Journal article

Publication year: 2002

Pages: 1855-1864

Journal: Biological Chemistry

Volume number: 383

Issue number: 12

ISSN: 1431-6730

eISSN: 1437-4315

DOI Link: https://doi.org/10.1515/BC.2002.209

Publisher: De Gruyter Brill

Abstract: 
The soluble N-terminal ectodomain of amyloid precursor protein (sAPP), resulting from alpha-secretase-mediated proteolytic processing, has been shown to function as a growth factor for epithelial cells, including keratinocytes and thyrocytes. Extracellularly applied sAPP binds to a cell surface receptor and exhibits a patchy binding pattern reminiscent of that observed for raft proteins. Here we show that (i) the receptor-bound sAPP resides in a detergent-insoluble membrane microdomain which cofractionates in density gradients with cholesterol-rich membrane rafts and caveolae; (ii) the sAPP-binding microdomains are different from caveolae; and (iii) sAPP is capable of binding to isolated rafts and inducing tyrosine phosphorylation of some raft proteins. These observations suggest that a novel type of membrane raft is involved in sAPP signaling.

Harvard Citation style: Tikkanen, R., Icking, A., Beicht, P., Waneck, G. and Herzog, V. (2002) The receptor-bound N-terminal ectodomain of the amyloid precursor protein is associated with membrane rafts, Biological Chemistry, 383(12), pp. 1855-1864. https://doi.org/10.1515/BC.2002.209

APA Citation style: Tikkanen, R., Icking, A., Beicht, P., Waneck, G., & Herzog, V. (2002). The receptor-bound N-terminal ectodomain of the amyloid precursor protein is associated with membrane rafts. Biological Chemistry. 383(12), 1855-1864. https://doi.org/10.1515/BC.2002.209