Dataset Information

Col4a1 mouse glomerular datasets

ABSTRACT: Glomeruli were isolated from Col4a1+/SVC and Ctrl mice. Samples were enriched for extracellular matrix. Glomerular extracellular matrix and cellular fractions were analysed by mass spectrometry.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Kidney

SUBMITTER: Franziska Lausecker

LAB HEAD: Rachel Lennon

PROVIDER: PXD022363 | Pride | 2022-08-12

REPOSITORIES: Pride

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Publications

Identification of an Altered Matrix Signature in Kidney Aging and Disease.

Randles Michael J MJ Lausecker Franziska F Kong Qingyang Q Suleiman Hani H Reid Graeme G Kolatsi-Joannou Maria M Davenport Bernard B Tian Pinyuan P Falcone Sara S Falcone Sara S Potter Paul P Van Agtmael Tom T Norman Jill T JT Long David A DA Humphries Martin J MJ Miner Jeffrey H JH Lennon Rachel R

Journal of the American Society of Nephrology : JASN 20210528 7

<h4>Background</h4>Accumulation of extracellular matrix in organs and tissues is a feature of both aging and disease. In the kidney, glomerulosclerosis and tubulointerstitial fibrosis accompany the decline in function, which current therapies cannot address, leading to organ failure. Although histologic and ultrastructural patterns of excess matrix form the basis of human disease classifications, a comprehensive molecular resolution of abnormal matrix is lacking.<h4>Methods</h4>Using mass spectr ...[more]

PMID: 34049963

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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.

Dataset Information

Col4a1 mouse glomerular datasets

Publications

Identification of an Altered Matrix Signature in Kidney Aging and Disease.

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