Ganglioside Detection from Formalin-Fixed Human Brain Tissue Utilizing MALDI Imaging Mass Spectrometry

Harris, Aaron J.; Roseborough, Austyn D.; Mor, Rahul; Yeung, Ken K.‐C.; Whitehead, Shawn N.

doi:10.1021/jasms.9b00110

Cited by 30 publications

(26 citation statements)

References 82 publications

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“…Due to our interest in sample preparation strategies for enriching neuropeptides for MS imaging analysis [14], here we explore the use of chemical modifiers, specifically formalin fixation, to identify neuropeptide localization in the crustacean brain. Our strategy is similar to a previous study from Harris et al, where they treated formalin fixation as a tissue wash to enhance lipid detection [33]. In this communication, we compare the neuropeptides that were detected between control, untreated tissue sections, and formalin-fixed tissue sections.…”

Section: Introductionmentioning

confidence: 93%

Complementary neuropeptide detection in crustacean brain by mass spectrometry imaging using formalin and alternative aqueous tissue washes

Buchberger

Johnson

2021

Anal Bioanal Chem

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Neuropeptides are low abundance signaling molecules that modulate almost every physiological process, and dysregulation of neuropeptides is implicated in disease pathology. Mass spectrometry (MS) imaging is becoming increasingly useful for studying neuropeptides as new sample preparation methods for improving neuropeptide detection are developed. In particular, proper tissue washes prior to MS imaging have shown to be quick and effective strategies for increasing the number of detectable neuropeptides. Treating tissues with solvents could result in either gain or loss of detection of analytes, and characterization of these wash effects is important for studies targeting sub-classes of neuropeptides. In this communication, we apply aqueous tissue washes that contain sodium phosphate salts, including 10% neutral buffered formalin (NBF), on crustacean brain tissues. Our optimized method resulted in complementary identification of neuropeptides between washed and unwashed tissues, indicating that our wash protocol may be used to increase total neuropeptide identifications. Finally, we show that identical neuropeptides were detected between tissues treated with 10% NBF and an aqueous 1% w/v sodium phosphate solution (composition of 10% NBF without formaldehyde), suggesting that utilizing a salt solution wash affects neuropeptide detection and formaldehyde does not affect neuropeptide detection when our wash protocol is performed.

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Section: Introductionmentioning

confidence: 93%

Complementary neuropeptide detection in crustacean brain by mass spectrometry imaging using formalin and alternative aqueous tissue washes

Buchberger

Johnson

2021

Anal Bioanal Chem

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“…In fact, the seminolipids (16:0/16:0), (18:1/16:0), and (18:0/16:0) were localized mainly in the middle and inner layers of the tubules. Single layer-specific seminolipids (14:0/16:0), (16:0/16:1), and (17:0/16:0) were localized in layer 2, 1, and 3, respectively [99,100].…”

Section: Animal Tissues As Exemplary For Molecular Imaging: Brain Testicles and Kidneymentioning

confidence: 98%

“…Another interesting work, which employed a protocol based on ammonium formate washing, is the detection and spatial localization of gangliosides, identified by on-tissue MS/MS, in negative mode on formalin-fixed rat brain tissue. They were mainly localized in the gray matter (cerebral cortex) compared with white matter (corpus callosum) [99].…”

Section: Animal Tissues As Exemplary For Molecular Imaging: Brain Testicles and Kidneymentioning

confidence: 99%

Unravel the Local Complexity of Biological Environments by MALDI Mass Spectrometry Imaging

Sgobba

Daguerre

Giampà

2021

IJMS

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Classic metabolomic methods have proven to be very useful to study functional biology and variation in the chemical composition of different tissues. However, they do not provide any information in terms of spatial localization within fine structures. Matrix-assisted laser desorption ionization mass spectrometry imaging (MALDI MSI) does and reaches at best a spatial resolution of 0.25 μm depending on the laser setup, making it a very powerful tool to analyze the local complexity of biological samples at the cellular level. Here, we intend to give an overview of the diversity of the molecules and localizations analyzed using this method as well as to update on the latest adaptations made to circumvent the complexity of samples. MALDI MSI has been widely used in medical sciences and is now developing in research areas as diverse as entomology, microbiology, plant biology, and plant–microbe interactions, the rhizobia symbiosis being the most exhaustively described so far. Those are the fields of interest on which we will focus to demonstrate MALDI MSI strengths in characterizing the spatial distributions of metabolites, lipids, and peptides in relation to biological questions.

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“…One way to improve the signal of these analytes is by washing tissues with specific solvents prior to analysis. Common washing solvents include ethanol, chloroform, xylene, and isopropanol, among other organic solvents, though ethanol has been particularly useful for neuropeptide analysis (Ly et al, 2019;Buchberger et al, 2020) and ammonium formate for removing salt adducts (Angel et al, 2012;Erich et al, 2019;Harris et al, 2020). However, there have been other interesting methods, such as using supercritical fluid CO 2 to remove lipids (Matsushita et al, 2017) and simply using xylene followed by ethanol for the removal of paraffin from formalin-fixed, paraffin-embedded tissue (Paine et al, 2018).…”

Section: B Decreasing Spectral Complexitymentioning

confidence: 99%

Advances in High‐resolution Maldi Mass Spectrometry for Neurobiology

DeLaney

Phetsanthad

2020

Mass Spectrometry Reviews

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Research in the field of neurobiology and neurochemistry has seen a rapid expansion in the last several years due to advances in technologies and instrumentation, facilitating the detection of biomolecules critical to the complex signaling of neurons. Part of this growth has been due to the development and implementation of high-resolution Fourier transform (FT) mass spectrometry (MS), as is offered by FT ion cyclotron resonance (FTICR) and Orbitrap mass analyzers, which improves the accuracy of measurements and helps resolve the complex biological mixtures often analyzed in the nervous system. The coupling of matrixassisted laser desorption/ionization (MALDI) with high-resolution MS has drastically expanded the information that can be obtained with these complex samples. This review discusses notable technical developments in MALDI-FTICR and MALDI-Orbitrap platforms and their applications toward molecules in the nervous system, including sequence elucidation and profiling with de novo sequencing, analysis of post-translational modifications, in situ analysis, key advances in sample preparation and handling, quantitation, and imaging. Notable novel applications are also discussed to highlight key developments critical to advancing our understanding of neurobiology and providing insight into the exciting future of this field.

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Ganglioside Detection from Formalin-Fixed Human Brain Tissue Utilizing MALDI Imaging Mass Spectrometry

Cited by 30 publications

References 82 publications

Complementary neuropeptide detection in crustacean brain by mass spectrometry imaging using formalin and alternative aqueous tissue washes

Complementary neuropeptide detection in crustacean brain by mass spectrometry imaging using formalin and alternative aqueous tissue washes

Unravel the Local Complexity of Biological Environments by MALDI Mass Spectrometry Imaging

Advances in High‐resolution Maldi Mass Spectrometry for Neurobiology

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