Removal of domain D2 or D3 of the human urokinase receptor does not affect ligand affinity

Leena Riittinen; Paola Limongi; Massimo P. Crippa; Massimo Conese; Luciano Hernandez-Marrero; Francesca Fazioli; Francesco Blasi

doi:10.1016/0014-5793(96)00033-6

Removal of domain D2 or D3 of the human urokinase receptor does not affect ligand affinity

Leena Riittinen, Paola Limongi, Massimo P. Crippa, Massimo Conese, Luciano Hernandez-Marrero, Francesca Fazioli, Francesco Blasi

IRCCS Ospedale San Raffaele

Research output: Contribution to journal › Article › peer-review

Abstract

The main ligand-binding determinant of the human urokinase receptor (uPAR) is located in the amino terminal domain D1, but when isolated this domain presents a 1500 fold lower affinity than the intact three-domain uPAR (D1D2D3). uPAR mutants missing either domain 2 (D1HD3) or domain 3 (D1D2) were expressed in murine LB6 cells and showed to be properly GPI-anchored to the cell surface. Binding assays with [ ¹²⁵I]ATF demonstrated that these mutants possessed a normal (D1D2) or slightly reduced (D1HD3) affinity, indicating that a high ligand-affinity may be achieved by a combination of D1 with domain D2 or D3.

Original language	English
Pages (from-to)	1-6
Number of pages	6
Journal	FEBS Letters
Volume	381
Issue number	1-2
DOIs	https://doi.org/10.1016/0014-5793(96)00033-6
Publication status	Published - Feb 26 1996

Keywords

GPI-anchored protein
uPA
Urokinase receptor

ASJC Scopus subject areas

Biochemistry
Biophysics
Molecular Biology

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10.1016/0014-5793(96)00033-6

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title = "Removal of domain D2 or D3 of the human urokinase receptor does not affect ligand affinity",

abstract = "The main ligand-binding determinant of the human urokinase receptor (uPAR) is located in the amino terminal domain D1, but when isolated this domain presents a 1500 fold lower affinity than the intact three-domain uPAR (D1D2D3). uPAR mutants missing either domain 2 (D1HD3) or domain 3 (D1D2) were expressed in murine LB6 cells and showed to be properly GPI-anchored to the cell surface. Binding assays with [ 125I]ATF demonstrated that these mutants possessed a normal (D1D2) or slightly reduced (D1HD3) affinity, indicating that a high ligand-affinity may be achieved by a combination of D1 with domain D2 or D3.",

keywords = "GPI-anchored protein, uPA, Urokinase receptor",

author = "Leena Riittinen and Paola Limongi and Crippa, {Massimo P.} and Massimo Conese and Luciano Hernandez-Marrero and Francesca Fazioli and Francesco Blasi",

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AU - Riittinen, Leena

AU - Limongi, Paola

AU - Crippa, Massimo P.

AU - Conese, Massimo

AU - Hernandez-Marrero, Luciano

AU - Fazioli, Francesca

AU - Blasi, Francesco

PY - 1996/2/26

Y1 - 1996/2/26

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