Development of a Proteomic Workflow for the Identification of Heparan Sulphate Proteoglycan-Binding Substrates of ADAM17.
ADAM17
ectodomain shedding
heparan sulphate proteoglycans
metalloproteinases
proteomics
secretome analysis
Journal
Proteomics
ISSN: 1615-9861
Titre abrégé: Proteomics
Pays: Germany
ID NLM: 101092707
Informations de publication
Date de publication:
24 Sep 2024
24 Sep 2024
Historique:
revised:
29
08
2024
received:
07
03
2024
accepted:
29
08
2024
medline:
25
9
2024
pubmed:
25
9
2024
entrez:
25
9
2024
Statut:
aheadofprint
Résumé
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 HSPG-binding ADAM17 substrates, we developed a proteomic workflow that involves addition of heparin to solubilize HSPG-binding proteins from the cell layer, thereby allowing their mass spectrometry detection by heparin-treated secretome (HEP-SEC) analysis. Applying this methodology to murine embryonic fibroblasts stimulated with an ADAM17 activator enabled us to identify 47 transmembrane proteins that were shed in response to ADAM17 activation. This included known HSPG-binding ADAM17 substrates (i.e., HB-EGF, CX3CL1) and 14 novel HSPG-binding putative ADAM17 substrates. Two of these, MHC-I and IL1RL1, were validated as ADAM17 substrates by immunoblotting.
Identifiants
pubmed: 39318062
doi: 10.1002/pmic.202400076
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e202400076Subventions
Organisme : 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"
ID : CN_00000033(CN5-Spoke6)-CUPB73C21001300006
Organisme : Deutsche Forschungsgemeinschaft (DFG, German Research Foundation)
Organisme : Munich Cluster for Systems Neurology
ID : EXC 2145 SyNergy- ID 390857198
Organisme : CLINSPECT-M
ID : (FKZ161L0214C)
Informations de copyright
© 2024 The Author(s). PROTEOMICS published by Wiley‐VCH GmbH.
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