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1
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Galectins and their ligands: Amplifiers, silencers or tuners of the inflammatory response?
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Rabinovich G.A., Baum L.G., Tinari N., Paganelli R., Natoli C., Liu F.-T., Iacobelli S. Galectins and their ligands: amplifiers, silencers or tuners of the inflammatory response? Trends Immunol. 23:2002;313-320.
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This inaugural article summarizes current evidence that many different glycoproteins and glycolipids participate in organizing the plasma membrane into functionally distinct microdomains that regulate functions such as adhesion and cell-cell signaling.
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-/-) show increased hypersensitivity to T cells and enhanced development of autoimmunity. Loss of the poly-N-acetyllactosamine oligosaccharide branches created by GnT V results in reduced galectin-3 binding, which shows that glycoprotein-galectin lattices on the cell surface modulate TCR signaling.
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-/-) show increased hypersensitivity to T cells and enhanced development of autoimmunity. Loss of the poly-N-acetyllactosamine oligosaccharide branches created by GnT V results in reduced galectin-3 binding, which shows that glycoprotein-galectin lattices on the cell surface modulate TCR signaling.
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Demetriou, M.1
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Jin L., McLean P.A., Neel B.G., Wortis H.H. Sialic acid binding domains of CD22 are required for negative regulation of B cell receptor signaling. J Exp Med. 195:2002;1199-1205. These two papers [8•,9•] show that ligand engagement by a transmembrane B cell lectin results in altered B cell signaling in response to immunoglobulin engagement. This work directly links saccharide recognition by the extracellular lectin domain to signaling by the intracellular domain.
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Nguyen J.T., Evans D.P., Galvan M., Pace K.E., Leitenberg D., Bui T.N., Baum L.G. CD45 modulates galectin-1 induced cell death: regulation by expression of core 2 O-glycans. J Immunol. 167:2001;5697-5707.
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An excellent synthesis of the various ways in which glycosylation, both within a cell and on its surface, controls protein folding and transport, antigen recognition and presentation, and the interaction of antigen receptors in the 'immune synapse', stressing the effects that glycosylation can have on immune signaling. This review and the one by Bertozzi and Kiessling [14] are part of a special feature on carbohydrates and glycobiology in Science.
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Rudd P.M., Elliot T., Cresswell P., Wilson I.A., Dwek R.A. Glycosylation and the immune system. Science. 291:2001;2370-2375. An excellent synthesis of the various ways in which glycosylation, both within a cell and on its surface, controls protein folding and transport, antigen recognition and presentation, and the interaction of antigen receptors in the 'immune synapse', stressing the effects that glycosylation can have on immune signaling. This review and the one by Bertozzi and Kiessling [14] are part of a special feature on carbohydrates and glycobiology in Science.
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