Activation of hexose transport by antibody.

In our attempts to study alterations in cell behaviour by membrane perturbations, the effects of specific antisera on membrane functions were examined. The present communication reports the nature and kinetics of the changes in hexose transport as a result of treatment of L6 rat myoblast cells with specific antibodies. Exposure to complement-inactivated rabbit anti-myoblast antiserum resulted in an almost immediate two- to three-fold increase in hexose transport; morphological changes were observed only after prolonged incubation with the antiserum. Similar stimulation of hexose transport was observed upon exposure of cells to immunoglobulin G (IgG) from both sheep anti-myoblast and rabbit anti-myoblast plasma membrane sera. It seems that the interaction of specific IgG with cell surface components is sufficient to elicit this response. We have established that over 90% of 2-deoxyglucose is phosphorylated upon entrance into rat myoblasts and that exposure of cells to specific antibody does not cause changes in cell volume or general leakiness of the cell membrane. The antibody-stimulated hexose transport system resembles its normal counterpart in its substrate affinity and specificity; it differs from that of the control cells only in the transport capacity. This increase in hexose capacity is brought about by processes independent of protein synthesis and is not likely the result of extensive reorganization of membrane components.