Journal article
Ex vivo 18O-labeling mass spectrometry identifies a peripheral amyloid β clearance pathway
E Portelius, N Mattsson, J Pannee, H Zetterberg, M Gisslén, H Vanderstichele, E Gkanatsiou, GAN Crespi, MW Parker, LA Miles, J Gobom, K Blennow
Molecular Neurodegeneration | BIOMED CENTRAL LTD | Published : 2017
Open access
Abstract
Background: Proteolytic degradation of amyloid β (Aβ) peptides has been intensely studied due to the central role of Aβ in Alzheimer’s disease (AD) pathogenesis. While several enzymes have been shown to degrade Aβ peptides, the main pathway of Aβ degradation in vivo is unknown. Cerebrospinal fluid (CSF) Aβ42 is reduced in AD, reflecting aggregation and deposition in the brain, but low CSF Aβ42 is, for unknown reasons, also found in some inflammatory brain disorders such as bacterial meningitis. Method: Using 18O-labeling mass spectrometry and immune-affinity purification, we examined endogenous proteolytic processing of Aβ in human CSF. Results: The Aβ peptide profile was stable in CSF sampl..
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Awarded by Magnus Bergvalls Stiftelse
Funding Acknowledgements
This work was supported by funding from The Swedish Research Council, Wallstrom's and Sjobloms Foundation, Gun and Bertil Stohne's Foundation, Magnus Bergwall's Foundation, Demensforbundet, Stiftelsen fur Gamla tjanarinnor, a National Health and Medical Research Council of Australia (NHMRC) Project Grant (APP1021935) and grants from the JO & JR Wicking Trust, The Mason Foundation and The Bethlehem Griffith Research Foundation to Infrastructure support to St. Vincent's Institute from the NHMRC Independent Research Institutes Infrastructure Support Scheme and the Victorian State Government Operational Infrastructure Support Program are gratefully acknowledged. MWP is an NHMRC Research Fellow.