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MALDI Imaging of Post Mortem Human Spinal Cord in Amyotrophic Lateral Sclerosis
Department of Chemical and Biological Engineering, Analytical Chemistry, Chalmers University of Technology, Gothenburg, Sweden;.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Neuroscience, Neurology.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmaceutical Biosciences.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Analytical Chemistry. Uppsala University, Science for Life Laboratory, SciLifeLab.
2013 (English)In: Journal of Neurochemistry, ISSN 0022-3042, E-ISSN 1471-4159, Vol. 124, no 5, 695-707 p.Article in journal (Refereed) Published
Abstract [en]

Amyotrophic lateral sclerosis (ALS) is a devastating, rapidly progressing disease of the central nervous system that is characterized by motor neuron degeneration in the brain stem and the spinal cord. Matrix assisted laser desorption/ionization imaging mass spectrometry (MALDI IMS) is an emerging powerful technique that allows for spatially resolved, comprehensive and specific characterization of molecular species in situ. In this study we report for the first time, MALDI imaging-based spatial protein profiling and relative quantification of post mortem human spinal cord samples obtained from ALS patients and controls. In normal spinal cord, protein distribution patterns were well in line with histological features. For example, thymosin beta 4, ubiquitin, histone proteins, acyl CoA binding protein, and macrophage inhibitory factor were predominantly localized to the grey matter. Furthermore, unsupervised statistics revealed a significant reduction of two protein species in ALS grey matter. One of these proteins (m/z 8451) corresponds to an endogenous truncated form of ubiquitin (Ubc 1-76), with both C-terminal glycine residues removed (Ubc-T/Ubc 1-74). This region-specific ubiquitin processing suggests a disease-related change in protease activity. These results highlight the importance of MALDI IMS as a versatile approach to elucidate molecular mechanisms of neurodegenerative diseases.

Place, publisher, year, edition, pages
2013. Vol. 124, no 5, 695-707 p.
Keyword [en]
amyotrophic lateral sclerosis, imaging mass spectrometry, matrix-assisted laser desorption/ionization, post-mortem spinal cord, tissue imaging.
National Category
Natural Sciences
Research subject
Biochemistry
Identifiers
URN: urn:nbn:se:uu:diva-182909DOI: 10.1111/jnc.12019ISI: 000315105000012OAI: oai:DiVA.org:uu-182909DiVA: diva2:561373
Available from: 2012-10-18 Created: 2012-10-18 Last updated: 2017-12-07Bibliographically approved

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Ekegren, TittiAndersson, MalinBergquist, Jonas

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