Proteomics

Dataset Information

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Proteomic profiling in mouse kidneys post-UUO


ABSTRACT: Increased export of transglutaminase-2 (TG2) by tubular epithelial cells (TECs) into the surrounding interstitium modifies the extracellular homeostatic balance leading to fibrotic membrane expansion. Although silencing of extracellular TG2 ameliorates progressive kidney scarring in animal models of chronic kidney disease, the pathway through which TG2 is secreted from TECs and contributes to disease progression has not been elucidated. In this study, we developed a global proteomic approach to identify binding partners of TG2 responsible for TG2 externalization in kidneys subjected to unilateral ureteric obstruction, using TG2-knockout kidneys as negative controls. We report a robust and unbiased analysis of the membrane interactome of TG2 in fibrotic kidneys relative to the entire proteome post-UUO detected by SWATH-mass spectrometry.

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Kidney Cell, Kidney

DISEASE(S): Chronic Kidney Disease

SUBMITTER: David Boocock  

LAB HEAD: David Boocock

PROVIDER: PXD008173 | Pride | 2018-02-07

REPOSITORIES: Pride

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Publications

Proteomic Profiling Reveals the Transglutaminase-2 Externalization Pathway in Kidneys after Unilateral Ureteric Obstruction.

Furini Giulia G   Schroeder Nina N   Huang Linghong L   Boocock David D   Scarpellini Alessandra A   Coveney Clare C   Tonoli Elisa E   Ramaswamy Raghavendran R   Ball Graham G   Verderio Claudia C   Johnson Timothy S TS   Verderio Elisabetta A M EAM  

Journal of the American Society of Nephrology : JASN 20180130 3


Increased export of transglutaminase-2 (TG2) by tubular epithelial cells (TECs) into the surrounding interstitium modifies the extracellular homeostatic balance, leading to fibrotic membrane expansion. Although silencing of extracellular TG2 ameliorates progressive kidney scarring in animal models of CKD, the pathway through which TG2 is secreted from TECs and contributes to disease progression has not been elucidated. In this study, we developed a global proteomic approach to identify binding p  ...[more]

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