Reduced Hemoglobin Signal and Improved Detection of Endogenous Proteins in Blood-Rich Tissues for MALDI Mass Spectrometry Imaging

Lin, Monica; Eberlin, Lívia S.; Seeley, Erin H.

doi:10.1021/jasms.1c00300

Cited by 10 publications

(10 citation statements)

References 37 publications

(45 reference statements)

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“…Many researchers have explored tissue washing strategies that aid in protein analysis. 106,107 Some notable examples of intact protein analysis include 23 kDa βcrystallins in lens tissue, 108 advanced oxidation modifications, 46 and ultrahigh mass resolution using FTICR instruments. 46,109 Additionally, novel matrices are being developed to assist in the analysis of intact, high molecular weight proteins.…”

Section: Proteins and Peptidesmentioning

confidence: 99%

“…To best ionize proteins directly from samples, sections are typically washed to remove endogenous salts, metabolites, and lipids. , The removal of these lower molecular weight abundant molecules can assist the ionization of intact proteins. Many researchers have explored tissue washing strategies that aid in protein analysis. , Some notable examples of intact protein analysis include 23 kDa β-crystallins in lens tissue, advanced oxidation modifications, and ultrahigh mass resolution using FTICR instruments. , Additionally, novel matrices are being developed to assist in the analysis of intact, high molecular weight proteins …”

Section: Sample Preparation Protocolsmentioning

confidence: 99%

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A Guide to MALDI Imaging Mass Spectrometry for Tissues

Moore,

Charkoftaki

2023

J. Proteome Res.

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Imaging mass spectrometry is a well-established technology that can easily and succinctly communicate the spatial localization of molecules within samples. This review communicates the recent advances in the field, with a specific focus on matrix-assisted laser desorption/ionization (MALDI) imaging mass spectrometry (IMS) applied on tissues. The general sample preparation strategies for different analyte classes are explored, including special considerations for sample types (fresh frozen or formalin-fixed,) strategies for various analytes (lipids, metabolites, proteins, peptides, and glycans) and how multimodal imaging strategies can leverage the strengths of each approach is mentioned. This work explores appropriate experimental design approaches and standardization of processes needed for successful studies, as well as the various data analysis platforms available to analyze data and their strengths. The review concludes with applications of imaging mass spectrometry in various fields, with a focus on medical research, and some examples from plant biology and microbe metabolism are mentioned, to illustrate the breadth and depth of MALDI IMS.

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Section: Proteins and Peptidesmentioning

confidence: 99%

Section: Sample Preparation Protocolsmentioning

confidence: 99%

A Guide to MALDI Imaging Mass Spectrometry for Tissues

Moore,

Charkoftaki

2023

J. Proteome Res.

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“…The surface distance between each recorded mass spectrum while scanning will determine the pixel size of the resulting image. 7 MSI has been used to detect endogenous molecules such as lipids, 8 proteins, 9 peptides, 10 metabolites, 11 and glycans 12 as well as exogenous molecules like certain small molecule drugs 13 and polymers. 14 Desorption electrospray ionization (DESI) is an ambient ionization technique with which tissue sections can be analyzed without sample pretreatment.…”

Section: ■ Introductionmentioning

confidence: 99%

Improved Detection of Tryptic Peptides from Tissue Sections Using Desorption Electrospray Ionization Mass Spectrometry Imaging

Bottomley,

Phillips,

Hart

2024

J. Am. Soc. Mass Spectrom.

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DESI-MSI is an ambient ionization technique used frequently for the detection of lipids, small molecules, and drug targets. Until recently, DESI had only limited use for the detection of proteins and peptides due to the setup and needs around deconvolution of data resulting in a small number of species being detected at lower spatial resolution. There are known differences in the ion species detected using DESI and MALDI for nonpeptide molecules, and here, we identify that this extends to proteomic species. DESI MS images were obtained for tissue sections of mouse and rat brain using a precommercial heated inlet (approximately 450 °C) to the mass spectrometer. Ion mobility separation resolved spectral overlap of peptide ions and significantly improved the detection of multiply charged species. The images acquired were of pixel size 100 μm (rat brain) and 50 μm (mouse brain), respectively. Observed tryptic peptides were filtered against proteomic target lists, generated by LC−MS, enabling tentative protein assignment for each peptide ion image. Precise localizations of peptide ions identified by DESI and MALDI were found to be comparable. Some spatially localized peptides ions were observed in DESI that were not found in the MALDI replicates, typically, multiply charged species with a low mass to charge ratio. This method demonstrates the potential of DESI-MSI to detect large numbers of tryptic peptides from tissue sections with enhanced spatial resolution when compared to previous DESI-MSI studies.

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“…7 Sample preparation for MALDI MSI is crucial and is closely related to tissue integrity, analyte delocalization, imaging resolution, ionization efficiency, throughput and reproducibility. [8][9][10] Many sample preparation techniques have been reported, such as sample handing (storage, cutting, and mounting), 11 tissue treatment (washing, digestion, and derivatization), 6,12,13 and matrix application (spray coating and solvent selection). 14 In turn, tissue slice thickness is a critical factor influencing the MALDI MS signal quality and imaging quality, especially for high mass analysis.…”

Section: Introductionmentioning

confidence: 99%