Immunology

E.L. Berg, M.R. Robinson, O. Mannsson, E.C. Butcher, J.L. Magnani, "A carbohydrate domain common to both Sialyl Lea and Sialyl Lex is recognized by the endothelial cell leukocyte adhesion molecule ELAM-1," Journal of Biological Chemistry, 266:14869, 1991. John Magnani (Glyco Tech Corp., Rockville, Md.): "A greater understanding of the physiological functions of carbohydrate structures is currently being pursued by an exciting new field of research termed `glycobiology.' My coauthors Eugene But

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John Magnani (Glyco Tech Corp., Rockville, Md.): "A greater understanding of the physiological functions of carbohydrate structures is currently being pursued by an exciting new field of research termed `glycobiology.' My coauthors Eugene Butcher and Ellen Berg at Stanford University have pioneered the study of lymphocyte recirculation. The first step in the extravasation of these cells from the bloodstream is their binding to the vascular endothelium of the blood vessel wall. Binding proteins classified as `selectins' recognize unique cell surface carbohydrate structures, thereby selecting specific cells from the blood for extravasation. Transfected mouse L cells expressing human E- selectin on the cell surface were used in cell binding studies with purified complex carbohydrates chemically linked to nonglycosylated proteins.

"This paper first showed that human E-selectin bound not only to the known carbohydrate ligand sialyl Lex but also to its structural isomer, sialyl Lea. To determine the common three- dimensional domain ...

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