Glycosylation of the amyloid peptide precursor containing the Kunitz protease inhibitor domain improves the inhibition of trypsin

Biochemical and Biophysical Research Communications
E Godfroid, J N Octave

Abstract

The amyloid beta peptide (A beta P) is the major constituent of the amyloid deposits that accumulate extracellularly in the brain of patients with Alzheimer's disease. This peptide is obtained from transmembrane amyloid protein precursors (APP) which sometimes contain a Kunitz protease inhibitor (KPI) insert in their extracellular domain and therefore are able to inhibit serine proteases. Expression of the transmembrane and the secreted APP containing the KPI domain was obtained by transient transfection of COS-1 cells. The overexpressed proteins were detected in immunoblotting experiments and inhibition of trypsin was analyzed using reverse enzymography. Our results indicate that post-translational modifications including glycosylation improve the inhibition of trypsin by the APP containing the KPI domain.

Citations

May 20, 1998·Molecular Neurobiology·K C BreenF D Hayes
Jun 3, 2006·Analytical and Bioanalytical Chemistry·Jillian R A NewtonMalcolm R Clench
Aug 16, 2006·Neuro-degenerative Diseases·M Menéndez-GonzálezB Blázquez Menes
Apr 5, 2007·Annals of the New York Academy of Sciences·Sara C T S DominguesOdete A B Da Cruz e Silva
Oct 1, 1995·Reviews in the Neurosciences·J N Octave
Nov 23, 2018·International Journal of Molecular Sciences·Jesús Hernández-PérezJorge Benavides

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