7^th World Congress on
Immunology

Biography:

Abstract:

The aberrant glycosylation on proteins and lipids has been implicated in malignant transformations through promoting the tumorigenesis, metastasis, and the evasion from the host immunity.  The I-branching β-1,6-N-acetylglucosaminyltransferase, responsible for the straight i conversion to branched I histo-blood group antigens, has been reported for its important effects on the migration, invasion, and metastasis of solid tumors.  First, we demonstrated that SHP-2-ERK2 signaling regulates the phosphorylation status of C/EBPa toby altering its binding affinity onto the IGnTC promoter region, thereby activating the synthesis of cell-surface I antigen formation during erythropoiesis.  Second, we addressed how the branched I antigens on the leukemia impacted the host immuno-surveillance mediated by natural killer (NK) cells.  The levels of I antigen presented on leukemia cells showed a positive correlation with the susceptibility to NK-mediated lysis.  Third, by the conjugation assay, elevating the expression of the I antigens on the leukemia cells that can only display low level of cell surface I antigens greatly increased the sensitivity to NK cytotoxicity.  Our findings suggested that branched I of the leukemia cells not only is important for NK targeting but also could serve as a potentially evaluation maker for NK-cell based leukemia treatment.