Neuropeptidomics: expanding proteomics downwards

Biochem Soc Trans. 2007 Jun;35(Pt 3):588-93. doi: 10.1042/BST0350588.


Biological function is mainly carried out by a dynamic population of proteins and peptides which may be used as markers for disease diagnosis, prognosis and as a guide for effective treatment. The study of proteins is called proteomics and it is generally performed by two-dimensional gel electrophoresis and mass spectrometric methods. However, gel-based proteomics is methodologically restricted from the low mass region, which includes important endogenous peptides. The study of endogenous peptides, peptidomics, is complicated by protein fragments produced post-mortem during conventional sample handling. Nanoflow liquid chromatography and MS, together with improved methods for sample preparation, have been used to semi-quantitatively monitor endogenous peptides in brain tissue. When rapidly heat-denatured brain tissue was analysed, these methods enabled simultaneous detection of hundreds of peptides and the identification of several endogenous peptides not previously described in the literature. In an application of the MPTP (1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine) model for Parkinson's disease, the expression of the small protein PEP-19 was compared with controls. The levels were found to be significantly decreased in the striatum of MPTP-treated animals.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Brain / metabolism
  • Humans
  • Mice
  • Molecular Sequence Data
  • Nerve Tissue Proteins / metabolism
  • Neuropeptides / chemistry
  • Neuropeptides / genetics
  • Neuropeptides / metabolism*
  • Parkinsonian Disorders / genetics
  • Parkinsonian Disorders / metabolism
  • Protein Processing, Post-Translational
  • Proteomics
  • Rats
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization


  • Nerve Tissue Proteins
  • Neuropeptides
  • Pcp4 protein, mouse