Abstract
The mechanism by which the A4 (beta-amyloid) domain of the Alzheimer amyloid precursor protein (APP) is deposited in plaques is unknown, and limited information is available concerning the extent to which other APP sites are associated with plaques. To address these issues, we prepared antiserum to a peptide adjacent to the N-terminus of the APP (referred to as N1) and examined its distribution in brain relative to A4 by double-immunostaining techniques. Anti-N1 localized to both neurons and glia in control and Alzheimer patients. In the Alzheimer brain, anti-N1 detected plaques. Quantitation revealed that 85% of thioflavin-positive plaques, and 91% of A4-positive plaques were also N1 positive. Double-staining methods directly demonstrated colocalization of distant APP sites. The data suggest that suggest that proposed mechanisms for amyloid deposition during plaque formation must take into account the extracytoplasmic domain, in addition to the A4 region, rather than be confined exclusively to the A4 site.
References
Mar 11, 1990·Proceedings of the National Academy of Sciences of the United States of America·H AraiJ Q Trojanowski
Aug 1, 1988·Proceedings of the National Academy of Sciences of the United States of America·R E MajochaC A Marotta
Aug 30, 1989·Biochemical and Biophysical Research Communications·J GhisoB Frangione
Mar 1, 1989·Proceedings of the National Academy of Sciences of the United States of America·D SchubertG Cole
Aug 1, 1989·Proceedings of the National Academy of Sciences of the United States of America·M R PalmertS G Younkin
Oct 31, 1989·Biochemical and Biophysical Research Communications·L M RefoloN K Robakis
Jan 1, 1989·Proceedings of the National Academy of Sciences of the United States of America·B Tate-OstroffC A Marotta
Sep 1, 1989·Journal of Neurochemistry·R E MajochaC A Marotta
Jan 1, 1989·Neuroscience·F M BenesC A Marotta
Feb 19, 1987·Nature·J KangB Müller-Hill
Feb 1, 1988·Proceedings of the National Academy of Sciences of the United States of America·S B ZainC A Marotta
Dec 5, 1988·FEBS Letters·L Autilio-GambettiP Gambetti
Feb 20, 1987·Science·R E TanziR L Neve
Jun 1, 1987·Proceedings of the National Academy of Sciences of the United States of America·N K RobakisH M Wisniewski
Oct 14, 1988·Biochemical and Biophysical Research Communications·M R PalmertS G Younkin
Jun 1, 1985·Proceedings of the National Academy of Sciences of the United States of America·C L MastersK Beyreuther
Jun 1, 1988·Journal of the American Geriatrics Society·E M Sajdel-SulkowskaC A Marotta
Feb 20, 1987·Science·D GoldgaberD C Gajdusek
Jun 1, 1985·Proceedings of the National Academy of Sciences of the United States of America·G PerryP Gambetti
Jun 1, 1985·Canadian Journal of Biochemistry and Cell Biology = Revue Canadienne De Biochimie Et Biologie Cellulaire·R E MajochaF M Benes
May 16, 1984·Biochemical and Biophysical Research Communications·G G Glenner, C W Wong
Feb 1, 1983·Journal of Neurochemistry·B A BrownC A Marotta
Citations
Jan 1, 1992·Journal of Molecular Neuroscience : MN·C A MarottaB Tate
Jan 1, 1992·Pharmacology & Therapeutics·A I BushC L Masters
Dec 1, 1999·Experimental Gerontology·F MarxB Grubeck-Loebenstein
Nov 13, 2012·Free Radical Biology & Medicine·Scott AytonAshley I Bush
Oct 5, 2014·The Journal of Biological Chemistry·Anna G VorobyevaAleister J Saunders
Dec 3, 2016·Neurology·Ellis S van EttenGisela M Terwindt
Dec 14, 2002·Annals of the New York Academy of Sciences·Gjumrakch AlievCarl W Cotman