Troubleshooting methods for APP processing in vitro.
BACKGROUND
The amyloid hypothesis states that Abeta is the main trigger for Alzheimer's disease. This report is focused in the study of the processing of the Amyloid Precursor Protein (APP) as a procedure to investigate the molecular mechanisms that may result in changes in the levels of Abeta.


METHODS
Here we analyse different methodologies for Abeta determination, soluble APP, APP-Carboxy terminus fragments (CTFs) and enzymes for synthesis (secretases) and degradation of Abeta. In addition the advantages and disadvantages of different methodologies are discussed.


CONCLUSIONS
The potential value of these procedures is described in the context of the function of APP and the different fragments derived from its cleavage.
Centre for Neuroscience, Division of Experimental Medicine, Imperial College London, Burlington Danes Building, Hammersmith Hospital, Du Cane Road, London W12 0NN, UK. m.sastre@imperial.ac.uk
Magdalena
M
Sastre
D000544:Alzheimer Disease / Q000209:etiology*; D053829:Amyloid Precursor Protein Secretases / Q000032:analysis / Q000378:metabolism; D016564:Amyloid beta-Protein Precursor / Q000032:analysis / Q000378:metabolism / Q000633:toxicity*; D000818:Animals; D019921:Biotinylation; D015153:Blotting, Western; D004797:Enzyme-Linked Immunosorbent Assay; D006801:Humans; D018613:Microscopy, Confocal; D010446:Peptide Fragments / Q000032:analysis; D013057:Spectrum Analysis; D013347:Subcellular Fractions / Q000737:chemistry / Q000378:metabolism; D018675:Toxicity Tests / Q000379:methods* / Q000592:standards
D016564:Amyloid beta-Protein Precursor; D010446:Peptide Fragments; D053829:Amyloid Precursor Protein Secretases