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Cleavage at the N-terminal Site of Alzheimer Amyloid beta/A4 Protein Is Essential for Its Secretion

Cleavage at the N-terminal Site of Alzheimer Amyloid beta/A4 Protein Is Essential for Its Secretion

K Maruyama, Y Kawamura, H Asada, S Ishiura, K Obata

Biochem Biophys Res Commun. 1994 Aug 15;202(3):1517-23.

PMID: 8060334

Abstract:

To characterize the secretory pathway of Alzheimer amyloid beta/A4 protein (beta/A4), mutated cDNAs of amyloid precursor protein (APP) were expressed transiently in COS cells. Although the expression of C100 (Met671-Asn770) resulted in the secretion of beta/A4-like peptide, the cells expressing the mutated APPs with the longer N-terminal domain beyond beta/A4 sequence secreted little beta/A4-like peptide. The C-terminal domain truncated APPs, with a stop codon at the end of beta/A4 sequence or the predicted membrane spanning domain produced little beta/A4-like peptide. When beta/A4 was expressed with direct addition of the signal sequence, beta/A4-like peptide was found in the cell lysate but little of it was secreted. Hence, the secretion of beta/A4 was started initially by cleavage at the N-terminal site of beta/A4, although cleavage at its C-terminal site was also necessary for its secretion.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR4248066	Amyloid Precursor Protein N-Terminal Peptide			Price

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