Adhesion of human cancer cells to vascular endothelium mediated by a carbohydrate antigen, sialyl Lewis A
A Takada, K Ohmori, N Takahashi, K Tsuyuoka… - Biochemical and …, 1991 - Elsevier
A Takada, K Ohmori, N Takahashi, K Tsuyuoka, A Yago, K Zenita, A Hasegawa, R Kannagi
Biochemical and biophysical research communications, 1991•ElsevierRecently the lectin-like domain on ELAM-1 (endothelial leukocyte adhesion molecule-1)
was shown to recognize a carbohydrate antigen, sialyl Lewis x. In this paper we
demonstrate, by a series of inhibition experiments utilizing specific monoclonal antibodies
and pure glycolipid preparations, that the sialyl Lewis a antigen serves as a specific ligand
for ELAM-1 as well as sialyl Lewis x and plays a significant role in the ELAM-1-mediated
binding of human cancer cells to activated andothelial cells.
was shown to recognize a carbohydrate antigen, sialyl Lewis x. In this paper we
demonstrate, by a series of inhibition experiments utilizing specific monoclonal antibodies
and pure glycolipid preparations, that the sialyl Lewis a antigen serves as a specific ligand
for ELAM-1 as well as sialyl Lewis x and plays a significant role in the ELAM-1-mediated
binding of human cancer cells to activated andothelial cells.
Abstract
Recently the lectin-like domain on ELAM-1 (endothelial leukocyte adhesion molecule-1) was shown to recognize a carbohydrate antigen, sialyl Lewis x. In this paper we demonstrate, by a series of inhibition experiments utilizing specific monoclonal antibodies and pure glycolipid preparations, that the sialyl Lewis a antigen serves as a specific ligand for ELAM-1 as well as sialyl Lewis x and plays a significant role in the ELAM-1-mediated binding of human cancer cells to activated andothelial cells.
Elsevier