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Clinical Proteomics

, Volume 2, Issue 1–2, pp 91–101 | Cite as

Assessment of protein stability in cerebrospinal fluid using surface-enhanced laser desorption/ionization time-of-flight mass spectrometry protein profiling

  • Srikanth Ranganathan
  • Anna Polshyna
  • Georgina Nicholl
  • James Lyons-Weiler
  • Robert BowserEmail author
Open Access
Original 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.

Keywords

Phosphatase Inhibitor Relative Peak Intensity Proteomic Alteration Surface Enhance Laser Desorption Ionization Sample Collection Procedure 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Humana Press Inc 2006

Authors and Affiliations

  • Srikanth Ranganathan
    • 2
  • Anna Polshyna
    • 2
  • Georgina Nicholl
    • 2
  • James Lyons-Weiler
    • 2
    • 1
  • Robert Bowser
    • 2
    Email author
  1. 1.Centers for Biomedical InformaticsUniversity of PittsburghPittsburgh
  2. 2.Department of PathologyUniversity of Pittsburgh School of MedicinePittsburgh

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