Processing and Secretion of Alzheimer's Disease Amyloid Precursor Protein.
Kayoko Kinbara, Hiroshi Kitagaki, Tadatoshi Kinouchi, Masamichi Okano, Hiroyuki Sorimachi, Shoichi Ishiura, Koichi Suzuki
Abstract
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Kayoko Kinbara, Hiroshi Kitagaki, Tadatoshi Kinouchi, Masamichi Okano, Hiroyuki Sorimachi, Shoichi Ishiura, Koichi Suzuki
Abstract
Open-access reader
KINBARA, K., KITAGAKI, H., KINOUCHI, T., OKANO, M., SORIMACHI, H., ISHIURA, S. and SUZUKI, K. Processing and Secretion of Alzheimers's Disease Amyloid Precursor Protein. Tohoku J. Exp. Med., 1994, 174 (3), 209-216 - We studied in vivo expression and in vitro secretion of the Alzheimer's disease amyloid precursor protein (APP). The results indicate that secretion of APP is mediated by PKC and the initial step of the processing may occur in the acidic secretooy granules of the glial cells. Our results suggest that a metabolic switch of APP in neural cells is critical in amyloid deposition.
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KINBARA, K., KITAGAKI, H., KINOUCHI, T., OKANO, M., SORIMACHI, H., ISHIURA, S. and SUZUKI, K. Processing and Secretion of Alzheimers's Disease Amyloid Precursor Protein. Tohoku J. Exp. Med., 1994, 174 (3), 209-216 - We studied in vivo expression and in vitro secretion of the Alzheimer's disease amyloid precursor protein (APP). The results indicate that secretion of APP is mediated by PKC and the initial step of the processing may occur in the acidic secretooy granules of the glial cells. Our results suggest that a metabolic switch of APP in neural cells is critical in amyloid deposition.
Key concepts: Secretion, Amyloid precursor protein, Alzheimer's disease, P3 peptide, Amyloid (mycology), In vivo, Chemistry, Cell biology