{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Madzharova E"],"funding":["Professor Ulrich auf dem Keller's Novo Nordisk Foundation Young Investigator Award","PRO-MS: Danish National Mass Spectrometry Platform for Functional Proteomics","Danish Cancer Society Foundation"],"pagination":["e5128"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11285871"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["33(8)"],"pubmed_abstract":["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 proteins in the extracellular space. We investigated the influence of truncated O-glycan trees, also referred to as Tn antigen, following the inactivation of C1GALT1-specific chaperone 1 (COSMC) on the general and MMP9-specific proteolytic processing in MDA-MB-231 breast cancer cells. Quantitative assessm"],"journal":["Protein science : a publication of the Protein Society"],"pubmed_title":["Substrate O-glycosylation actively regulates extracellular proteolysis."],"pmcid":["PMC11285871"],"funding_grant_id":["R302-A17618","5072-00007B","NNF16OC0020670"],"pubmed_authors":["Kalogeropoulos K","Auf dem Keller U","Madzharova E","Francavilla C","Sabino F"],"additional_accession":[]},"is_claimable":false,"name":"Substrate O-glycosylation actively regulates extracellular proteolysis.","description":"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 proteins in the extracellular space. We investigated the influence of truncated O-glycan trees, also referred to as Tn antigen, following the inactivation of C1GALT1-specific chaperone 1 (COSMC) on the general and MMP9-specific proteolytic processing in MDA-MB-231 breast cancer cells. Quantitative assessm","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Aug","modification":"2026-06-03T00:19:01.091Z","creation":"2026-04-22T03:11:30.501Z"},"accession":"S-EPMC11285871","cross_references":{"pubmed":["39074261"],"doi":["10.1002/pro.5128"]}}