Proteins antigenically related to the human erythrocyte glucose transporter in normal and Rous sarcoma virus-transformed chicken embryo fibroblasts.

Publisher Website
Google Scholar
Abstract
Antibody raised against the purified human erythrocyte glucose transporter specifically precipitated 4 proteins from normal and Rous sarcoma virus-transformed chicken embryo cells; a major protein of MW 41,000 and minor proteins of MW 68,000, 73,000, and 82,000. The MW 41,000 and 82,000 proteins were found only in a membrane fraction, not in the soluble fraction, and displayed a heterogeneous mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, suggesting glycosylation. The MW 41,000 and 82,000 proteins were increased in amount after malignant transformation in direct proportion to the increase in hexose transport rate and the increase was dependent on the expression of the src gene product as revealed with a temperature-conditional src mutant. The MW 41,000 and 82,000 proteins evidently are the glucose transporter of chicken embryo fibroblasts or a component of the glucose transporter. Malignant transformation apparently increases the rate of glucose transport by increasing the number of transporters in the membrane.