en.wikipedia.org/wiki/Urokinase_receptor
1 correction found
When urokinase is bound to the receptor, there is cleavage between the GPI-anchor and the uPAR, releasing a soluble form of the protein known as suPAR.
This sentence mixes up two different cleavage events. Full-length suPAR is mainly generated by cleavage at the GPI anchor by phospholipases/GDE3, whereas urokinase primarily cleaves uPAR in the D1-D2 linker region, not at the GPI anchor.
Full reasoning
Recent reviews distinguish GPI-anchor shedding from urokinase-mediated proteolysis of uPAR.
- A 2026 Journal of Clinical Investigation review states that full-length suPAR is generated by GPI-anchor cleavage and identifies the responsible enzymes as phospholipase C, phospholipase D, or GDE3.
- The same review says urokinase (uPA) instead predominantly cleaves the linker region between domains D1 and D2, releasing D1.
- A 2021 Frontiers in Immunology review likewise separates the sites: it lists uPA among proteases that cleave the linker region, while cleavage in the GPI anchor is attributed to phospholipase C and D (plus cathepsin G and plasmin).
So the article's wording is inaccurate because it specifically says that when urokinase is bound, the cleavage occurs between the GPI-anchor and uPAR to release suPAR. The literature instead describes GPI-anchor cleavage as a different process from the main urokinase-mediated cleavage event.
2 sources
- The role of suPAR and related proteins in kidney, heart diseases, and diabetes
Proteolysis at the GPI anchor by phospholipase C (PLC), phospholipase D (PLD), or glycophosphodiesterase 3 (GDE3) generates circulating soluble uPAR (suPAR)... Urokinase plasminogen activator (uPA), plasmin, and several matrix metalloproteinases (MMPs) predominantly cleave within the linker region between D1 and D2, releasing D1.
- Soluble Urokinase Plasminogen Activator Receptor (suPAR) as a Biomarker of Systemic Chronic Inflammation
uPAR has cleavage sites for several proteases in the linker region ... (uPA) and the GPI anchor (phospholipase C and D, cathepsin G, plasmin), which upon cleavage can result in three suPAR isoforms.