| 摘要 |
<p>Peptides derived from three regions of the lectin binding region of GMP-140 have been found to selectively interact with "selectins", including GMP-140, ELAM-1, and lymphocyte homing receptor. The three regions include amino acids 19-34, 54-72, and 66-89, based on the numbers of the residues contained in the peptide, with residue 1 defined as the N terminus of the mature protein after cleavage of the signal peptide. Fucosylated sialyated lactosamine structures that bind to GMP-140 have also been discovered. The structure is created by expression of alpha (1,3) fucosyltransferases capable of modifying acceptors containing alpha (2,3) sialic acid-substituted lactosaminoglycans. Le<x>, Gal beta 1,4(Fuc alpha 1,3)GlcNAc beta 1-R (where R is a protein or other carbohydrate structure) forms the core of this sialyated structure. The peptides and carbohydrate structures are useful as diagnostics and for clinical applications in the modulation or inhibition of coagulation processes or inflammatory processes.</p> |
