Glycobiology Advance Access originally published online on August 17, 2006
Glycobiology 2006 16(12):1262-1271; doi:10.1093/glycob/cwl037
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Effects of N-glycan processing inhibitors on signaling events and induction of apoptosis in galectin-1-stimulated Jurkat T lymphocytes
2 Institute of Medical Biochemistry and Molecular Biology, University of Rostock, Schillingallee 70, D-18057 Rostock, Germany;
3 Faculty of Science, Department of Chemistry, Cairo University, Gisa 12613, Cairo, Egypt; and
4 Faculty of Specific Education, Mansoura University, Mansoura, 35516, New Damietta City, Egypt
1 To whom correspondence should be addressed; e-mail: hermann.walzel{at}med.uni-rostock.de
Received on June 2, 2006; revised on July 12, 2006; accepted on August 4, 2006
To elucidate the role of N-linked glycans in triggering T-cell functions, the effects of the N-glycan processing inhibitors 1-deoxymannojirimycin (1-DMM) and swainsonine (SW) were investigated on signaling events and induction of apoptosis in galectin-1 (gal-1)-stimulated Jurkat T lymphocytes. The treatment of Jurkat E6.1 cells with 1-DMM and SW strongly reduced the cell binding of gal-1–biotin, conjugate binding to cell lysate glycoproteins, and to cluster of differentiation (CD) 3 immunoprecipitates on blots as well as the binding of CD2 and CD3 to immobilized gal-1. The mannosidase inhibitors efficiently decreased gal-1-induced calcium mobilization. Both phases originated from a transient Ca2+ release of internal stores, and the sustained influx across the plasma membrane was found to be involved. Both inhibitors suppressed in transiently transfected Jurkat T lymphocytes the gal-1-induced expression of the luciferase (luc) reporter gene constructs pNFAT-TA-Luc and pAP1(phorbol-12-myristate-13-acetate [PMA])-TA-Luc. The data provide evidence that gal-1 triggers through binding to N-linked glycans a Ca2+-sensitive apoptotic pathway.
Key words: apoptosis / galectin-1 / Jurkat T lymphocytes / N-glycan processing / signaling
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