Stimulation of glycolysis and amino acid uptake in NRK-49F cells by transforming growth factor beta and epidermal growth factor.

Glycolysis in normal resting rat kidney cells (NRK-49F) was stimulated by a 2-hr 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 methionine abolished the stimulation of glycolysis by TGF-beta. The uptake of methylaminoisobutyrate via system A was stimulated by either TGF-beta or EGF. The greater than 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. Moreover, an antiserum against EGF receptor partially depressed the response to TGF-beta, suggesting some overlapping interactions of EGF and TGF-beta.