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

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