scholarly journals Quantitative Mass Spectrometry Imaging of Biological Systems

2021 ◽  
Vol 72 (1) ◽  
Author(s):  
Daisy Unsihuay ◽  
Daniela Mesa Sanchez ◽  
Julia Laskin
Keyword(s):  
Mass Spectrometry ◽  
Mass Spectrometry Imaging ◽  
Matrix Effects ◽  
High Sensitivity ◽  
Biological Tissues ◽  
Annual Review ◽  
Publication Date ◽  
Label Free ◽  
Complex Samples ◽  
Mass Dependent

Mass spectrometry imaging (MSI) is a powerful, label-free technique that provides detailed maps of hundreds of molecules in complex samples with high sensitivity and subcellular spatial resolution. Accurate quantification in MSI relies on a detailed understanding of matrix effects associated with the ionization process along with evaluation of the extraction efficiency and mass-dependent ion losses occurring in the analysis step. We present a critical summary of approaches developed for quantitative MSI of metabolites, lipids, and proteins in biological tissues and discuss their current and future applications. Expected final online publication date for the Annual Review of Physical Chemistry, Volume 72 is April 2021. Please see http://www.annualreviews.org/page/journal/pubdates for revised estimates.

scholarly journals An Ion Mobility-Mass Spectrometry Imaging Workflow

2020 ◽  
Author(s):  
Daniela Mesa Sanchez ◽  
Steve Creger ◽  
Veerupaksh Singla ◽  
Ruwan T. Kurulugama ◽  
John Fjeldsted ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Ion Mobility ◽  
Mass Spectrometry Imaging ◽  
Feature Detection ◽  
Drift Time ◽  
Biological Tissues ◽  
Ion Mobility Mass Spectrometry ◽  
Label Free ◽  
User Input ◽  
Spatially Resolved

<p>Mass spectrometry imaging (MSI) is a powerful technique for the label-free spatially-resolved analysis of biological tissues. Coupling ion mobility (IM) separation with MSI allows separation of isobars in the mobility dimension and increases confidence of peak assignments. Recently, imaging experiments have been implemented on the Agilent 6560 Ion Mobility Quadrupole Time of Flight Mass Spectrometer, making MSI experiments more broadly accessible to the MS community. However, the absence of data analysis software for this system presents a bottleneck. Herein, we present a vendor-specific imaging workflow to visualize IM-MSI data produced on the Agilent IM-MS system. Specifically, we have developed a Python script, the ion mobility-mass spectrometry image creation script (IM-MSIC), which interfaces Agilent’s Mass Hunter Mass Profiler software with the MacCoss lab’s Skyline software and generates drift time and mass-to-charge selected ion images. In the workflow, Mass Profiler is used for an untargeted feature detection. The IM-MSIC script mediates user input of data and extracts ion chronograms utilizing Skyline’s command-line interface, then proceeds towards ion image generation within a single user interface. Ion image post-processing is subsequently performed using different tools implemented in accompanying scripts.</p>

scholarly journals An Ion Mobility-Mass Spectrometry Imaging Workflow

2020 ◽  
Author(s):  
Daniela Mesa Sanchez ◽  
Steve Creger ◽  
Veerupaksh Singla ◽  
Ruwan T. Kurulugama ◽  
John Fjeldsted ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Ion Mobility ◽  
Mass Spectrometry Imaging ◽  
Feature Detection ◽  
Drift Time ◽  
Biological Tissues ◽  
Ion Mobility Mass Spectrometry ◽  
Label Free ◽  
User Input ◽  
Spatially Resolved

<p>Mass spectrometry imaging (MSI) is a powerful technique for the label-free spatially-resolved analysis of biological tissues. Coupling ion mobility (IM) separation with MSI allows separation of isobars in the mobility dimension and increases confidence of peak assignments. Recently, imaging experiments have been implemented on the Agilent 6560 Ion Mobility Quadrupole Time of Flight Mass Spectrometer, making MSI experiments more broadly accessible to the MS community. However, the absence of data analysis software for this system presents a bottleneck. Herein, we present a vendor-specific imaging workflow to visualize IM-MSI data produced on the Agilent IM-MS system. Specifically, we have developed a Python script, the ion mobility-mass spectrometry image creation script (IM-MSIC), which interfaces Agilent’s Mass Hunter Mass Profiler software with the MacCoss lab’s Skyline software and generates drift time and mass-to-charge selected ion images. In the workflow, Mass Profiler is used for an untargeted feature detection. The IM-MSIC script mediates user input of data and extracts ion chronograms utilizing Skyline’s command-line interface, then proceeds towards ion image generation within a single user interface. Ion image post-processing is subsequently performed using different tools implemented in accompanying scripts.</p>

scholarly journals Label-Free Mass Spectrometry-Based Quantification of Linker Histone H1 Variants in Clinical Samples

