Conference paper

Publication year: 2002

Pages: 171-180

Journal: Histochemistry and Cell Biology

Volume number: 117

Issue number: 2

ISSN: 0948-6143

eISSN: 1432-119X

DOI Link: https://doi.org/10.1007/s00418-001-0351-5

Conference: 43rd Symposium of the Society-for-Histochemistry

Publisher: Springer

Abstract: 
Proteolytic processing of the Alzheimer amyloid precursor protein (APP) results in the generation of at least two distinct classes of biologically relevant peptides: (1) the amyloid beta peptides which are believed to be involved in the pathogenesis of Alzheimer's disease and (2) the soluble N-terminal ectodomain (sAPP) which exhibits a protective but as yet ill-defined effect on neurons and epithelial cells. In this report we present an overview on the functions of sAPP as an epithelial growth factor. This function involves specific binding of sAPP to membrane rafts and results in signal transduction and various physiological effects in epithelial cells as different as keratinocytes and thyrocytes. At nanomolar concentrations sAPP induces a two to fourfold increase in the rate of cell proliferation and cell migration. Specific inhibition of APP expression by antisense techniques results in decreased sAPP release and in reduced proliferative and motogenic activities. Proliferation and migration are known to be part of complex processes such as wound healing which, therefore, might be facilitated by the growth factor function of sAPP.

Harvard Citation style: Schmitz, A., Tikkanen, R., Kirfel, G. and Herzog, V. (2002) The biological role of the Alzheimer amyloid precursor protein in epithelial cells, Histochemistry and Cell Biology, 117(2), pp. 171-180. https://doi.org/10.1007/s00418-001-0351-5

APA Citation style: Schmitz, A., Tikkanen, R., Kirfel, G., & Herzog, V. (2002). The biological role of the Alzheimer amyloid precursor protein in epithelial cells. Histochemistry and Cell Biology. 117(2), 171-180. https://doi.org/10.1007/s00418-001-0351-5