The Metabolism of Human Soluble Amyloid Precursor Protein Isoforms Is Quantifiable by a Stable Isotope Labeling-Tandem Mass Spectrometry Method
Zakaria, JAD; Bateman, R.J.; Lysakowska, M.; et al.
To better understand the pathophysiological mechanisms of Alzheimer’s disease, Dobrowolska Zakaria et al. developed a novel method to measure the metabolism of amyloid precursor protein (APP) isoforms in vivo. This utilized a stable isotope labeling kinetics (SILK) approach (e.g., with 13C6 L-leucine) together with immunoprecipitation and LC-SRM/MS. Among the findings, the kinetic rates and quantitation of APP isoforms were reproducibly determined in humans for the first time. Although larger sample tests are necessary, evidence suggests that this strategy could help guide clinical trial programs, for example, on therapeutic intervention.
Articles
- Cardiac Myosin Filaments are Maintained by Stochastic Protein Replacement
- An Optimized MRM-Based Workflow of the l-Arginine/Nitric Oxide Pathway Metabolites Revealed Disease- and Sex-Related Differences in the Cardiovascular Field
- Continuous Oral Stable Isotope Ingestion to Measure Whole-Body Protein Turnover
- The Metabolism of Human Soluble Amyloid Precursor Protein Isoforms Is Quantifiable by a Stable Isotope Labeling-Tandem Mass Spectrometry Method
- TurnoveR: A Skyline External Tool for Analysis of Protein Turnover in Metabolic Labeling Studies
- Isotope Tracing in Health and Disease
