Molecular imaging of amyloid β peptides in mouse brain sections using mass spectrometry

Stoeckli, Markus; Staab, Dieter; Staufenbiel, Matthias; Wiederhold, Karl‐Heinz; Signor, Luca

doi:10.1016/s0003-2697(02)00386-x

Cited by 217 publications

(197 citation statements)

References 13 publications

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“…In this study, the detection limits for the two peptides were not exactly determined. However, tissue spiking experiments showed the lower limit of detection to be in the range of nanomolar concentrations, which is in agreement with previously published peptide work [4].…”

Section: Resultssupporting

confidence: 92%

“…M atrix-assisted laser desorption/ionization (MALDI) mass spectrometric imaging (MSI) [1] is a novel molecular imaging method, which has already proven its value in numerous studies, including measurement of neuropeptides [2][3][4] in mouse brain sections and small organic compound distributions measured on whole-body tissue sections [5,6]. However, the full potential of this method still remains to be explored.…”

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confidence: 99%

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Imaging of aβ-peptide distribution in whole-body mice sections by MALDI mass spectrometry

Stoeckli

Staab

Schweitzer

et al. 2007

J. Am. Soc. Mass Spectrom.

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Section: Resultssupporting

confidence: 92%

mentioning

confidence: 99%

Imaging of aβ-peptide distribution in whole-body mice sections by MALDI mass spectrometry

Stoeckli

Staab

Schweitzer

et al. 2007

J. Am. Soc. Mass Spectrom.

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“…Several groups have demonstrated the ability to examine sample heterogeneity and investigate peptide and protein distribution in cellular and tissue samples [16 -22] with MALDI MS. To date, such work has focused on mammalian tissues such as measuring the distribution of amyloid ␤ in the mouse brain [22]. These studies present the exciting ability to distinguish various tissue types within a tissue section; however, the small cell sizes in such samples do not allow for resolution at the cellular level, so that, for example, the neuropeptide in particular cells can be determined.…”

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confidence: 99%

Spatial profiling invertebrate ganglia using MALDI MS

Kruse

Sweedler

2003

J. Am. Soc. Mass Spectrom.

108

100

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The ability of MALDI TOF MS to spatially map peptides and proteins directly from a tissue is an exciting advance to imaging mass spectrometry. Recent advances in instrumentation for MS have resulted in instruments capable of achieving several micron spatial resolution while acquiring high-resolution mass spectra. Currently, the ability to obtain high quality mass spectrometric images depends on sample preparation protocols that often result in limited spatial resolution. A number of sample preparation and matrix deposition protocols are evaluated for spatial profiling of Aplysia californica exocrine gland and neuronal tissues. Such samples are different from mammalian tissues, but make good targets for method optimization because of the wealth of biochemical information available on neuropeptide processing and distribution. Electrospray matrix deposition and a variety of freezing methods have been found to be optimum for these invertebrate tissues,

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“…The basis of MALDI was developed by Koichi Tanaka (Nobel laureate in chemistry in 2002), and sophisticated by Franz Hillenkamp and Michael Karas (Karas and Hillenkamp 1988), allowing the analysis of large numbers of biomolecules ranging from small metabolite molecules (m/z<1000) (Garrett et al 2006;Khatib-Shahidi et al 2006) to much larger proteins with molecular weights of 10 5 (Chaurand et al 2006;Stoeckli et al 2002), by covering them with a matrix and ionizing them using a pulse laser beam. High-molecular weight materials, such as proteins and DNA, are fragile and tend to be fragmented when ionized by conventional ionization methods.…”

Section: Principle Of Msmentioning

confidence: 99%

Imaging mass spectrometry: principle and application

2009

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Imaging mass spectrometry (IMS) is twodimensional mass spectrometry to visualize the spatial distribution of biomolecules, which does not need either separation or purification of target molecules, and enables us to monitor not only the identification of unknown molecules but also the localization of numerous molecules simultaneously. Among the ionization techniques, matrix assisted laser desorption/ionization (MALDI) is one of the most generally used for IMS, which allows the analysis of numerous biomolecules ranging over wide molecular weights. Proper selection and preparation of matrix is essential for successful imaging using IMS. Tandem mass spectrometry, which is referred to MS n , enables the structural analysis of a molecule detected by the first step of IMS. Applications of IMS were initially developed for studying proteins or peptides. At present, however, targets of IMS research have expanded to the imaging of small endogenous metabolites such as lipids, exogenous drug pharmacokinetics, exploring new disease markers, and other new scientific fields. We hope that this new technology will open a new era for biophysics.

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Molecular imaging of amyloid β peptides in mouse brain sections using mass spectrometry

Cited by 217 publications

References 13 publications

Imaging of aβ-peptide distribution in whole-body mice sections by MALDI mass spectrometry

Imaging of aβ-peptide distribution in whole-body mice sections by MALDI mass spectrometry

Spatial profiling invertebrate ganglia using MALDI MS

Imaging mass spectrometry: principle and application

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