retinal pathology and the processing of APP in terms of t he pathogenesis of AD, whereas chloroquine-induced myopathy is a usefu l extra neuronal model. (C) 1997 Elsevier Science B.V.