Cell-induced potentiation of the plasminogen activation system is abolished by a monoclonal antibody that recognizes the NH2-terminal domain of the urokinase receptor

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Standard

Cell-induced potentiation of the plasminogen activation system is abolished by a monoclonal antibody that recognizes the NH2-terminal domain of the urokinase receptor. / Rønne, E; Behrendt, N; Ellis, V; Ploug, M; Danø, K; Høyer-Hansen, G.

I: FEBS Letters, Bind 288, Nr. 1-2, 19.08.1991, s. 233-6.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Rønne, E, Behrendt, N, Ellis, V, Ploug, M, Danø, K & Høyer-Hansen, G 1991, 'Cell-induced potentiation of the plasminogen activation system is abolished by a monoclonal antibody that recognizes the NH2-terminal domain of the urokinase receptor', FEBS Letters, bind 288, nr. 1-2, s. 233-6.

APA

Rønne, E., Behrendt, N., Ellis, V., Ploug, M., Danø, K., & Høyer-Hansen, G. (1991). Cell-induced potentiation of the plasminogen activation system is abolished by a monoclonal antibody that recognizes the NH2-terminal domain of the urokinase receptor. FEBS Letters, 288(1-2), 233-6.

Vancouver

Rønne E, Behrendt N, Ellis V, Ploug M, Danø K, Høyer-Hansen G. Cell-induced potentiation of the plasminogen activation system is abolished by a monoclonal antibody that recognizes the NH2-terminal domain of the urokinase receptor. FEBS Letters. 1991 aug. 19;288(1-2):233-6.

Author

Rønne, E ; Behrendt, N ; Ellis, V ; Ploug, M ; Danø, K ; Høyer-Hansen, G. / Cell-induced potentiation of the plasminogen activation system is abolished by a monoclonal antibody that recognizes the NH2-terminal domain of the urokinase receptor. I: FEBS Letters. 1991 ; Bind 288, Nr. 1-2. s. 233-6.

Bibtex

@article{1bdcab2890804c949927cf97db9b85fe,
title = "Cell-induced potentiation of the plasminogen activation system is abolished by a monoclonal antibody that recognizes the NH2-terminal domain of the urokinase receptor",
abstract = "We have raised four monoclonal antibodies recognizing different epitopes within the human cell-surface receptor for urokinase-type plasminogen activator (u-PA). One of these antibodies completely abolishes the potentiation of plasmin generation observed upon incubation of the zymogens pro-u-PA and plasminogen with U937 cells. This antibody, which is also the only one to completely inhibit the binding of DFP-inactivated [125I]-u-PA to U937 cells, is directed against the u-PA binding NH2-terminal domain of u-PAR, a well-defined fragment formed by limited chymotrypsin digestion of purified u-PAR, demonstrating the functional independence of the u-PA binding domain as well as the critical role of u-PAR in the assembly of the cell-surface plasminogen activation system.",
keywords = "Antibodies, Monoclonal, Cell Line, Chymotrypsin, Epitopes, Fibrinolysin, Humans, Kinetics, Plasminogen, Plasminogen Activators, Precipitin Tests, Receptors, Cell Surface, Receptors, Urokinase Plasminogen Activator, Structure-Activity Relationship, Journal Article, Research Support, Non-U.S. Gov't",
author = "E R{\o}nne and N Behrendt and V Ellis and M Ploug and K Dan{\o} and G H{\o}yer-Hansen",
year = "1991",
month = aug,
day = "19",
language = "English",
volume = "288",
pages = "233--6",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "1-2",

}

RIS

TY - JOUR

T1 - Cell-induced potentiation of the plasminogen activation system is abolished by a monoclonal antibody that recognizes the NH2-terminal domain of the urokinase receptor

AU - Rønne, E

AU - Behrendt, N

AU - Ellis, V

AU - Ploug, M

AU - Danø, K

AU - Høyer-Hansen, G

PY - 1991/8/19

Y1 - 1991/8/19

N2 - We have raised four monoclonal antibodies recognizing different epitopes within the human cell-surface receptor for urokinase-type plasminogen activator (u-PA). One of these antibodies completely abolishes the potentiation of plasmin generation observed upon incubation of the zymogens pro-u-PA and plasminogen with U937 cells. This antibody, which is also the only one to completely inhibit the binding of DFP-inactivated [125I]-u-PA to U937 cells, is directed against the u-PA binding NH2-terminal domain of u-PAR, a well-defined fragment formed by limited chymotrypsin digestion of purified u-PAR, demonstrating the functional independence of the u-PA binding domain as well as the critical role of u-PAR in the assembly of the cell-surface plasminogen activation system.

AB - We have raised four monoclonal antibodies recognizing different epitopes within the human cell-surface receptor for urokinase-type plasminogen activator (u-PA). One of these antibodies completely abolishes the potentiation of plasmin generation observed upon incubation of the zymogens pro-u-PA and plasminogen with U937 cells. This antibody, which is also the only one to completely inhibit the binding of DFP-inactivated [125I]-u-PA to U937 cells, is directed against the u-PA binding NH2-terminal domain of u-PAR, a well-defined fragment formed by limited chymotrypsin digestion of purified u-PAR, demonstrating the functional independence of the u-PA binding domain as well as the critical role of u-PAR in the assembly of the cell-surface plasminogen activation system.

KW - Antibodies, Monoclonal

KW - Cell Line

KW - Chymotrypsin

KW - Epitopes

KW - Fibrinolysin

KW - Humans

KW - Kinetics

KW - Plasminogen

KW - Plasminogen Activators

KW - Precipitin Tests

KW - Receptors, Cell Surface

KW - Receptors, Urokinase Plasminogen Activator

KW - Structure-Activity Relationship

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

M3 - Journal article

C2 - 1715292

VL - 288

SP - 233

EP - 236

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 1-2

ER -

ID: 178215086