Assessment of protein stability in cerebrospinal fluid using surface-enhanced laser desorption/ionization time-of-flight mass spectrometry protein profiling
Document Type
Article
Abstract
Recent studies have evaluated proper acquisition and storage procedures for the use of serum or plasma for mass spectrometry (MS)-based proteomics. The present study examines the proteome stability of human cerebrospinal fluid (CSF) over time at 23°C (room temperature) and 4°C using surface-enhanced laser desorption/ionization time-of-flight MS. Data analysis revealed that statistically significant differences in protein profiles are apparent within 4 h at 23°C and between 6 and 8 h at 4°C. Inclusion of protease and phosphatase inhibitor cocktails into the CSF samples failed to significantly reduce proteome alterations over time. We conclude that MS-based proteomic analysis of CSF requires careful assessment of sample collection procedures for rapid and optimal sample acquisition and storage. Copyright © 2006 Humana Press Inc.
Keywords
Cerebrospinal fluid, Mass spectrometry, Profiling, Proteomics
Publication Date
3-1-2006
Publication Title
Clinical Proteomics
ISSN
15426416
Volume
2
Issue
1-2
First Page
91
Last Page
102
Digital Object Identifier (DOI)
10.1385/CP:2:1:91
Recommended Citation
Ranganathan, Srikanth; Polshyna, Anna; Nicholl, Georgina; Lyons-Weiler, James; and Bowser, Robert, "Assessment of protein stability in cerebrospinal fluid using surface-enhanced laser desorption/ionization time-of-flight mass spectrometry protein profiling" (2006). Translational Neuroscience. 591.
https://scholar.barrowneuro.org/neurobiology/591