Modulation of O-glycans and N-glycans on murine CD8 T cells fails to alter annexin V ligand induction by galectin 1.

Abstract

Thymic negative selection and contraction of responding T cell oligoclones after infection represent important cell ablation processes required for maintaining T cell homeostasis. It has been proposed that galectin 1 contributes to these processes through interaction with lactosyl sequences principally on cell surface glycoproteins bearing core 2 (C2GnT1)-branched O-glycans. According to this model, specific T cell surface proteins cross-linked by galectin 1 induce signaling, ligand redistribution, and apoptosis in both immature thymocytes and activated T cells. The influence of lactosyl residues contained in branched O-glycans or complex N-glycans on galectin 1 binding and induction of annexin V ligand in murine CD8 T cells was assessed. Neither galectin binding nor galectin-induced expression of annexin V ligand was perturbed under conditions in which: 1) C2GnT1 activity was differentially induced by CD8 T cell activation/culture with IL-2 vs IL-4; 2) activated CD8(+) T cells lacked C2GnT1 expression; or 3) complex N-glycan formation was blocked by swainsonine. The maintenance of galectin 1 binding and induced annexin V expression under conditions that alter lactosamine abundance on O- or complex N-glycans suggest that galectin 1-mediated apoptosis is neither a simple function of fluctuating C2GnT1 activity nor a general C2GnT1-dependent mechanism underlying contraction of CD8 T cells subsequent to activation.