Abstract
Glycolysis in normal resting rat kidney cells (NRK-49F) was stimulated by a 2-h exposure to transforming growth factors prior to assay. Transforming growth factor .beta. (TGF-.beta.) was effective when added alone, and further addition of epidermal growth factor (EGF) had little effect. The stimulation by TGF-.beta. was abolished when cycloheximide was present during the incubation, suggesting that protein synthesis is required for the effect. Incubation of the cells with 25 mM M abolished the stimulation of glycolysis by TGF-.beta.. The uptake of methylaminoisobutyrate via system A was stimulated by either TGF-.beta. or EGF. The > 3-fold stimulation of uptake by 1 ng of pure TGF-.beta. per ml was usually somewhat enhanced on addition of 0.5 ng of EGF per ml. An antiserum against EGF receptor partially depressed the response to TGF-.beta., suggesting some overlapping interactions of EGF and TGF-.beta.