Dataset Information

MS imaging-guided microproteomics for spatial omics on a single instrument

ABSTRACT: Mass spectrometry imaging (MSI) allows investigating the spatial distribution of chemical compounds directly in biological tissues. As the analytical depth of MSI is limited, MSI needs to be coupled to more sensitive local extraction-based omics approaches to achieve a comprehensive molecular characterization. For this it is important to retain the spatial information provided by MSI for follow-up omics studies. It has been shown that regiospecific MSI data can be used to guide a laser microdissection system (LMD) for ultra-sensitive LC-MS analyses. So far, this combination has required separate and specialized MS instrumentation. Recent advances in dual-source instrumentation, harboring both MALDI and ESI sources, promise state-of-the-art MSI and liquid-based proteomic capabilities on the same MS instrument. In this study, we demonstrate that such an instrument can offer both, fast lipid-based MSI at high mass- and high lateral resolution, and sensitive LC-MS on local protein extracts from the exact same tissue section.

INSTRUMENT(S): Bruker Daltonics flex series

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Breast

DISEASE(S): Breast Cancer

SUBMITTER: Benjamin Balluff

LAB HEAD: Benjamin Balluff

PROVIDER: PXD020362 | Pride | 2020-11-16

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	112000Cells_Slot1-5_1.d.zip	Other
	122000Cells_Slot1-6_1.d.zip	Other
	132000Cells_Slot1-7_1.d.zip	Other
	212000Cells_Slot1-8_1.d.zip	Other
	222000Cells_Slot1-9_1.d.zip	Other

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Publications

MS Imaging-Guided Microproteomics for Spatial Omics on a Single Instrument.

Dewez Frédéric F Oejten Janina J Henkel Corinna C Hebeler Romano R Neuweger Heiko H De Pauw Edwin E Heeren Ron M A RMA Balluff Benjamin B

Proteomics 20200819 23

Mass spectrometry imaging (MSI) allows investigating the spatial distribution of chemical compounds directly in biological tissues. As the analytical depth of MSI is limited, MSI needs to be coupled to more sensitive local extraction-based omics approaches to achieve a comprehensive molecular characterization. For this, it is important to retain the spatial information provided by MSI for follow-up omics studies. It has been shown that regiospecific MSI data can be used to guide a laser microdis ...[more]

PMID: 32767647

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Project description:Aberrant protease activity has been implicated in the etiology of various prevalent diseases including neurodegeneration and cancer, in particular metastasis. Matrix-assisted laser desorption/ionization (MALDI) mass spectrometry imaging (MSI) has recently been established as a key technology for bioanalysis of multiple biomolecular classes such as proteins, lipids, and glycans. However, it has not yet been systematically explored for investigation of a tissue’s endogenous protease activity. In this study, we demonstrate that different tissues, spray-coated with substance P as a tracer, digest this peptide with different time-course profiles. Furthermore, we reveal that distinct cleavage products originating from substance P are generated transiently and that proteolysis can be attenuated by protease inhibitors in a concentration-dependent manner. To show the translational potential of the method, we analyzed protease activity of gastric carcinoma in mice. Our MSI and quantitative proteomics results reveal differential distribution of protease activity – with strongest activity being observed in mouse tumor tissue, suggesting the general applicability of the workflow in animal pharmacology and clinical studies.Aberrant protease activity has been implicated in the etiology of various prevalent diseases including neurodegeneration and cancer, in particular metastasis. Matrix-assisted laser desorption/ionization (MALDI) mass spectrometry imaging (MSI) has recently been established as a key technology for bioanalysis of multiple biomolecular classes such as proteins, lipids, and glycans. However, it has not yet been systematically explored for investigation of a tissue’s endogenous protease activity. In this study, we demonstrate that different tissues, spray-coated with substance P as a tracer, digest this peptide with different time-course profiles. Furthermore, we reveal that distinct cleavage products originating from substance P are generated transiently and that proteolysis can be attenuated by protease inhibitors in a concentration-dependent manner. To show the translational potential of the method, we analyzed protease activity of gastric carcinoma in mice. Our MSI and quantitative proteomics results reveal differential distribution of protease activity – with strongest activity being observed in mouse tumor tissue, suggesting the general applicability of the workflow in animal pharmacology and clinical studies.