Journal article

Glycosylation changes in hFUT1 transgenic mice increase TCR signaling and apoptosis resulting in thymocyte maturation arrest

Gregory TC Moore, Steven J Brown, Adam C Winterhalter, Mark Lust, Evelyn J Salvaris, Carly Selan, Harshal H Nandurkar, Paul V Desmond, Peter J Cowan, Anthony JF d'Apice

MOLECULAR IMMUNOLOGY | PERGAMON-ELSEVIER SCIENCE LTD | Published : 2008

Abstract

Glycosylation of cell surface proteins is important in thymocyte maturation. In particular, the level of sialylation of key glycoproteins such as CD45 is believed to play a major role in regulating TCR signaling, adhesion and apoptosis of developing thymocytes. We show here that transgenic expression of human alpha1-2 fucosyltransferase (hFUT1) in mice resulted in a marked shift from sialylation to fucosylation of thymocyte glycoproteins. This was associated with a significant reduction in thymocyte number, an increased rate of apoptosis in double positive and single positive thymocytes, and a maturation arrest at TCR-dependent developmental transitions reminiscent of CD45 deficiency. Indeed..

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