Novel oligodendrocyte transmembrane signaling systems. Investigations utilizing antibodies as ligands.
Antibodies are increasingly being used as tools to study the function of cell surface markers. Several types of responses may occur upon the selective binding of an antibody to an epitope on a receptor. Antibody binding may trigger signals that are normally transduced by endogenous ligands. Moreover, antibody binding may activate normal signals in a manner that disrupts a sequence of events that coordinates either differentiation, mitogenesis, or morphogenesis. Alternately, it is possible that binding elicits either a modified signal or no signal. This article focuses on the cascade of events that occur following specific antibody binding to myelin markers expressed by cultured murine oligodendrocytes. Binding of specific antibodies to the oligodendrocyte membrane surface markers myelin/oligodendrocyte glycoprotein (MOG), myelin/oligodendrocyte specific protein (MOSP), galactocerebroside (GalC), and sulfatide on cultured murine oligodendrocytes results in different effects with regard to phospholipid turnover, Ca2+ influxes, and antibody:marker distribution. The consequence of each antibody-elicited cascade of events appears to be the regulation of the cytoskeleton within the oligodendroglial membrane sheets. The antibody binding studies described in this article demonstrate that these myelin surface markers are capable of transducing signals. Since endogenous ligands for these myelin markers have yet to be identified, it is not known if these signals are normally transduced or are a modification of normally transduced signals.
Department of Biomedical Sciences, E. K. Shriver Center, Waltham, MA 02254.
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D000818:Animals; D000906:Antibodies / Q000276:immunology; D000937:Antigen-Antibody Reactions; D000954:Antigens, Surface / Q000276:immunology / Q000502:physiology*; D002118:Calcium / Q000502:physiology; D002478:Cells, Cultured; D003599:Cytoskeleton / Q000648:ultrastructure; D005699:Galactosylceramides / Q000276:immunology / Q000502:physiology; D008562:Membrane Glycoproteins / Q000276:immunology / Q000502:physiology; D008563:Membrane Lipids / Q000502:physiology; D051379:Mice; D009185:Myelin Proteins; D009186:Myelin Sheath / Q000502:physiology; D018992:Myelin-Associated Glycoprotein; D063308:Myelin-Oligodendrocyte Glycoprotein; D009836:Oligodendroglia / Q000502:physiology* / Q000648:ultrastructure; D010743:Phospholipids / Q000502:physiology; D011956:Receptors, Cell Surface / Q000276:immunology / Q000502:physiology; D015398:Signal Transduction; D013433:Sulfoglycosphingolipids / Q000276:immunology / Q000378:metabolism
D000906:Antibodies; D000954:Antigens, Surface; D005699:Galactosylceramides; D008562:Membrane Glycoproteins; D008563:Membrane Lipids; C571327:Mog protein, mouse; D009185:Myelin Proteins; D018992:Myelin-Associated Glycoprotein; D063308:Myelin-Oligodendrocyte Glycoprotein; D010743:Phospholipids; D011956:Receptors, Cell Surface; D013433:Sulfoglycosphingolipids; D002118:Calcium