[HTML][HTML] The cleavage of the urokinase receptor regulates its multiple functions
The urokinase-type plasminogen activator (uPA) is able to cleave its cell surface receptor
(uPAR) anchored to the cell membrane through a glycophosphatidylinositol tail. The
cleavage leads to the formation of cell surface truncated forms, devoid of the N-terminal
domain 1 (D1) and unmasks or disrupts, depending on the cleavage site, a sequence in the
D1-D2 linker region (residues 88–92), which in the soluble form is a potent chemoattractant
for monocyte-like cells. To investigate the possible role (s) of the cleaved forms of cell …
(uPAR) anchored to the cell membrane through a glycophosphatidylinositol tail. The
cleavage leads to the formation of cell surface truncated forms, devoid of the N-terminal
domain 1 (D1) and unmasks or disrupts, depending on the cleavage site, a sequence in the
D1-D2 linker region (residues 88–92), which in the soluble form is a potent chemoattractant
for monocyte-like cells. To investigate the possible role (s) of the cleaved forms of cell …