NEUROFIBRILLARY LESIONS IN EXPERIMENTAL ALUMINUM-INDUCED ENCEPHALOPATHY AND ALZHEIMERS-DISEASE SHARE IMMUNOREACTIVITY FOR AMYLOID PRECURSORPROTEIN, A-BETA, ALPHA(1)-ANTICHYMOTRYPSIN AND UBIQUITIN-PROTEIN CONJUGATES
Y. Huang et al., NEUROFIBRILLARY LESIONS IN EXPERIMENTAL ALUMINUM-INDUCED ENCEPHALOPATHY AND ALZHEIMERS-DISEASE SHARE IMMUNOREACTIVITY FOR AMYLOID PRECURSORPROTEIN, A-BETA, ALPHA(1)-ANTICHYMOTRYPSIN AND UBIQUITIN-PROTEIN CONJUGATES, Brain research, 771(2), 1997, pp. 213-220
Neurofibrillary tangles of Alzheimer's disease contain predominantly t
au protein and to a lesser de ee amyloid precursor protein (APP), A be
ta protein, alpha(1)-antichymotrypsin (ACT) and ubiquitin. Previously
we have demonstrated the presence of phosphorylated tau and neurofilam
ent proteins in neurofibrillary degeneration (NFD) induced by aluminum
(Al) maltolate in rabbits [Savory et al., Brain Res. 669 (1995) 325-3
29; Savory et al., Brain Res. 707 (1996) 272-281]. Using the same anim
al system we have now detected APP, A beta, ACT and ubiquitin-like imm
unoreactivities in NFD-bearing neurons, often colocalizing in the NFD.
Diffuse cytoplasmic staining for APP, A beta and ubiquitin was also p
resent in neurons without NFD from Al maltolate-treated rabbits. This
study provides additional support for immunochemical similarities betw
een Al-induced NFD in rabbits and the neurofibrillary tangles in human
subjects with Alzheimer's disease. (C) 1997 Elsevier Science B.V.