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
APA
Vancouver
Author
Bibtex
}
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