Imaging mass spectrometry to visualize biomolecule distributions in mouse brain tissue following hemispheric cortical spreading depression

Jones, Emrys A.; Shyti, Reinald; Zeijl, René J. M. van; Heiningen, Sandra H. van; Ferrari, Michel D.; Deelder, André M.; Tolner, Else A.; Maagdenberg, Arn M. J. M. van den; McDonnell, Liam A.

doi:10.1016/j.jprot.2012.06.025

Cited by 37 publications

(29 citation statements)

References 42 publications

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“…MALDI mass spectrometry imaging (MSI) is a technique providing the detection of both the molecular weight and spatial distribution of biomolecules . It has the potential to display colocalized peptides that constitutes an important prerequisite for the identification of proteins and their assignment to histoanatomical structures and pathologies, for example, amyloid .…”

Section: Introductionmentioning

confidence: 99%

MALDI Mass Spectrometry Imaging: A Novel Tool for the Identification and Classification of Amyloidosis

et al. 2017

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Amyloidosis is a group of diseases caused by extracellular accumulation of fibrillar polypeptide aggregates. So far, diagnosis is performed by Congo red staining of tissue sections in combination with polarization microscopy. Subsequent identification of the causative protein by immunohistochemistry harbors some difficulties regarding sensitivity and specificity. Mass spectrometry based approaches have been demonstrated to constitute a reliable method to supplement typing of amyloidosis, but still depend on Congo red staining. In the present study, we used matrix‐assisted laser desorption/ionization mass spectrometry imaging coupled with ion mobility separation (MALDI‐IMS MSI) to investigate amyloid deposits in formalin‐fixed and paraffin‐embedded tissue samples. Utilizing a novel peptide filter method, we found a universal peptide signature for amyloidoses. Furthermore, differences in the peptide composition of ALλ and ATTR amyloid were revealed and used to build a reliable classification model. Integrating the peptide filter in MALDI‐IMS MSI analysis, we developed a bioinformatics workflow facilitating the identification and classification of amyloidosis in a less time and sample‐consuming experimental setup. Our findings demonstrate also the feasibility to investigate the amyloid's protein composition, thus paving the way to establish classification models for the diverse types of amyloidoses and to shed further light on the complex process of amyloidogenesis.

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Section: Introductionmentioning

confidence: 99%

MALDI Mass Spectrometry Imaging: A Novel Tool for the Identification and Classification of Amyloidosis

et al. 2017

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“…MSI allows for partitioning of the tissue surface into regions with the same or similar mass spectrometric (MS) profiles. Hence, it enables the investigation of molecular changes that occur prior to or without any morphologic changes [ 7 ] and the identification of hidden anatomic features.…”

Section: Introductionmentioning

confidence: 99%

Precise Anatomic Localization of Accumulated Lipids in Mfp2 Deficient Murine Brains Through Automated Registration of SIMS Images to the Allen Brain Atlas

Škrášková

Khmelinskii

Abdelmoula

et al. 2015

J. Am. Soc. Mass Spectrom.

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Mass spectrometry imaging (MSI) is a powerful tool for the molecular characterization of specific tissue regions. Histochemical staining provides anatomic information complementary to MSI data. The combination of both modalities has been proven to be beneficial. However, direct comparison of histology based and mass spectrometry-based molecular images can become problematic because of potential tissue damages or changes caused by different sample preparation. Curated atlases such as the Allen Brain Atlas (ABA) offer a collection of highly detailed and standardized anatomic information. Direct comparison of MSI brain data to the ABA allows for conclusions to be drawn on precise anatomic localization of the molecular signal. Here we applied secondary ion mass spectrometry imaging at high spatial resolution to study brains of knock-out mouse models with impaired peroxisomal β-oxidation. Murine models were lacking D-multifunctional protein (MFP2), which is involved in degradation of very long chain fatty acids. SIMS imaging revealed deposits of fatty acids within distinct brain regions. Manual comparison of the MSI data with the histologic stains did not allow for an unequivocal anatomic identification of the fatty acids rich regions. We further employed an automated pipeline for co-registration of the SIMS data to the ABA. The registration enabled precise anatomic annotation of the brain structures with the revealed lipid deposits. The precise anatomic localization allowed for a deeper insight into the pathology of Mfp2 deficient mouse models.Graphical AbstractᅟElectronic supplementary materialThe online version of this article (doi:10.1007/s13361-015-1146-6) contains supplementary material, which is available to authorized users.

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“…) and non‐negative matrix factorization (NMF) (Jones et al . ) have been applied. However, many studies report combinations of MVA methods such as PCA and hierarchical cluster analysis (De Sio et al .…”

Section: Discussionmentioning

confidence: 99%

Molecular imaging mass spectrometry for probing protein dynamics in neurodegenerative disease pathology

Michno

Wehrli

Blennow

et al. 2018

Journal of Neurochemistry

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Recent advances in the understanding of basic pathological mechanisms in various neurological diseases depend directly on the development of novel bioanalytical technologies that allow sensitive and specific chemical imaging at high resolution in cells and tissues. Mass spectrometry-based molecular imaging (IMS) has gained increasing popularity in biomedical research for mapping the spatial distribution of molecular species in situ. The technology allows for comprehensive, untargeted delineation of in situ distribution profiles of metabolites, lipids, peptides and proteins. A major advantage of IMS over conventional histochemical techniques is its superior molecular specificity. Imaging mass spectrometry has therefore great potential for probing molecular regulations in CNS-derived tissues and cells for understanding neurodegenerative disease mechanism. The goal of this review is to familiarize the reader with the experimental workflow, instrumental developments and methodological challenges as well as to give a concise overview of the major advances and recent developments and applications of IMS-based protein and peptide profiling with particular focus on neurodegenerative diseases. This article is part of the Special Issue "Proteomics".

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Imaging mass spectrometry to visualize biomolecule distributions in mouse brain tissue following hemispheric cortical spreading depression

Cited by 37 publications

References 42 publications

MALDI Mass Spectrometry Imaging: A Novel Tool for the Identification and Classification of Amyloidosis

MALDI Mass Spectrometry Imaging: A Novel Tool for the Identification and Classification of Amyloidosis

Precise Anatomic Localization of Accumulated Lipids in Mfp2 Deficient Murine Brains Through Automated Registration of SIMS Images to the Allen Brain Atlas

Molecular imaging mass spectrometry for probing protein dynamics in neurodegenerative disease pathology

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