Cancer-specific MALDI-TOF profiles of blood serum and plasma: biological meaning and perspectives

J Proteomics. 2010 Jan 3;73(3):537-51. doi: 10.1016/j.jprot.2009.09.011. Epub 2009 Sep 25.

Abstract

MALDI-TOF mass-spectrometry has become a popular tool of cancer research during the last decade. High throughput and relative simplicity of this technology have made it attractive for biomarker discovery and validation across various platforms in blood serum/plasma. Many technical approaches have been developed for plasma/serum profiling including protein-chip based SELDI-TOF mass-spectrometry, purification of serum on magnetic beads, analysis of carrier-associated fraction and mass-spectrometric immunoassays. Extensive data about the identity of differential features detected on mass-spectra up to now makes it possible to draw conclusions about potency and perspectives of MALDI-TOF mass-spectrometry in this field. A great majority of identified differentially expressed proteins are either house-keeping or inflammatory proteins as well as their modifications or fragments. Discriminating ability of mass-spectra is likely to be based on differential modification and fragmentation patterns of abundant serum proteins reflecting activity of enzymes including proteases and their inhibitors.

Publication types

  • Review

MeSH terms

  • Blood Chemical Analysis / methods
  • Blood Proteins / analysis
  • Humans
  • Metabolome* / physiology
  • Neoplasm Proteins / analysis*
  • Neoplasm Proteins / blood
  • Neoplasms / blood*
  • Neoplasms / metabolism
  • Peptide Hydrolases / analysis
  • Peptide Hydrolases / blood
  • Peptide Hydrolases / metabolism
  • Plasma / chemistry
  • Plasma / metabolism
  • Protease Inhibitors / analysis
  • Protease Inhibitors / metabolism
  • Serum / chemistry
  • Serum / metabolism
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / methods*

Substances

  • Blood Proteins
  • Neoplasm Proteins
  • Protease Inhibitors
  • Peptide Hydrolases