TY - JOUR
T1 - Characterization of the novel murine monoclonal anti-von Willebrand factor (vWf) antibody GUR76-23 which inhibits vWf interaction with α(IIb)β3 but not α(v)β3 integrin
AU - Yokoyama, Kenji
AU - Handa, Makoto
AU - Oda, Atsushi
AU - Katayama, Masahiko
AU - Fujimura, Yoshihiro
AU - Murata, Mitsuru
AU - Kawai, Yohko
AU - Watanabe, Kiyoaki
AU - Ikeda, Yasuo
PY - 1997/5/8
Y1 - 1997/5/8
N2 - von Willebrand factor (vWf) is known to interact with the two β3 integrins, α(IIb)β3 and α(v)β3, in an RGD-dependent manner. We characterized a novel murine monoclonal antibody to human vWf, GUR76-23, which recognized a site within the carboxy-terminal half of the molecule containing the RGD sequence. This antibody inhibited high shear-induced platelet aggregation and blocked adhesion of ADP plus epinephrine-stimulated platelets to vWf, indicating that it interferes with the interaction with α(IIb)β3. Unlike antibodies against the RGD site, however, the antibody was without effect on adhesion of cultured human umbilical vein endothelial cells to vWf, a phenomenon known to involve the interaction with α(v)β3. GUR76-23 binding was not displaced by anti-RGD antibodies. These results suggest that the adhesive interaction of vWf with these two β3 integrins may be differentially modulated by a site(s) other than the common RGD module.
AB - von Willebrand factor (vWf) is known to interact with the two β3 integrins, α(IIb)β3 and α(v)β3, in an RGD-dependent manner. We characterized a novel murine monoclonal antibody to human vWf, GUR76-23, which recognized a site within the carboxy-terminal half of the molecule containing the RGD sequence. This antibody inhibited high shear-induced platelet aggregation and blocked adhesion of ADP plus epinephrine-stimulated platelets to vWf, indicating that it interferes with the interaction with α(IIb)β3. Unlike antibodies against the RGD site, however, the antibody was without effect on adhesion of cultured human umbilical vein endothelial cells to vWf, a phenomenon known to involve the interaction with α(v)β3. GUR76-23 binding was not displaced by anti-RGD antibodies. These results suggest that the adhesive interaction of vWf with these two β3 integrins may be differentially modulated by a site(s) other than the common RGD module.
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U2 - 10.1006/bbrc.1997.6605
DO - 10.1006/bbrc.1997.6605
M3 - Article
C2 - 9168979
AN - SCOPUS:0030957733
SN - 0006-291X
VL - 234
SP - 147
EP - 152
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -