Ultra-High Mass Resolution MALDI Imaging Mass Spectrometry of Proteins and Metabolites in a Mouse Model of Glioblastoma

Abstract MALDI mass spectrometry imaging is able to simultaneously determine the spatial distribution of hundreds of molecules directly from tissue sections, without labeling and without prior knowledge. Ultra-high mass resolution measurements based on Fourier-transform mass spectrometry have been u...

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Autores principales:	M. Dilillo, R. Ait-Belkacem, C. Esteve, D. Pellegrini, S. Nicolardi, M. Costa, E. Vannini, E. L. de Graaf, M. Caleo, L. A. McDonnell
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/c165c4c1b6644d96ad31944605dd372f
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spelling	oai:doaj.org-article:c165c4c1b6644d96ad31944605dd372f2021-12-02T16:06:15ZUltra-High Mass Resolution MALDI Imaging Mass Spectrometry of Proteins and Metabolites in a Mouse Model of Glioblastoma10.1038/s41598-017-00703-w2045-2322https://doaj.org/article/c165c4c1b6644d96ad31944605dd372f2017-04-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-00703-whttps://doaj.org/toc/2045-2322Abstract MALDI mass spectrometry imaging is able to simultaneously determine the spatial distribution of hundreds of molecules directly from tissue sections, without labeling and without prior knowledge. Ultra-high mass resolution measurements based on Fourier-transform mass spectrometry have been utilized to resolve isobaric lipids, metabolites and tryptic peptides. Here we demonstrate the potential of 15T MALDI-FTICR MSI for molecular pathology in a mouse model of high-grade glioma. The high mass accuracy and resolving power of high field FTICR MSI enabled tumor specific proteoforms, and tumor-specific proteins with overlapping and isobaric isotopic distributions to be clearly resolved. The protein ions detected by MALDI MSI were assigned to proteins identified by region-specific microproteomics (0.8 mm2 regions isolated using laser capture microdissection) on the basis of exact mass and isotopic distribution. These label free quantitative experiments also confirmed the protein expression changes observed by MALDI MSI and revealed changes in key metabolic proteins, which were supported by in-situ metabolite MALDI MSI.M. DililloR. Ait-BelkacemC. EsteveD. PellegriniS. NicolardiM. CostaE. VanniniE. L. de GraafM. CaleoL. A. McDonnellNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q M. Dilillo R. Ait-Belkacem C. Esteve D. Pellegrini S. Nicolardi M. Costa E. Vannini E. L. de Graaf M. Caleo L. A. McDonnell Ultra-High Mass Resolution MALDI Imaging Mass Spectrometry of Proteins and Metabolites in a Mouse Model of Glioblastoma
description	Abstract MALDI mass spectrometry imaging is able to simultaneously determine the spatial distribution of hundreds of molecules directly from tissue sections, without labeling and without prior knowledge. Ultra-high mass resolution measurements based on Fourier-transform mass spectrometry have been utilized to resolve isobaric lipids, metabolites and tryptic peptides. Here we demonstrate the potential of 15T MALDI-FTICR MSI for molecular pathology in a mouse model of high-grade glioma. The high mass accuracy and resolving power of high field FTICR MSI enabled tumor specific proteoforms, and tumor-specific proteins with overlapping and isobaric isotopic distributions to be clearly resolved. The protein ions detected by MALDI MSI were assigned to proteins identified by region-specific microproteomics (0.8 mm2 regions isolated using laser capture microdissection) on the basis of exact mass and isotopic distribution. These label free quantitative experiments also confirmed the protein expression changes observed by MALDI MSI and revealed changes in key metabolic proteins, which were supported by in-situ metabolite MALDI MSI.
format	article
author	M. Dilillo R. Ait-Belkacem C. Esteve D. Pellegrini S. Nicolardi M. Costa E. Vannini E. L. de Graaf M. Caleo L. A. McDonnell
author_facet	M. Dilillo R. Ait-Belkacem C. Esteve D. Pellegrini S. Nicolardi M. Costa E. Vannini E. L. de Graaf M. Caleo L. A. McDonnell
author_sort	M. Dilillo
title	Ultra-High Mass Resolution MALDI Imaging Mass Spectrometry of Proteins and Metabolites in a Mouse Model of Glioblastoma
title_short	Ultra-High Mass Resolution MALDI Imaging Mass Spectrometry of Proteins and Metabolites in a Mouse Model of Glioblastoma
title_full	Ultra-High Mass Resolution MALDI Imaging Mass Spectrometry of Proteins and Metabolites in a Mouse Model of Glioblastoma
title_fullStr	Ultra-High Mass Resolution MALDI Imaging Mass Spectrometry of Proteins and Metabolites in a Mouse Model of Glioblastoma
title_full_unstemmed	Ultra-High Mass Resolution MALDI Imaging Mass Spectrometry of Proteins and Metabolites in a Mouse Model of Glioblastoma
title_sort	ultra-high mass resolution maldi imaging mass spectrometry of proteins and metabolites in a mouse model of glioblastoma
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/c165c4c1b6644d96ad31944605dd372f
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Ultra-High Mass Resolution MALDI Imaging Mass Spectrometry of Proteins and Metabolites in a Mouse Model of Glioblastoma

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