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Focused proteomics in post-mortem human spinal cord.

Journal article
Authors Titti Ekegren
Jörg Hanrieder
Sten-Magnus Aquilonius
Jonas Bergquist
Published in Journal of proteome research
Volume 5
Issue 9
Pages 2364-71
ISSN 1535-3893
Publication year 2006
Published at Institute of Neuroscience and Physiology, Department of Psychiatry and Neurochemistry
Pages 2364-71
Language en
Links dx.doi.org/10.1021/pr060237f
Keywords Amyotrophic Lateral Sclerosis, metabolism, Dissection, methods, Humans, Lasers, Postmortem Changes, Proteins, analysis, Proteomics, methods, Spectrometry, Mass, Electrospray Ionization, Spinal Cord, chemistry
Subject categories Neurochemistry, Neurology

Abstract

With a highly sensitive electrospray ionization-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 18 versus 16 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, for example, hemoglobin alpha- and beta chain, myelin basic protein, thioredoxin, alpha enolase, and choline 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.

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