Metabolic changes of E-selectin caused by the binding of a mucin carrying sialylLewis A antigens

H Nakada, M Inoue, I Yamashina - Biochemical and biophysical research …, 1997 - Elsevier
H Nakada, M Inoue, I Yamashina
Biochemical and biophysical research communications, 1997Elsevier
Mucin-type glycoproteins carrying sialylLeA antigens (SL-GP) were isolated from the ascites
fluid of a patient with colorectal cancer. SL-GP bound to E-selectin on endothelial cells in
Ca2+-and sialylLeA antigen-dependent manners. To examine the metabolic change in E-
selectin caused by ligation, endothelial cells were labeled with32P-phosphate or35S-Met
and35S-Cys. Phosphorylation at one or more serine residues of E-selectin was elevated by
ligation with SL-GP but not with sialylLeA hexasaccharide. Pulse-labeling of E-selectin …
Mucin-type glycoproteins carrying sialylLeA antigens (SL-GP) were isolated from the ascites fluid of a patient with colorectal cancer. SL-GP bound to E-selectin on endothelial cells in Ca2+- and sialylLeA antigen-dependent manners. To examine the metabolic change in E-selectin caused by ligation, endothelial cells were labeled with32P-phosphate or35S-Met and35S-Cys. Phosphorylation at one or more serine residues of E-selectin was elevated by ligation with SL-GP but not with sialylLeA hexasaccharide. Pulse-labeling of E-selectin with35S-Met and35S-Cys in the presence of SL-GP indicated that the degradation of E-selectin was accelerated by SL-GP ligation, but labeling after pre-ligation with SL-GP revealed an increase in the synthesis of E-selectin. The synthesis may reflect compensation for the E-selectin degraded on pre-ligation. These results indicate that the overall metabolism of E-selectin was enhanced by the ligation of SL-GP, with degradation and synthesis being apparently balanced.
Elsevier
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