Studies on the effect of glycoprotein processing inhibitors on fusion of L6 myoblast cell lines |
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| Authors: | M A Spearman J C Jamieson J A Wright |
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| Affiliation: | 1. GHU Paris Psychiatrie & Neurosciences, Hôpital Sainte-Anne, Service Hospitalo-Universitaire, Pôle Hospitalo-Universitaire Paris 15, Paris, France;2. Université de Paris, Paris, France;3. Physics for Medicine Paris, INSERM, ESPCI Paris, CNRS, PSL Research University, Université Paris Diderot, Sorbonne Paris Cite, Paris, France;4. Institut Pasteur, G5 Evolutionary Genomics of RNA Viruses, Paris, France;5. Institut Pasteur, Experimental Neuropathology Unit, Paris, France;6. Institut Pasteur, Functional Genetics of Infectious Diseases Unit, Paris, France;7. Institut Pasteur, Chemogenomic and Biological Screening Core Facility, C2RT, Paris, France;8. Fondation Rothschild, Department of Anaesthesiology, ASMR-II Consulting, Regstem, Paris, France;9. Université de Paris, Laboratoire de Psychologie du développement et de l''Education de l''Enfant, CNRS, Paris, France;10. Université de Paris, Institut de Psychiatrie et Neurosciences de Paris, INSERM, Paris, France;11. GHU Paris Psychiatrie & Neurosciences, Hôpital Sainte-Anne, Service de Neuropathologie, Paris, France |
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| Abstract: | The effect of oligosaccharide processing inhibitors on the fusion of L6 myoblasts was studied. The glucosidase inhibitors, castanospermine, 1-deoxynojirimycin and N-methyl-deoxynojirimycin were potent inhibitors of myoblast fusion, as was the mannosidase II inhibitor, swainsonine. Inhibition of fusion was reversed when inhibitors were removed. However, the mannosidase I inhibitor, 1-deoxymannojirimycin did not inhibit fusion. Changes in cell membrane oligosaccharide structure were followed by monitoring the binding of concanavalin A (conA) and wheat germ agglutinin (WGA) to cell surface membranes in cells treated with processing inhibitors. All the processing inhibitors resulted in increased binding of conA and decreased binding of WGA; this is consistent with the known mechanisms of inhibition of the inhibitors used in the study. Inhibition of fusion by the processing inhibitors also resulted in reduced activities of creatine phosphokinase, an enzyme used as a marker for biochemical differentiation during fusion. Treatment of a non-differentiating conA-resistant cell line with processing inhibitors did not induce fusion, but the cells did show altered lectin-binding properties. The main conclusion drawn from these studies is that cell surface glycoproteins probably containing the mannose (Man)9 structure are important for the fusion reaction. |
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