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J. Biol. Chem., Vol. 262, Issue 10, 4437-4440, Apr, 1987
E Appella, EA Robinson, SJ Ullrich, MP Stoppelli, A Corti, G Cassani and F Blasi
Previous studies have shown that the region of human urokinase-type
plasminogen activator (uPA) responsible for receptor binding resides in the
amino-terminal fragment (ATF, residues 1-135) (Stoppelli, M.P., Corti, A.,
Soffientini, A., Cassani, G., Blasi, F., and Assoian, R.K. (1985) Proc.
Natl. Acad. Sci. U.S. A. 82, 4939-4943). The area within ATF responsible
for specific receptor binding has now been identified by the ability of
different synthetic peptides corresponding to different regions of the
amino terminus of uPA to inhibit receptor binding of 125I-labeled ATF. A
peptide corresponding to human [Ala19]uPA-(12-32) resulted in 50%
inhibition of ATF binding at 100 nM. Peptides uPA-(18-32) and
[Ala13]uPA-(9-20) inhibit at 100 and 2000 microM, respectively. The human
peptide uPA-(1-14) and the mouse peptide [Ala20]uPA-(13-33) have no effect
on ATF receptor binding. This region of uPA is referred to as the growth
factor module since it shares partial amino acid sequence homology
(residues 14-33) to epidermal growth factor (EGF). Furthermore, this region
of EGF is responsible for binding of EGF to its receptor (Komoriya, A.
Hortsch, M., Meyers, C., Smith, M., Kanety, H., and Schlessinger, J. (1984)
Proc. Natl. Acad. Sci. U.S.A. 81, 1351-1355). However, EGF does not inhibit
ATF receptor binding. Comparison of the sequences responsible for receptor
binding of uPA and EGF indicate that the region of highest homology is
between residues 13-19 and 14-20 of human uPA and EGF, respectively. In
addition, there is a conservation of the spacings of four cysteines in this
module whereas there is no homology between residues 20-30 and 21-33 of uPA
and EGF. Thus, residues 20-30 of uPA apparently confer receptor binding
specificity, and residues 13-19 provide the proper conformation to the
adjacent binding region.
The receptor-binding sequence of urokinase. A biological function for the growth-factor module of proteases
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C. Rogers, F. G.P. Welt, M. J. Karnovsky, and E. R. Edelman Monocyte Recruitment and Neointimal Hyperplasia in Rabbits: Coupled Inhibitory Effects of Heparin Arterioscler. Thromb. Vasc. Biol., October 1, 1996; 16(10): 1312 - 1318. [Abstract] [Full Text]
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N. Behrendt, E. Ronne, and K. Dano Domain Interplay in the Urokinase Receptor. REQUIREMENT FOR THE THIRD DOMAIN IN HIGH AFFINITY LIGAND BINDING AND DEMONSTRATION OF LIGAND CONTACT SITES IN DISTINCT RECEPTOR DOMAINS J. Biol. Chem., September 13, 1996; 271(37): 22885 - 22894. [Abstract] [Full Text] [PDF]
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T. H. Bugge, T. T. Suh, M. J. Flick, C. C. Daugherty, J. R, H. Solberg, V. Ellis, K. Danø, and J. L. Degen The Receptor for Urokinase-type Plasminogen Activator Is Not Essential for Mouse Development or Fertility J. Biol. Chem., July 14, 1995; 270(28): 16886 - 16894. [Abstract] [Full Text] [PDF]
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C.-I W. Q. Y. and Charles S. Craik and C. I. Wang Isolation of a High Affinity Inhibitor of Urokinase-type Plasminogen Activator by Phage Display of Ecotin J. Biol. Chem., May 19, 1995; 270(20): 12250 - 12256. [Abstract] [Full Text] [PDF]
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S. J. Mandriota, G. Seghezzi, J.-D. Vassalli, N. Ferrara, S. Wasi, R. Mazzieri, P. Mignatti, and M. S. Pepper Vascular Endothelial Growth Factor Increases Urokinase Receptor Expression in Vascular Endothelial Cells J. Biol. Chem., April 28, 1995; 270(17): 9709 - 9716. [Abstract] [Full Text] [PDF]
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V. Novokhatny, L. Medved, H. R. Lijnen, and K. Ingham Tissue-type Plasminogen Activator (tPA) Interacts with Urokinase-type Plasminogen Activator (uPA) via tPA's Lysine Binding Site J. Biol. Chem., April 14, 1995; 270(15): 8680 - 8685. [Abstract] [Full Text] [PDF]
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L. Naldini, E. Vigna, A. Bardelli, A. Follenzi, F. Galimi, and P. M. Comoglio Biological Activation of pro-HGF (Hepatocyte Growth Factor) by Urokinase Is Controlled by a Stoichiometric Reaction J. Biol. Chem., January 13, 1995; 270(2): 603 - 611. [Abstract] [Full Text] [PDF]
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F. Del Amo, D. Smith, P. Swiatek, M Gendron-Maguire, R. Greenspan, A. McMahon, and T Gridley Expression pattern of Motch, a mouse homolog of Drosophila Notch, suggests an important role in early postimplantation mouse development Development, January 7, 1992; 115(3): 737 - 744. [Abstract] [PDF]
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O. D. Liang, T. Chavakis, S. M. Kanse, and K. T. Preissner Ligand Binding Regions in the Receptor for Urokinase-type Plasminogen Activator. STRUCTURAL REQUIREMENTS FOR A MULTIDOMAIN BINDING REGION AND RECEPTOR-RECEPTOR INTERACTION J. Biol. Chem., July 27, 2001; 276(31): 28946 - 28953. [Abstract] [Full Text] [PDF]
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