TAILIEUCHUNG - Báo cáo khoa học: Membrane trafficking of CD98 and its ligand galectin 3 in BeWo cells ) implication for placental cell fusion

CD98 heavy chain (CD98hc), expressed at high levels in developing human trophoblasts, is an integral membrane protein with multiple N-linked gly-cosylation sites and known to be important for cell fusion, adhesion, and amino acid transport. Western blotting and flow cytometry were used to study the effect of brefeldin A, an inhibitor of protein translocation through the Golgi, on CD98hc in the human placental trophoblast cell line BeWo. | ỊFEBS Journal Membrane trafficking of CD98 and its ligand galectin 3 in BeWo cells - implication for placental cell fusion Paola Dalton1 Helen C. Christian1 Christopher W. G. Redman2 Ian L. Sargent2 and C. A. R. Boyd1 1 Department of Physiology Anatomy and Genetics University of Oxford UK 2 Nuffield Department of Obstetrics and Gynaecology John Radcliffe Hospital Oxford UK Keywords brefeldin A CD98 cell fusion galectin 3 trafficking Correspondence P. Dalton Department of Physiology Anatomy and Genetics University of Oxford Oxford OX1 3QX UK Fax 44 186 527 2420 Tel 44 795 286 8502 E-mail paoladalton@ Received 28 December 2006 revised 6 March 2007 accepted 23 March 2007 doi CD98 heavy chain CD98hc expressed at high levels in developing human trophoblasts is an integral membrane protein with multiple N-linked glycosylation sites and known to be important for cell fusion adhesion and amino acid transport. Western blotting and flow cytometry were used to study the effect of brefeldin A an inhibitor of protein translocation through the Golgi on CD98hc in the human placental trophoblast cell line BeWo. Although brefeldin A treatment caused increased cell surface expression of CD98hc a novel partially glycosylated form of the protein was found and concomitantly cell fusion was reduced. Western blotting showed that CD98 and galectin 3 a proposed ligand for the glycosylated extracellular domain of CD98hc co-immunoprecipitated and double-label immuno-electron microscopy confirmed that CD98hc associated with galec-tin 3. Furthermore cell fusion was reduced specifically by the disaccharide lactose a known ligand for the carbohydrate recognition domain of galectin 3 suggesting that the association was functional. Taken together the data suggest that N-glycosylation of CD98 and subsequent interaction with galectin 3 is critical for aspects of placental cell biology and provides a rationale for the observation that in the mouse .

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