2020 ◽  
Vol 21 (19) ◽  
pp. 7330
Author(s):  
Roberta Noberini ◽  
Cristina Morales Torres ◽  
Evelyn Oliva Savoia ◽  
Stefania Brandini ◽  
Maria Giovanna Jodice ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Histone H1 ◽  
Histone Variants ◽  
Linker Histone ◽  
Clinical Samples ◽  
Label Free ◽  
Complex Samples ◽  
Linker Histone H1 ◽  
Ideal Tool ◽  
Free Quantification

Epigenetic aberrations have been recognized as important contributors to cancer onset and development, and increasing evidence suggests that linker histone H1 variants may serve as biomarkers useful for patient stratification, as well as play an important role as drivers in cancer. Although traditionally histone H1 levels have been studied using antibody-based methods and RNA expression, these approaches suffer from limitations. Mass spectrometry (MS)-based proteomics represents the ideal tool to accurately quantify relative changes in protein abundance within complex samples. In this study, we used a label-free quantification approach to simultaneously analyze all somatic histone H1 variants in clinical samples and verified its applicability to laser micro-dissected tissue areas containing as low as 1000 cells. We then applied it to breast cancer patient samples, identifying differences in linker histone variants patters in primary triple-negative breast tumors with and without relapse after chemotherapy. This study highlights how label-free quantitation by MS is a valuable option to accurately quantitate histone H1 levels in different types of clinical samples, including very low-abundance patient tissues.

scholarly journals Exemplifying the Screening Power of Mass Spectrometry Imaging over Label-Based Technologies for Simultaneous Monitoring of Drug and Metabolite Distributions in Tissue Sections

2015 ◽  
Vol 21 (2) ◽  
pp. 187-193 ◽  
Author(s):  
Richard J. A. Goodwin ◽  
Anna Nilsson ◽  
C. Logan Mackay ◽  
John G. Swales ◽  
Maria K. Johansson ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Mass Spectrometry Imaging ◽  
Cyclic Peptide ◽  
Analysis Data ◽  
Resolving Power ◽  
High Mass ◽  
Whole Body ◽  
Ion Cyclotron Resonance ◽  
Label Free ◽  
Tissue Sections

Mass spectrometry imaging (MSI) provides pharmaceutical researchers with a suite of technologies to screen and assess compound distributions and relative abundances directly from tissue sections and offer insight into drug discovery–applicable queries such as blood-brain barrier access, tumor penetration/retention, and compound toxicity related to drug retention in specific organs/cell types. Label-free MSI offers advantages over label-based assays, such as quantitative whole-body autoradiography (QWBA), in the ability to simultaneously differentiate and monitor both drug and drug metabolites. Such discrimination is not possible by label-based assays if a drug metabolite still contains the radiolabel. Here, we present data exemplifying the advantages of MSI analysis. Data of the distribution of AZD2820, a therapeutic cyclic peptide, are related to corresponding QWBA data. Distribution of AZD2820 and two metabolites is achieved by MSI, which [14C]AZD2820 QWBA fails to differentiate. Furthermore, the high mass-resolving power of Fourier transform ion cyclotron resonance MS is used to separate closely associated ions.

scholarly journals MALDI-TOF/TOF Tandem Mass Spectrometry Imaging Reveals Non-uniform Distribution of Disaccharide Isomers in Plant Tissues

2020 ◽  
Author(s):  
lingpeng zhan ◽  
xi huang ◽  
jinjuan xue ◽  
huihui liu ◽  
caiqiao xiong ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Tandem Mass Spectrometry ◽  
Mass Spectrometry Imaging ◽  
Biological Tissues ◽  
Plant Tissues ◽  
Tandem Mass ◽  
Imaging Analysis ◽  
Maldi Tof ◽  
Ms Imaging ◽  
Imaging Approach

Mass spectrometry imaging (MSI) has been increasingly utilized in investigating the locations of biomolecules within tissues. However, the isomeric compounds are rarely distinguished in the MS images, due to inability of MSI methods to differentiate isomers in the probing area. Coupling tandem mass spectrometry with MSI can facilitate differentiating isomeric compounds in ion images. Here we apply MALDI-TOF/TOF tandem mass spectrometry imaging approach to revealing the spatial distributions of isomeric disaccharides in plant tissues. First, the MS/MS imaging analysis of disaccharide-matrix droplet spots demonstrated the feasibility of distinguishing isomeric species in tissues, by measuring the relative intensity of specific fragments. Then, we conducted tandem MS imaging of disaccharides in onion bulb tissues, which indicated that sucrose and other unknown non-sucrose disaccharides exhibit heterogeneous locations throughout the tissues. This method enables us to image disaccharide isomers differentially in biological tissues, and to discover new saccharide species in plant. This work also emphasizes the necessity of considering isobaric compounds when interpreting MSI results.<br>

