ArticleJournal of the American Society for Mass Spectrometry2007
Stable isotope labeling tandem mass spectrometry (SILT) to quantify protein production and clearance rates.
Article in Journal of the American Society for Mass Spectrometry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
31 citing papers in PubMed, 72 citations in OpenAlex.
- An integrated multi-study analysis of intra-subject variability in cerebrospinal fluid amyloid-β concentrations collected by lumbar puncture and indwelling lumbar catheter.Alzheimer's research & therapy · 2015Trial
- An antidepressant decreases CSF Aβ production in healthy individuals and in transgenic AD mice.Science translational medicine · 2014Trial
- A gamma-secretase inhibitor decreases amyloid-beta production in the central nervous system.Annals of neurology · 2009Trial
- Determining and interpreting protein lifetimes in mammalian tissues.Trends in biochemical sciences · 2023Review
- The performance of plasma amyloid beta measurements in identifying amyloid plaques in Alzheimer's disease: a literature review.Alzheimer's research & therapy · 2022Review
- Protein turnover models for LC-MS data of heavy water metabolic labeling.Briefings in bioinformatics · 2022Article
- Proteome Dynamics from Heavy Water Metabolic Labeling and Peptide Tandem Mass Spectrometry.International journal of mass spectrometry · 2019Article
- Production of seedable Amyloid-β peptides in model of prion diseases upon PrPNature communications · 2019Article
- Protein production is an early biomarker for RNA-targeted therapies.Annals of clinical and translational neurology · 2018Article
- Lost in Translation? Finding Our Way To Effective Alzheimer's Disease Therapies.Journal of Alzheimer's disease : JAD · 2018Review
- Is Beta-Amyloid Accumulation a Cause or Consequence of Alzheimer's Disease?Journal of Alzheimer's parkinsonism & dementia · 2016Article
- Circulating protein synthesis rates reveal skeletal muscle proteome dynamics.The Journal of clinical investigation · 2016Article
- In vivo kinetic approach reveals slow SOD1 turnover in the CNS.The Journal of clinical investigation · 2015Article
- Amyloid-β efflux from the central nervous system into the plasma.Annals of neurology · 2014Article
- CNS amyloid-β, soluble APP-α and -β kinetics during BACE inhibition.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014Article
- Amyloid-beta isoform metabolism quantitation by stable isotope-labeled kinetics.Analytical biochemistry · 2013Article
- Monitoring autophagy in the treatment of protein aggregate diseases: steps toward identifying autophagic biomarkers.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2013Review
- Pathogenic prions deviate PrP(C) signaling in neuronal cells and impair A-beta clearance.Cell death & disease · 2013Article
- Measurement of apolipoprotein E and amyloid β clearance rates in the mouse brain using bolus stable isotope labeling.Molecular neurodegeneration · 2012Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
In all biological systems, protein amount is a function of the rate of production and clearance. The speed of a response to a disturbance in protein homeostasis is determined by turnover rate. Quantifying alterations in protein synthesis and clearance rates is vital to understanding disease pathogenesis (e.g., aging, inflammation). No methods currently exist for quantifying production and clearance rates of low-abundance (femtomole) proteins in vivo. We describe a novel, mass spectrometry-based method for quantitating low-abundance protein synthesis and clearance rates in vitro and in vivo in animals and humans. The utility of this method is demonstrated with amyloid-beta (Abeta), an important low-abundance protein involved in Alzheimer's disease pathogenesis. We used in vivo stable isotope labeling, immunoprecipitation of Abeta from cerebrospinal fluid, and quantitative liquid chromatography electrospray-ionization tandem mass spectrometry (LC-ESI-tandem MS) to quantify human Abeta protein production and clearance rates. The method is sensitive and specific for stable isotope-labeled amino acid incorporation into CNS Abeta (+/-1% accuracy). This in vivo method can be used to identify pathophysiologic changes in protein metabolism and may serve as a biomarker for monitoring disease risk, progression, or response to novel therapeutic agents. The technique is adaptable to other macromolecules, such as carbohydrates or lipids.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.