Glucose transport protein is structurally and immunologically related to band 3 and senescent cell antigen.

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Senescent cell antigen, a polypeptide that appears on the surface of senescent and damaged cells, has been shown to be derived from band 3. In the present study, the relationship between the as yet unidentified glucose transporter and senescent cell antigen is examined. Since cytochalasin B is a specific and potent competitive inhibitor of glucose transport in human erythrocytes, the glucose transport carrier was isolated by affinity chromatography on cytochalasin B-Sepharose 4B columns and eluted with D-glucose. This purification procedure is both a method of isolation and a functional assay for the glucose transporter. Purified glucose transporter gave a sharp, single band at Mr approximately equal to 60,000 when analyzed by NaDod-SO4/PAGE. Glucose transporter was identified in erythrocyte membranes by the immunoblotting technique, using both antibodies raised against purified glucose transporter and anti-idiotypic antibodies. Two-dimensional peptide mapping revealed substantial peptide homology between glucose transporter and senescent cell antigen. In addition, the glucose transporter shared peptide homology with band 3 and its defined proteolytic fragments located toward the carboxyl terminus of band 3. Peptide homology between glucose transporter and the Mr approximately equal to 41,000 cytoplasmic segment of band 3 that contains the amino terminus could not be demonstrated. Thus, glucose transporter appears to be part of or derived from band 3, and to share substantial peptide homology with senescent cell antigen.

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