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PXD011104

PXD011104 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleTissue protease activity with MALDI MSI
DescriptionAberrant 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.
HostingRepositoryPRIDE
AnnounceDate2018-10-25
AnnouncementXMLSubmission_2018-10-25_08:42:16.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterKatrin Erich
SpeciesList scientific name: Mus musculus (Mouse); NCBI TaxID: 10090; scientific name: Bos taurus (Bovine); NCBI TaxID: 9913;
ModificationListNo PTMs are included in the dataset
InstrumentBruker Daltonics solarix series; ultraflex
Dataset History
RevisionDatetimeStatusChangeLog Entry
02018-09-17 01:22:35ID requested
12018-10-25 08:42:17announced
Publication List
Erich K, Reinle K, M, ü, ller T, Munteanu B, Sammour DA, Hinsenkamp I, Gutting T, Burgermeister E, Findeisen P, Ebert MP, Krijgsveld J, Hopf C, Spatial Distribution of Endogenous Tissue Protease Activity in Gastric Carcinoma Mapped by MALDI Mass Spectrometry Imaging. Mol Cell Proteomics, 18(1):151-161(2019) [pubmed]
Keyword List
curator keyword: Technical, Biomedical
submitter keyword: MALDI-MSI, Protease activity,
Contact List
Prof. Dr. Carsten Hopf
contact affiliationCenter for Mass Spectrometry and Optical Spectroscopy (CeMOS), Mannheim University of Applied Sciences, Paul-Wittsack Str. 10, 68163 Mannheim, Germany
contact emailc.hopf@hs-mannheim.de
lab head
Katrin Erich
contact affiliationCeMOS HS Mannheim
contact emailkatrin.erich89@gmail.com
dataset submitter
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Dataset FTP location
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