W Yamao-Harigaya

Learn More
Proteolytic modifications of amyloid precursor protein (APP) play key roles in the development of Alzheimer's disease. However, each specific in vivo process has not yet been fully resolved in spatial terms because the orthodox approach employing electrophoretic analysis requires homogenization of samples and thus provides limited information on the(More)
We aimed to determine quantitatively the fine amino- and carboxyl-terminal structure of A beta peptides deposited in human brain using a set of 12 anti-A beta antibodies that distinguish between terminal modifications including isomerization, stereoisomerization, limited proteolysis, and cyclization. Immunochemical examination of cortical blocks from aged(More)
The neuroblastoma cell line NB-1 is induced to start neurite outgrowth by dibutyryl cyclic AMP (Bt2cAMP). To study the function of Alzheimer amyloid protein precursor (APP), a stable cell line overexpressing APP was established by cDNA transfection. The APP cDNA was driven by the cytomegalovirus early gene promoter. The transformant underwent degeneration(More)
One of the pathological changes of Alzheimer's disease is the deposit of beta/A4 protein, which is derived from Alzheimer amyloid precursor protein (APP). In the secretory pathway, APP is cleaved at an internal region of beta/A4 protein by a hypothetical enzyme "secretase." Our previous study showed that the site of cleavage of APP by secretase is(More)
One of the features of Alzheimer's disease (AD) is the formation of senile plaques, of which the main component is a 42 amino acid beta-protein (beta P). Molecular cloning of beta P revealed the presence of a 90-130 kDa precursor, amyloid precursor protein (APP). Since APP is expressed in normal brain without producing beta P, some abnormal processing is(More)
  • 1