By Weiming Xia, Huaxi Xu

Within the look for an efficient remedy for Alzheimer's affliction, APP is a different version protein that illustrates the big choice of simple and complicated characterization strategies to be had.

Exploring a number of organic options to elucidate the constitution and serve as of this transmembrane protein, this article provides each one approach with distinct, step by step protocols to accomplish reproducible effects and supply a framework for learning different membrane proteins.

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Amyloid Precursor Protein: A Practical Approach

Within the look for an efficient remedy for Alzheimer's disorder, APP is a special version protein that illustrates the big variety of uncomplicated and complicated characterization suggestions to be had. Exploring various organic concepts to elucidate the constitution and serve as of this transmembrane protein, this article offers every one approach with targeted, step by step protocols to accomplish reproducible effects and supply a framework for learning different membrane proteins.

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2 MAIN SCHEME OF APPROACHES The analysis of APP processing in the endocytic pathway has been difficult because of the concurrent secretion and internalization of APP molecules from the cell surface. The assay described presents a reliable and reproducible method to measure the secretion of sAPP and APP internalization from the cell surface simultaneously. 1). 1 Schematical overview about the different methods to characterize APP trafficking using a radiolabeled antibody. The first method describes a pulse/chase experiment to analyze the kinetics of APP secretion and internalization.

15, 3769, 1996. 5. Zambrano, N. et al. Interaction of the phosphotyrosine interaction/phosphotyrosine binding-related domains of Fe65 with wild-type and mutant Alzheimer’s beta-amyloid precursor proteins. J. Biol. Chem. 272, 6399, 1997. 6. Chow, N. et al. APP-BP1, a novel protein that binds to the carboxyl-terminal region of the amyloid precursor protein. J. Biol. Chem. 271, 11339, 1996. 7. P. et al. The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein.

Et al. Involvement of amyloid precursor protein in functional synapse formation in cultured hippocampal neurons. J. Neurosci. Res. 51, 185, 1998. 21, Leveugle, B. et al. Heparin promotes beta-secretase cleavage of the Alzheimer’s amyloid precursor protein. Neurochem. Int. 30, 543, 1997. 22. Fenton, H. et al. Hepatocyte growth factor (HGF/SF) in Alzheimer’s disease. Brain Res. 779, 262, 1998. 23. Leveugle, B. et al. Heparin oligosaccharides that pass the blood–brain barrier inhibit beta-amyloid precursor protein secretion and heparin binding to beta-amyloid peptide.

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