Imaging mass spectrometry at cellular length scales

Altelaar, Maarten; Luxembourg, S.L.; McDonnell, Liam A.; Piersma, Sander R.; Heeren, Ron M. A.

doi:10.1038/nprot.2007.117

Cited by 102 publications

(78 citation statements)

References 92 publications

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“…One of the advantages of IMS is the ability to discriminate among structurally heterogeneous molecules by their masses ( 33,34 ) and image them simultaneously. A recent breakthrough in statistical IMS (35)(36)(37)(38) has enabled comprehensive imaging analysis of GPL molecular families.…”

Section: Euthanization Of Animals and Tissue Extractionmentioning

confidence: 99%

“…To extract important information from such large IMS data sets (40,000 data points for the four developing brain sections), PCA, an unsupervised multivariate data analysis technique ( 37,38,56 ), was used. PCA is useful for obtaining an overview of entire data sets (i.e., general trends in fl uctuations in GPLs' expression with development) before proceeding to a more detailed data analysis (i.e., visualization of individual GPLs).…”

Section: Statistical Analysis Revealed Temporal and Spatial Changes Imentioning

confidence: 99%

See 1 more Smart Citation

Visualization of the cell-selective distribution of PUFA-containing phosphatidylcholines in mouse brain by imaging mass spectrometry

Sugiura

Konishi

Zaima

et al. 2009

Journal of Lipid Research

182

191

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Section: Euthanization Of Animals and Tissue Extractionmentioning

confidence: 99%

Section: Statistical Analysis Revealed Temporal and Spatial Changes Imentioning

confidence: 99%

Visualization of the cell-selective distribution of PUFA-containing phosphatidylcholines in mouse brain by imaging mass spectrometry

Sugiura

Konishi

Zaima

et al. 2009

Journal of Lipid Research

182

191

View full text Add to dashboard Cite

“…This algorithm can be adapted for all datasets of similar nature in imaging mass spectrometry, particularly the mass microscope being developed as part of our high-resolution imaging mass spectrometry research efforts [25,26].…”

Section: Discussionmentioning

confidence: 99%

Automated, feature-based image alignment for high-resolution imaging mass spectrometry of large biological samples

Broersen

Liere

Altelaar

et al. 2008

J. Am. Soc. Mass Spectrom.

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High-resolution imaging mass spectrometry of large biological samples is the goal of several research groups. In mosaic imaging, the most common method, the large sample is divided into a mosaic of small areas that are then analyzed with high resolution. Here we present an automated alignment routine that uses principal component analysis to reduce the uncorrelated noise in the imaging datasets, which previously obstructed automated image alignment. An additional signal quality metric ensures that only those regions with sufficient signal quality are considered. We demonstrate that this algorithm provides superior alignment performance than manual stitching and can be used to automatically align large imaging mass spectrometry datasets comprising many individual mosaic tiles. (J Am Soc Mass Spectrom 2008, 19, 823-832) © 2008 American Society for Mass Spectrometry I maging mass spectrometry is a rapidly developing analytical tool because it provides the ability to map the profiles of specific biomolecules, in which the intrinsic mass of the molecule differentiates between any modified forms; to record the distributions of multiple analytes in parallel; and to perform these analyses without a label and with clinical samples [1]. This combination of specificity, parallel detection, and non-targeted analysis has led to great excitement for its potential as a discovery tool.It is the goal of many research groups to be able to perform high-resolution analysis of large samples, thus combining the ability to examine distributions between organs/tumors and their surroundings as well as to investigate the subcellular/intracellular locations of the biomolecules. The central premise of this approach is that the subcellular locations will provide some of the information required to explain differences in the more global patterns.High spatial resolution measurements are a wellestablished ability of secondary ion mass spectrometry (SIMS). Recent advances in both ionization efficiency (polyatomic primary ions) and sample preparation have significantly improved the sensitivity for detecting intact, medium-sized molecular ions (Ͻ1000 Da) from tissues and cells [1][2][3][4][5][6]. High-resolution images of small peptides, lipids, cholesterol, vitamins, and pharmaceuticals have all been reported, and through the use of large polyatomic primary ions three-dimensional (3D) molecular imaging results are beginning to appear [7][8][9].The images are normally created by moving the ionization beam in a set pattern across the sample and performing mass analysis at each point of the raster (spatially correlated mass spectrometry). The raster pattern typically uses 8-or 10-bit encoding; as a result the maximum analysis field contains 256 ϫ 256 (or 1024 ϫ 1024) pixels. In a typical high spatial resolution SIMS measurement the pixel size is about 200 nm, meaning maximum analysis areas of approximately 50 or 200 m, respectively. This is much smaller than many of the biological samples of interest; for example, a tissue section of an adult rat ...

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“…[12][13][14][15] The method involves spraying or multiple spotting of a chemical matrix solution on the target tissue specimen attached to a MALDI sample plate. Molecules contained in an area (50 µm or less) overlaid by matrix droplets are extracted and co-crystallized after the organic solvent has dried.…”

Section: Maldi-ims Maldi-ims Developed Bymentioning

confidence: 99%

Molecular and Functional Analysis of Cellular Phenomena Using Single-Cell Mass Spectrometry

Tsuyama

Mizuno

Masujima

2012

Biological & Pharmaceutical Bulletin

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Single-cell analysis has attracted attention in many fields of biological studies as a tool to survey the precise mechanisms of cellular and molecular behavior. The development of sensitive mass spectrometry allows the study of molecules in single cells or small regions. Matrix-assisted laser desorption/ionization imaging mass spectrometry and secondary-ion mass spectrometry use in situ ionization of specimens on sample plates to visualize molecular distributions as images from mass spectra. Several single-cell mass spectrometry technologies that initially recover a single cell followed by ionization have been developed. Among them, only nanospray-mediated sampling and ionization named Live Single-cell Mass Spectrometry can be used for real-time analysis. This paper explains that method in detail.

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Imaging mass spectrometry at cellular length scales

Cited by 102 publications

References 92 publications

Visualization of the cell-selective distribution of PUFA-containing phosphatidylcholines in mouse brain by imaging mass spectrometry

Visualization of the cell-selective distribution of PUFA-containing phosphatidylcholines in mouse brain by imaging mass spectrometry

Automated, feature-based image alignment for high-resolution imaging mass spectrometry of large biological samples

Molecular and Functional Analysis of Cellular Phenomena Using Single-Cell Mass Spectrometry

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