TY - JOUR
T1 - Inhibition of fibronectin receptor function by antibodies against baby hamster kidney cell wheat germ agglutinin receptors
AU - Oppenheimer Marks, N.
AU - Grinnell, F.
PY - 1982/12/1
Y1 - 1982/12/1
N2 - Previous studies suggest that the baby hamster kidney (BHK) cell fibronectin receptor is also a wheat germ agglutinin receptor (WGA-R). To analyze this possibility further, IgG and Fab fragments of antibodies produced against a BHK cell WGA-R preparation were tested to determine their effects on cell adhesion mediated by fibronectin, wheat germ agglutinin, concanavalin A, and polycationic ferritin. The WGA-R preparation was isolated by octylglucoside extraction of BHK cells followed by chromatography of the extract on WGAagarose. The antibodies against the WGA-R preparation reacted primarily wih polypeptides of molecular weights 48, 61, 83, 105, 120, 165,210, and 230 kilodaltons (kdaltons). tt was concluded that the antibodies interfered with BHK cell fibronectin receptors on the basis of the ability of anti-WGA-R IgG or Fab fragments to (a) inhibit cell spreading on fibronectin-coated substrata; (b) cause rounding and detachment of cells previously spread on fibronectin-coated substrata; and (c) inhibit binding of fibronectin-coated latex beads to the cells. Antibody activity was blocked by treatment of anti-WGA-R with the WGA-R preparation or by absorption of anti- WGA-R with intact BHK cells. The antibodies also appeared to prevent coupling of ligandreceptor complexes (involving concanavalin A or polycationic ferritin) with the cytoskeleton. Finally, cell rounding and detachment caused by the antibodies were found to require metabolic energy since it did not occur in the presence of azide or at 4°C.
AB - Previous studies suggest that the baby hamster kidney (BHK) cell fibronectin receptor is also a wheat germ agglutinin receptor (WGA-R). To analyze this possibility further, IgG and Fab fragments of antibodies produced against a BHK cell WGA-R preparation were tested to determine their effects on cell adhesion mediated by fibronectin, wheat germ agglutinin, concanavalin A, and polycationic ferritin. The WGA-R preparation was isolated by octylglucoside extraction of BHK cells followed by chromatography of the extract on WGAagarose. The antibodies against the WGA-R preparation reacted primarily wih polypeptides of molecular weights 48, 61, 83, 105, 120, 165,210, and 230 kilodaltons (kdaltons). tt was concluded that the antibodies interfered with BHK cell fibronectin receptors on the basis of the ability of anti-WGA-R IgG or Fab fragments to (a) inhibit cell spreading on fibronectin-coated substrata; (b) cause rounding and detachment of cells previously spread on fibronectin-coated substrata; and (c) inhibit binding of fibronectin-coated latex beads to the cells. Antibody activity was blocked by treatment of anti-WGA-R with the WGA-R preparation or by absorption of anti- WGA-R with intact BHK cells. The antibodies also appeared to prevent coupling of ligandreceptor complexes (involving concanavalin A or polycationic ferritin) with the cytoskeleton. Finally, cell rounding and detachment caused by the antibodies were found to require metabolic energy since it did not occur in the presence of azide or at 4°C.
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U2 - 10.1083/jcb.95.3.876
DO - 10.1083/jcb.95.3.876
M3 - Article
C2 - 6296159
AN - SCOPUS:0020465828
SN - 0021-9525
VL - 95
SP - 876
EP - 884
JO - Journal of Cell Biology
JF - Journal of Cell Biology
IS - 3
ER -