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.
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June 2007
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Conference Article|
May 22 2007
Neuropeptidomics: expanding proteomics downwards
M. Svensson;
M. Svensson
*Laboratory for Biological and Medical Mass Spectrometry, Uppsala University, Box 583 Biomedical Centre, SE-75123 Uppsala, Sweden
†Department of Pharmaceutical Biosciences, Uppsala University, Biomedical Centre, SE-75123 Uppsala, Sweden
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K. Sköld;
K. Sköld
*Laboratory for Biological and Medical Mass Spectrometry, Uppsala University, Box 583 Biomedical Centre, SE-75123 Uppsala, Sweden
†Department of Pharmaceutical Biosciences, Uppsala University, Biomedical Centre, SE-75123 Uppsala, Sweden
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A. Nilsson;
A. Nilsson
*Laboratory for Biological and Medical Mass Spectrometry, Uppsala University, Box 583 Biomedical Centre, SE-75123 Uppsala, Sweden
†Department of Pharmaceutical Biosciences, Uppsala University, Biomedical Centre, SE-75123 Uppsala, Sweden
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M. Fälth;
M. Fälth
*Laboratory for Biological and Medical Mass Spectrometry, Uppsala University, Box 583 Biomedical Centre, SE-75123 Uppsala, Sweden
†Department of Pharmaceutical Biosciences, Uppsala University, Biomedical Centre, SE-75123 Uppsala, Sweden
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P. Svenningsson;
P. Svenningsson
‡Department of Physiology and Pharmacology, Karolinska Institutet, SE-17177 Stockholm, Sweden
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P.E. Andrén
P.E. Andrén
1
*Laboratory for Biological and Medical Mass Spectrometry, Uppsala University, Box 583 Biomedical Centre, SE-75123 Uppsala, Sweden
†Department of Pharmaceutical Biosciences, Uppsala University, Biomedical Centre, SE-75123 Uppsala, Sweden
1To whom correspondence should be addressed (email [email protected]).
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Publisher: Portland Press Ltd
Received:
March 15 2007
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2007 Biochemical Society
2007
Biochem Soc Trans (2007) 35 (3): 588–593.
Article history
Received:
March 15 2007
Citation
M. Svensson, K. Sköld, A. Nilsson, M. Fälth, P. Svenningsson, P.E. Andrén; Neuropeptidomics: expanding proteomics downwards. Biochem Soc Trans 1 June 2007; 35 (3): 588–593. doi: https://doi.org/10.1042/BST0350588
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