DEVELOPMENT OF A MONOCLONAL-ANTIBODY SPECIFIC FOR THE COOH-TERMINAL OF BETA-AMYLOID-1-42 AND ITS IMMUNOHISTOCHEMICAL REACTIVITY IN ALZHEIMERS-DISEASE AND RELATED DISORDERS
Gm. Murphy et al., DEVELOPMENT OF A MONOCLONAL-ANTIBODY SPECIFIC FOR THE COOH-TERMINAL OF BETA-AMYLOID-1-42 AND ITS IMMUNOHISTOCHEMICAL REACTIVITY IN ALZHEIMERS-DISEASE AND RELATED DISORDERS, The American journal of pathology, 144(5), 1994, pp. 1082-1088
The beta-amyloid peptide (beta AP) has been characterized by protein s
equencing techniques as a 39-43 amino acid protein with heterogeneous
COOH-terminal. Controversy exists regarding the predominant form of be
ta AP in neuritic plaques (NP) and cerebral vasculature of Alzheimer's
disease (AD) brain. A monoclonal antibody was developed that selectiv
ely recognizes the free COOH-terminal of beta AP 1-42 but not beta AP
species with shorter or longer COOH-terminal. Brain sections from AD a
nd related disorders were examined using this antibody. In AD samples,
the antibody stained diffuse amyloid and NP cores, many intraneuronal
and extraneuronal neurofibrillary tangles (NFT), but not cerebrovascu
lar amyloid. Pick and Lewy bodies lacked immunoreactivity. These findi
ngs suggest that beta AP 1-42 is present in early and mature amyloid d
eposits and NFT, but that species of beta AP other than 1-42 comprise
human vascular deposits.