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J. Biol. Chem., Vol. 266, Issue 12, 7842-7847, Apr, 1991
N Behrendt, M Ploug, L Patthy, G Houen, F Blasi and K Dano
The purified urokinase plasminogen activator receptor (u-PAR) was cleaved
into two fragments by mild chymotrypsin treatment. The smaller fragment
(apparent Mr 16,000) possessed the ligand-binding capability, as shown by
chemical cross-linking analysis. This fragment constituted the NH2-terminal
part of the intact receptor, probably including the whole sequence 1-87,
and contained N-linked carbohydrate. After detergent phase separation in
the Triton X-114 system, the fragment was present in the water phase where
its binding activity could be demonstrated in the absence of the rest of
the protein. An analysis of internal homology in the amino acid sequence of
u-PAR revealed the presence of three repeats of approximately 90 residues
each. The ligand- binding fragment corresponds to the first repeat,
supporting that this unit is a structurally autonomous domain. Domains
homologous with the internal repeats of u-PAR constitute the extracellular
part of Ly-6 antigens and of the squid glycoprotein Sgp-2. Like u-PAR,
these proteins are attached to the membrane by a glycosyl-
phosphatidylinositol anchor. The hydrophilic, ligand-binding u-PAR domain
identified in the present study has potential applications in interfering
with cell-surface plasmin-mediated proteolysis.
The ligand-binding domain of the cell surface receptor for urokinase- type plasminogen activator
Finsen Laboratory, Rigshospitalet, Copenhagen, Denmark.
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