This Article Full Text (PDF) References Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Alert me to new issues of the journal Add to Saved Citations Download to citation manager Request Permissions Request Reprints Add to My Marked Citations Citing Articles Citing Articles via Google Scholar Citing Articles via Scopus Google Scholar Articles by Tate-Ostroff, B. Articles by Marotta, C. A. Search for Related Content PubMed Articles by Tate-Ostroff, B. Articles by Marotta, C. A. Social Bookmarking                         What's this?

of Amino Terminal and A4 (ß-Amyloid) Antigens in Alzheimer Plaques: Evidence for Coordinated Processing of the Amyloid Precursor Protein

Department of Psychiatry, Harvard Medical School, Neurobiology Laboratory, Massachusetts General Hospital, Boston, MA, Mailman Research Center, McLean Hospital, Belmont, MA

Ronald E. Majocha

Department of Psychiatry, Harvard Medical School, Neurobiology Laboratory, Massachusetts General Hospital, Boston, MA, Mailman Research Center, McLean Hospital, Belmont, MA

Elisabeth C. Walcott

Mailman Research Center, McLean Hospital, Belmont, MA

Montserrat Ventosa-Michelman

Mailman Research Center, McLean Hospital, Belmont, MA

Charles A. Marotta

Department of Psychiatry, Harvard Medical School, Neuroscience Program, Harvard Medical School, Boston, MA, Neurobiology Laboratory, Massachusetts General Hospital, Boston, MA

The mechanism by which the A4 (ß-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 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. (J Geriatr Psychiatry Neurol 1990;3:139-145).

Journal of Geriatric Psychiatry and Neurology, Vol. 3, No. 3, 139-145 (1990)
DOI: 10.1177/089198879000300303


CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    Twitter    What's this?