ArticleBiochimica et biophysica acta2008
The epidermal growth factor receptor (EGFR) is proteolytically modified by the Matriptase-Prostasin serine protease cascade in cultured epithelial cells.
Article in Biochimica et biophysica acta, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 61 citations in OpenAlex.
- Circulating prostasin is an independent marker of mortality risk in patients with idiopathic pulmonary fibrosis.ERJ open research · 2025Article
- A Serine Protease Inhibitor, Camostat Mesilate, Suppresses Urinary Plasmin Activity and Alleviates Hypertension and Podocyte Injury in Dahl Salt-Sensitive Rats.International journal of molecular sciences · 2023Article
- Exosome-Mediated Activation of the Prostasin-Matriptase Serine Protease Cascade in B Lymphoma Cells.Cancers · 2023Article
- WNK1 controls endosomal trafficking through TRIM27-dependent regulation of actin assembly.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Membrane protease prostasin promotes insulin secretion by regulating the epidermal growth factor receptor pathway.Scientific reports · 2023Article
- Liver-Specific Overexpression of Prostasin Attenuates High-Fat Diet-Induced Metabolic Dysregulation in Mice.International journal of molecular sciences · 2021Article
- Prostasin regulates PD-L1 expression in human lung cancer cells.Bioscience reports · 2021Article
- The cell-surface anchored serine protease TMPRSS13 promotes breast cancer progression and resistance to chemotherapy.Oncogene · 2020Article
- Proteomic Analysis of Peri-Wounding Tissue Expressions in Extracorporeal Shock Wave Enhanced Diabetic Wound Healing in a Streptozotocin-Induced Diabetes Model.International journal of molecular sciences · 2020Article
- Entosis and apical cell extrusion constitute a tumor-suppressive mechanism downstream of Matriptase.The Journal of cell biology · 2020Article
- Targeting metastatic breast cancer with peptide epitopes derived from autocatalytic loop of Prss14/ST14 membrane serine protease and with monoclonal antibodies.Journal of experimental & clinical cancer research : CR · 2019Article
- Proteolytic Processing of SERK3/BAK1 Regulates Plant Immunity, Development, and Cell Death.Plant physiology · 2019Article
- Antibody-Linked Fluorogen-Activating Proteins for Antigen Detection and Cell Ablation.Bioconjugate chemistry · 2019Article
- Functional analysis of corin protein domains required for PCSK6-mediated activation.The international journal of biochemistry & cell biology · 2018Article
- Over forty years of bladder cancer glycobiology: Where do glycans stand facing precision oncology?Oncotarget · 2017Review
- Proteolytic cleavages in the extracellular domain of receptor tyrosine kinases by membrane-associated serine proteases.Oncotarget · 2017Article
- Molecular Pathways: Receptor Ectodomain Shedding in Treatment, Resistance, and Monitoring of Cancer.Clinical cancer research : an official journal of the American Association for Cancer Research · 2017Review
- Signaling pathways induced by serine proteases to increase intestinal epithelial barrier function.PloS one · 2017Article
- Article
- Old dog, new tricks: extracellular domain arginine methylation regulates EGFR function.The Journal of clinical investigation · 2015Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Prostasin is expressed at the apical surface of normal epithelial cells and suppresses in vitro invasion of cancer cells. Prostasin re-expression in the PC-3 prostate carcinoma cells down-regulated the epidermal growth factor receptor (EGFR) protein expression and EGF-induced phosphorylation of the extracellular signal-regulated kinases (Erk1/2). We report here that prostasin and its activating enzyme matriptase are capable of inducing proteolytic cleavages in the EGFR extracellular domain (ECD) when co-expressed in the FT-293 cells, generating two amino-terminally truncated fragments EGFR135 and EGFR110, at 135 and 110 kDa. Prostasin's role in EGFR cleavage is dependent on the serine active-site but not the GPI-anchor. The modifications of EGFR were confirmed to be on the primary structure by deglycosylation. EGFR135 and EGFR110 are not responsive to EGF stimulation, indicating loss of the ligand-binding domains. EGFR110 is constitutively phosphorylated and in its presence Erk1/2 phosphorylation is increased in the absence of EGF. The protease-induced EGFR cleavages are not dependent on EGFR phosphorylation. The EGFR ECD proteolytic modification by matriptase-prostasin is also observed in the BEAS-2B normal lung epithelial cells, the BPH-1 benign prostate hyperplasia and the MDA-MB-231 breast cancer cell lines; and represents a novel mechanism for epithelial cells to modulate EGF-EGFR signaling.
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