17th International Mass Spectrometry Conference :: Prague, 2006
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|Session:||Proteomics: New Methods|
|Presentation date:||Tue, Aug 29, 2006|
|Presentation time:||09:50 – 11:20|
Joerg Hanrieder1, Titti Ekegren1, Sten Magnus Aquilonius2, Jonas Bergquist11 Department of Physical and Analytical Chemistry, Uppsala University, Uppsala, Sweden
Correspondence address: Joerg Hanrieder, Uppsala University, Analytical Chemistry, Box 599, Uppsala, 75124 Sweden.
Keywords: Electrospray Ionization (ESI); Fourier Transform ICR; MALDI; Proteomic.
Novel aspect: A rapid and highly sensitive proteomic system for protein analysis in human tissue samples, significantly identifying proteins of the CNS as an alternative to the today most accepted but more time-consuming methods.
With a highly sensitive electrospray ionisation Fourier transform ion cyclotron resonance mass spectrometry (ESI-FTICR MS) system proteins were identified in minimal amounts of spinal cord from patients with the neurodegenerative disease amyotrophic lateral sclerosis (ALS) and compared to proteins in spinal cord from control subjects. The results show eighteen versus sixteen significantly identified (p < 0.05) proteins, respectively, all known to be found in the central nervous system. The most abundant protein in both groups was the glial fibrillary acidic protein, GFAP. Other proteins were e. g. hemoglobin alpha- and beta chain, myelin basic protein, thioredoxin, alpha enolase and cholin acetyltransferase. This study also includes the technique of laser microdissection in combination with pressure catapulting (LMPC) for the dissection of samples and specific neurons. Furthermore complementary experiments with nanoLC-matrix assisted laser desorption ionization time of flight tandem mass spectrometry (MALDI-TOF-TOF MS) confirmed the results of the ESI-FTICR MS screening and provided additional results of further identified proteins.