Degradation and biosynthesis of the glucose transporter protein in chicken embryo fibroblasts transformed by the src oncogene.

AUTOR(ES)

Shawver, L K

RESUMO

The rate of glucose transport in cultured fibroblasts is regulated to a number of physiological variables, including malignant transformation by src, glucose starvation, and stimulation with mitogens. Much of this transport regulation can be accounted for by variations in the amount of transporter protein in the cells. To determine the mechanisms by which levels of the transporter are regulated, we measured the rates of synthesis and degradation of the transporter by pulse-chase experiments and immunoprecipitation of the transporter. We found that transformation by the src oncogene results in a large decrease in the rate at which the transporter protein is degraded but that it does not appreciably increase the rate of transporter biosynthesis. On the other hand, glucose starvation and mitogen stimulation increase the rate of transporter biosynthesis, although a role for control of degradation is possible in these circumstances also. Variations in the rate of glucose transport or the amount of the transporter are not associated with phosphorylation of the transporter protein.

Documentos Relacionados

• Differential regulation of glucose transporter isoforms by the src oncogene in chicken embryo fibroblasts.
• The src oncogene can regulate a human glucose transporter expressed in chicken embryo fibroblasts.
• Biosynthesis of calmodulin in normal and virus-transformed chicken embryo fibroblasts.
• Proteins antigenically related to the human erythrocyte glucose transporter in normal and Rous sarcoma virus-transformed chicken embryo fibroblasts.
• Phosphorylation and activation of epidermal growth factor receptors in cells transformed by the src oncogene.