Journal article

Publication year: 2014

Pages: 119-129

Journal: Molecular Neurobiology

Volume number: 50

Issue number: 1

ISSN: 0893-7648

DOI Link: https://doi.org/10.1007/s12035-014-8652-6

Publisher: Springer

Abstract: 
The senile plaque is a pathologic hallmark of Alzheimer's disease (AD). Amyloid-beta peptide (A beta), the main constituent of senile plaques, is neurotoxic especially in its oligomeric form. A beta is derived from the sequential cleavage of amyloid precursor protein (APP) by beta- and gamma-secretases in the amyloidogenic pathway. Alternatively, APP can be cleaved by alpha-secretases within the A beta domain to produce neurotrophic and neuroprotective alpha-secretase-cleaved soluble APP (sAPP alpha) in the nonamyloidogenic pathway. Since APP and alpha-, beta-, and gamma-secretases are membrane proteins, APP processing should be highly dependent on the membrane composition and the biophysical properties of cellular membrane. In this review, we discuss the role of the biophysical properties of cellular membrane in APP processing, especially the effects of phospholipases A(2) (PLA(2)s), fatty acids, cholesterol, and A beta on membrane fluidity in relation to their effects on APP processing.

Harvard Citation style: Yang, X., Sun, G., Eckert, G. and Lee, J. (2014) Cellular Membrane Fluidity in Amyloid Precursor Protein Processing, Molecular Neurobiology, 50(1), pp. 119-129. https://doi.org/10.1007/s12035-014-8652-6

APA Citation style: Yang, X., Sun, G., Eckert, G., & Lee, J. (2014). Cellular Membrane Fluidity in Amyloid Precursor Protein Processing. Molecular Neurobiology. 50(1), 119-129. https://doi.org/10.1007/s12035-014-8652-6