{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Calligaris M"],"funding":["Deutsche Forschungsgemeinschaft (DFG, German Research Foundation)","CLINSPECT-M","Munich Cluster for Systems Neurology","National Recovery and Resilience Plan M4C2, part of the NextGenerationEU Programme, granted by the European Union for the Research Programme \"National Biodiversity Future Center - NBFC\"","NIGMS NIH HHS"],"pagination":["e202400076"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11648071"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["24(23-24)"],"pubmed_abstract":["Ectodomain shedding, which is the proteolytic release of transmembrane proteins from the cell surface, is crucial for cell-to-cell communication and other biological processes. The metalloproteinase ADAM17 mediates ectodomain shedding of over 50 transmembrane proteins ranging from cytokines and growth factors, such as TNF and EGFR ligands, to signalling receptors and adhesion molecules. Yet, the ADAM17 sheddome is only partly defined and biological functions of the protease have not been fully characterized. Some ADAM17 substrates (e.g., HB-EGF) are known to bind to heparan sulphate proteoglycans (HSPG), and we hypothesised that such substrates would be under-represented in traditional secretome analyses, due to their binding to cell surface or pericellular HSPGs. Thus, to identify novel H"],"journal":["Proteomics"],"pubmed_title":["Development of a Proteomic Workflow for the Identification of Heparan Sulphate Proteoglycan-Binding Substrates of ADAM17."],"pmcid":["PMC11648071"],"funding_grant_id":["R35 GM134907","EXC 2145 SyNergy- ID 390857198","(FKZ161L0214C)","CN_00000033(CN5-Spoke6)-CUPB73C21001300006"],"pubmed_authors":["Lichtenthaler SF","Troeberg L","Lo Pinto M","Zito G","Puccio MC","Spano DP","Muller SA","Scilabra SD","Bonelli S","Blobel CP","Calligaris M"],"additional_accession":[]},"is_claimable":false,"name":"Development of a Proteomic Workflow for the Identification of Heparan Sulphate Proteoglycan-Binding Substrates of ADAM17.","description":"Ectodomain shedding, which is the proteolytic release of transmembrane proteins from the cell surface, is crucial for cell-to-cell communication and other biological processes. The metalloproteinase ADAM17 mediates ectodomain shedding of over 50 transmembrane proteins ranging from cytokines and growth factors, such as TNF and EGFR ligands, to signalling receptors and adhesion molecules. Yet, the ADAM17 sheddome is only partly defined and biological functions of the protease have not been fully characterized. Some ADAM17 substrates (e.g., HB-EGF) are known to bind to heparan sulphate proteoglycans (HSPG), and we hypothesised that such substrates would be under-represented in traditional secretome analyses, due to their binding to cell surface or pericellular HSPGs. Thus, to identify novel H","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Dec","modification":"2026-06-02T11:20:45.441Z","creation":"2025-04-04T01:55:02.453Z"},"accession":"S-EPMC11648071","cross_references":{"pubmed":["39318062"],"doi":["10.1002/pmic.202400076"]}}