Bioimaging TOF‐SIMS: localization of cholesterol in rat kidney sections

Nygren, Håkan; Malmberg, Per; Kriegeskotte, C.; Arlinghaus, Heinrich F.

doi:10.1016/j.febslet.2004.04.052

Cited by 106 publications

(59 citation statements)

References 19 publications

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“…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. Surface modification techniques such as metal assisted SIMS or matrix enhanced SIMS can be used to extend the useable mass range to small peptides and proteins [14,[21][22][23][24][25][26][27][28][29][30].…”

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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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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“…Nygren et al have exploited sample metallization to record the distribution of cholesterol in a rat kidney tissue section of a Male Sprague-Dawley, which revealed a high concentration in the nuclear region of epithelial cells. [29] In this case the cholesterol image was obtained using the silver cationized molecular ions.…”

mentioning

confidence: 99%

Higher sensitivity secondary ion mass spectrometry of biological molecules for high resolution, chemically specific imaging

McDonnell

Heeren

Lange

et al. 2006

J. Am. Soc. Mass Spectrom.

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To expand the role of high spatial resolution secondary ion mass spectrometry (SIMS) in biological studies, numerous developments have been reported in recent years for enhancing the molecular ion yield of high mass molecules. These include both surface modification, including matrix-enhanced SIMS and metal-assisted SIMS, and polyatomic primary ions. Using rat brain tissue sections and a bismuth primary ion gun able to produce atomic and polyatomic primary ions, we report here how the sensitivity enhancements provided by these developments are additive. Combined surface modification and polyatomic primary ions provided Ϸ15.8 times more signal than using atomic primary ions on the raw sample, whereas surface modification and polyatomic primary ions yield Ϸ3.8 and Ϸ8.4 times more signal. This higher sensitivity is used to generate chemically specific images of higher mass biomolecules using a single molecular ion

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“…It is currently undergoing a revival with the advent of novel primary ion beam types using molecular clusters (Gold or Bismuth cluster sources) [40] or larger molecules (C60) [41]. This approach extends the useful mass range into the realm of lipids [42] and cholesterol [43]. Yet, the real promise of high-resolution imaging of larger biomolecules (peptides and proteins) has yet to be shown with SIMS imaging without surface modifications.…”

Section: Mass Spectrometric Imagingmentioning

confidence: 99%

Proteome imaging: A closer look at life's organization

Heeren

2005

Proteomics

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Imaging the proteome is a term that is used in many different contexts. The term implies that the entire cohort of proteins and their modifications are visualized. This unfortunately is not the case. In this mini-review, a concise overview is provided on different imaging technologies that are currently used to investigate the structure, function and dynamics of proteins and their organization. These techniques have been selected for review based on the unique insights they provide in subsets of the proteome. These techniques have been illustrated with practical examples of their merits. Mass spectrometry-based imaging technologies are playing a key role in proteome research and have been reviewed in more detail. They hold the promise of detailed molecular insight in the spatial organization of living system.

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Bioimaging TOF‐SIMS: localization of cholesterol in rat kidney sections

Cited by 106 publications

References 19 publications

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

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

Higher sensitivity secondary ion mass spectrometry of biological molecules for high resolution, chemically specific imaging

Proteome imaging: A closer look at life's organization

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