Dataset Information

MSI-1 knockdown in MB002 medulloblastoma cell line

ABSTRACT: MSI-1 is a RNA-binding protein that is required for normal neural stem cell and brain cancer stem cells. To understand its molecular mechanisms in medulloblastoma, we peroformed whole-cell proteomic analysis in MB002 medulloblastoma cells, after knockdown of MSI-1.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell

DISEASE(S): Brain Cancer

SUBMITTER: Yu Lu

LAB HEAD: Yu Lu

PROVIDER: PXD012432 | Pride | 2022-02-15

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	-MKameda-TMT6-60ug-180min-70flowrate-2stage-8ul_16ul-1_8kV-F.msf	Msf
	20180726-MKameda-TMT6-60ug-180min-70flowrate-2stage-15ul_16ul-1_8kV-F12.raw	Raw
	20180726-MKameda-TMT6-60ug-180min-70flowrate-2stage-8ul_16ul-1_8kV-F11.raw	Raw
	20180727-MKameda-TMT6-60ug-180min-70flowrate-2stage-8ul_16ul-1_8kV-F06.raw	Raw
	20180727-MKameda-TMT6-60ug-180min-70flowrate-2stage-8ul_16ul-1_8kV-F13-2.raw	Raw

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Publications

Identification of HnRNPC as a novel Tau exon 10 splicing factor using RNA antisense purification mass spectrometry.

Xing Sansi S Wang Jane J Wu Ruilin R Hefti Marco M MM Crary John F JF Lu Yu Y

RNA biology 20211231 1

Alternative splicing in Tau exon 10 generates 3 R- and 4 R-Tau proteoforms, which have equal abundance in healthy adult human brain. Aberrant alternative splicing in Tau exon 10 leads to distortion of the balanced 3 R- and 4 R-Tau expression levels, which is a causal factor to trigger toxic Tau aggregation, neuron dysfunction and patient death in a group of neurodegenerative diseases known as tauopathies. Hence, identification of regulators upstream of the Tau exon 10 splicing events are crucial ...[more]

PMID: 34965173

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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.