Variable-Temperature Native Mass Spectrometry for Studies of Protein Folding, Stabilities, Assembly, and Molecular Interactions

2021 ◽  
Vol 51 (1) ◽  
Author(s):  
Arthur Laganowsky ◽  
David E. Clemmer ◽  
David H. Russell
Keyword(s):  
Mass Spectrometry ◽  
Dynamic Range ◽  
Protein Complexes ◽  
Noncovalent Interactions ◽  
Variable Temperature ◽  
Regulatory Protein ◽  
Conformational Dynamics ◽  
Native Mass Spectrometry ◽  
Annual Review ◽  
Publication Date

The structures and conformational dynamics of proteins, protein complexes, and their noncovalent interactions with other molecules are controlled specifically by the Gibbs free energy (entropy and enthalpy) of the system. For some organisms, temperature is highly regulated, but the majority of biophysical studies are carried out at room, nonphysiological temperature. In this review, we describe variable-temperature electrospray ionization (vT-ESI) mass spectrometry (MS)-based studies with unparalleled sensitivity, dynamic range, and selectivity for studies of both cold- and heat-induced chemical processes. Such studies provide direct determinations of stabilities, reactivities, and thermodynamic measurements for native and non-native structures of proteins and protein complexes and for protein–ligand interactions. Highlighted in this review are vT-ESI-MS studies that reveal 40 different conformers of chymotrypsin inhibitor 2, a classic two-state (native → unfolded) unfolder, and thermochemistry for a model membrane protein system binding lipid and its regulatory protein. Expected final online publication date for the Annual Review of Biophysics, Volume 51 is May 2022. Please see http://www.annualreviews.org/page/journal/pubdates for revised estimates.

scholarly journals Insight to Functional Conformation and Noncovalent Interactions of Protein-Protein Assembly Using MALDI Mass Spectrometry

Molecules ◽  
2020 ◽  
Vol 25 (21) ◽  
pp. 4979
Author(s):  
Marco Giampà ◽  
Elvira Sgobba
Keyword(s):  
Mass Spectrometry ◽  
Conformational Changes ◽  
Protein Interactions ◽  
Noncovalent Interactions ◽  
Conformational Dynamics ◽  
High Sensitivity ◽  
Maldi Mass Spectrometry ◽  
Noncovalent Interaction ◽  
Ionization Mass ◽  
Label Free

Noncovalent interactions are the keys to the structural organization of biomolecule e.g., proteins, glycans, lipids in the process of molecular recognition processes e.g., enzyme-substrate, antigen-antibody. Protein interactions lead to conformational changes, which dictate the functionality of that protein-protein complex. Besides biophysics techniques, noncovalent interaction and conformational dynamics, can be studied via mass spectrometry (MS), which represents a powerful tool, due to its low sample consumption, high sensitivity, and label-free sample. In this review, the focus will be placed on Matrix-Assisted Laser Desorption Ionization Mass Spectrometry (MALDI-MS) and its role in the analysis of protein-protein noncovalent assemblies exploring the relationship within noncovalent interaction, conformation, and biological function.

scholarly journals Mass spectrometry imaging of triglycerides in biological tissues by laser desorption ionization from silicon nanopost arrays

2019 ◽  
Vol 55 (4) ◽  
pp. e4443 ◽  
Author(s):  
Jarod A. Fincher ◽  
Andrew R. Korte ◽  
Jacqueline E. Dyer ◽  
Sridevi Yadavilli ◽  
Nicholas J. Morris ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Mass Spectrometry Imaging ◽  
Laser Desorption ◽  
Biological Tissues ◽  
Laser Desorption Ionization ◽  
Desorption Ionization

scholarly journals NanoSIMS imaging: an approach for visualizing and quantifying lipids in cells and tissues

2016 ◽  
Vol 65 (3) ◽  
pp. 669-672 ◽  
Author(s):  
Cuiwen He ◽  
Loren G Fong ◽  
Stephen G Young ◽  
Haibo Jiang
Keyword(s):  
Mass Spectrometry ◽  
Spatial Resolution ◽  
Mass Spectrometry Imaging ◽  
Secondary Ion Mass Spectrometry ◽  
High Spatial Resolution ◽  
High Sensitivity ◽  
New Approach ◽  
The Past ◽  
Secondary Ion ◽  
In Cells

Over the past few decades, several approaches have been used to image lipids in cells and tissues, but most have limited spatial resolution and sensitivity. Here, we discuss a relatively new approach, nanoscale secondary ion mass spectrometry imaging, that makes it possible to visualize lipids in cells and tissues in a quantitative fashion and with high spatial resolution and high sensitivity.

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