Glycosylation in the control of selectin counter-receptor structure and function

摘要: Leukocyte trafficking is characterized by sequential cell adhesion and activation events that deliver specific leukocyte subsets to distinct extravascular locations under different pathophysiological circumstances. E-, P- and/or L-selectin-dependent leukocyte-endothelial adhesive interactions contribute essentially this process. Selectin counter-receptor activity on high endothelial venules borne glycoproteins whose ability support requires post-translational modifications. These modifications are typified serine/threonine-linked oligosaccharides capped with the sialyl Lewis x moiety, an alpha2-3sialylated, alpha1-3ucosylated tetrasaccharide synthesized glycosyltransferases. Recent advances in glycan structure analysis characterizing mice targeted deletions of glycosyltransferase sulfotransferase genes discloses essential role for 6-O GlcNAc sulfate modification L-selectin activity. Related studies identify novel extended Core 1 type O-glycans bearing 6-sulfosialyl define molecular nature MECA-79 epitope, disclose a requirement alpha1-3fucosyltransferases FucT-IV FucT-VII elaboration activities. Parallel also demonstrate these 2 fucosyltransferases, core transferase, 2-type determinants make contributions P-selectin activity, figure prominently control E-selectin