Imaging mass spectrometry: A new technology for the analysis of protein expression in mammalian tissues

Stoeckli, Markus; Chaurand, Pierre; Hallahan, Dennis E.; Caprioli, Richard M.

doi:10.1038/86573

Cited by 1,108 publications

(870 citation statements)

References 22 publications

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“…In this technique, the proteins and peptides in thin sections are directly imaged (66). Typically, a frozen tissue section is mounted on a target plate and is covered with an energy-absorbing matrix, for example, sinapinic acid.…”

Section: Neuropeptides In Disease Modelsmentioning

confidence: 99%

Neuropeptidomics: MS Applied to the Discovery of Novel Peptides from the Brain

Svensson¹,

Sköld²,

Nilsson³

et al. 2007

Anal. Chem.

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Section: Neuropeptides In Disease Modelsmentioning

confidence: 99%

Neuropeptidomics: MS Applied to the Discovery of Novel Peptides from the Brain

Svensson¹,

Sköld²,

Nilsson³

et al. 2007

Anal. Chem.

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“…Recently, imaging mass spectrometry (IMS) has been recognized as a proteomic tool for in situ spatial analysis of (diseased) tissue [9,10]. Matrixassisted laser desorption/ionization (MALDI) MS has been shown to be able to determine the localization of native biomolecular components like proteins and peptides in tissue [11][12][13][14][15]. Often, the data includes several unknown species with a spatial distribution that indicates it is associated with a disease or biochemicallyaltered region of the tissue.…”

mentioning

confidence: 99%

“…Both MALDI [16,17] and secondary ion mass spectrometry (SIMS) [18 -20] approaches can provide good mass resolution images (ϳ10 4 ). MALDI can be used for the analysis of high mass species (up to 100 kDa) at low spatial resolution (pixel size Ͼ25 m) [11]. Very high spatial resolution is obtained using SIMS (pixel size Ͻ1 m) [19], however its sensitivity rapidly decreases with increasing mass, making the technique less suited for protein analysis.…”

mentioning

confidence: 99%

Imaging of peptides in the rat brain using MALDI-FTICR mass spectrometry

Taban

Altelaar

Burgt

et al. 2007

J. Am. Soc. Mass Spectrom.

148

136

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Analytical methods are pursued to measure the identity and location of biomolecules down to the subcellular ( m) level. Available mass spectrometric imaging methods either compromise localization accuracy or identification accuracy in their analysis of surface biomolecules. In this study, imaging FTICR-MS is applied for the spatially resolved mass analysis of rat brain tissue with the aim to optimize protein identification by the high mass accuracy and online MS/MS capabilities of the technique. Mass accuracies up to 6 ppm were obtained in the direct MALDI-analysis of the tissue together with a spatial resolution of 200 m. The spatial distributions of biomolecules differing in mass by less than 0.1 Da could be resolved, and are shown to differ significantly. Online MS/MS analysis of selected ions was demonstrated. A comparison of the FTICR-MS imaging results with stigmatic TOF imaging on the same sample is presented. To reduce the extended measuring times involved, it is recommended to restrict the FTICR-MS analyses to areas of interest as can be preselected by other, faster imaging methods. (J Am Soc Mass Spectrom 2007, 18, 145-151)

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“…Highly sensitive investigation of single cells, neurons, or tissue areas is a field of dramatically growing consideration [18 -24]. Due to instrumental and methodological limitations, MALDI imaging has so far been limited to a lateral resolution of approximately 30 m [18,[25][26][27][28][29][30], limiting its application to relatively large structures.…”

mentioning

confidence: 99%

Scanning microprobe matrix-assisted laser desorption ionization (SMALDI) mass spectrometry: Instrumentation for sub-micrometer resolved LDI and MALDI surface analysis

Spengler

Hubert

2002

J. Am. Soc. Mass Spectrom.

269

256

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A new instrument and method is described for laterally resolved mass spectrometric surface analysis. Fields of application are in both the life sciences and the material sciences. The instrument provides for imaging of the distribution of selected sample components from natural and artificial surfaces. Samples are either analyzed by laser desorption ionization (LDI) time-of-flight mass spectrometry or, after preparation with a suitable matrix, by matrixassisted laser desorption ionization (MALDI) mass spectrometry. Areas of 100 ϫ 100 m are scanned with minimal increments of 0.25 m, and between 10,000 and 160,000 mass spectra are acquired per image within 3 to 50 min (scan rate up to 50 pixels per s). The effective lateral resolution is in the range of 0.6 to 1.5 m depending on sample properties, preparation methods and laser wavelength. Optical investigation of the same sample area by UV confocal scanning laser microscopy was found to be very attractive in combination with scanning MALDI mass analysis because pixel-identical images can be created with both techniques providing for a strong increase in analytical information. This article describes the method and instrumentation, including first applicational examples in elemental analysis, imaging of pine tree roots, and investigation of MALDI sample morphology in biomolecular analysis. (J Am Soc Mass Spectrom 2002, 13, 735-748)

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Imaging mass spectrometry: A new technology for the analysis of protein expression in mammalian tissues

Cited by 1,108 publications

References 22 publications

Neuropeptidomics: MS Applied to the Discovery of Novel Peptides from the Brain

Neuropeptidomics: MS Applied to the Discovery of Novel Peptides from the Brain

Imaging of peptides in the rat brain using MALDI-FTICR mass spectrometry

Scanning microprobe matrix-assisted laser desorption ionization (SMALDI) mass spectrometry: Instrumentation for sub-micrometer resolved LDI and MALDI surface analysis

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