Dataset Information

Protease Regulation by Subtrate O-Glycosylation

ABSTRACT: In this study, we systematically assessed the fine-tuning of limited proteolysis in the extracellular space by glycosylation, one of the most widely observed PTMs, using cells, and applying the Terminal Amine Labeling of Substrates (TAILS) approach, a quantitative proteomics workflow for the system-wide assessment of protein N termini and protease cleavage events in complex biological samples

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Cell Culture

DISEASE(S): Breast Cancer

SUBMITTER: Elizabeta Madzharova

LAB HEAD: Chiara Francavilla

PROVIDER: PXD050580 | Pride | 2024-08-10

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	20191209_MB_Evo_44mins_FS_Eli_NPO1.raw	Raw
	20191209_MB_Evo_44mins_FS_Eli_NPO10.raw	Raw
	20191209_MB_Evo_44mins_FS_Eli_NPO11.raw	Raw
	20191209_MB_Evo_44mins_FS_Eli_NPO12.raw	Raw
	20191209_MB_Evo_44mins_FS_Eli_NPO13.raw	Raw

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Publications

Substrate O-glycosylation actively regulates extracellular proteolysis.

Madzharova Elizabeta E Sabino Fabio F Kalogeropoulos Konstantinos K Francavilla Chiara C Auf dem Keller Ulrich U

Protein science : a publication of the Protein Society 20240801 8

Extracellular proteolysis critically regulates cellular and tissue responses and is often dysregulated in human diseases. The crosstalk between proteolytic processing and other major post-translational modifications (PTMs) is emerging as an important regulatory mechanism to modulate protease activity and maintain cellular and tissue homeostasis. Here, we focus on matrix metalloproteinase (MMP)-mediated cleavages and N-acetylgalactosamine (GalNAc)-type of O-glycosylation, two major PTMs of protei ...[more]

PMID: 39074261

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