The Journal of Cell Biology, Vol 100, 1548-1557, Copyright © 1985 by The Rockefeller University Press

ARTICLES

Anion transporter: highly cell-type-specific expression of distinct polypeptides and transcripts in erythroid and nonerythroid cells

JV Cox, RT Moon and E Lazarides

Affinity-purified antibodies and cDNA probes specific for the chicken erythrocyte anion transporter (also referred to as band 3) have been used to demonstrate that this protein is expressed in a highly cell- type-specific manner in the avian kidney. Indirect immunofluorescence analysis indicates that this polypeptide is present in only a small subset of total kidney cells and is predominantly localized to the proximal convoluted tubule of this organ. Chicken erythrocytes synthesize and accumulate two structurally and serologically related band 3 polypeptides. The polypeptide that accumulates in kidney membranes has an apparent molecular weight greater than either of its erythroid counterparts. This diversity is also reflected at the RNA level, as the single band 3 mRNA species detected during various stages of erythroid development is distinct in size from that found in kidney cells. Genomic DNA blot analysis suggests that both the erythroid and kidney band 3 RNAs arise from a single gene. Furthermore, of the adult tissues we have examined that are known to express ankyrin and spectrin polypeptides, only kidney accumulates detectable levels of the band 3 mRNA and polypeptide. These observations suggest that a subset of kidney cells use an anion transport mechanism analogous to that of erythrocytes and that band 3 is expressed in a noncoordinate manner with other components of the erythroid membrane skeleton in nonerythroid cells.
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This article has been cited by other articles:

• Ghosh, S., Dorsey, F. C., Cox, J. V. (2002). CK2 constitutively associates with and phosphorylates chicken erythroid ankyrin and regulates its ability to bind to spectrin. J. Cell Sci. 115: 4107-4115 [Abstract] [Full Text]  
• Holappa, K., Suokas, M., Soininen, P., Kellokumpu, S. (2001). Identification of the Full-length AE2 (AE2a) Isoform as the Golgi-associated Anion Exchanger in Fibroblasts. J. Histochem. Cytochem. 49: 259-270 [Abstract] [Full Text]  
• Kellokumpu, S, Neff, L, Jamsa-Kellokumpu, S, Kopito, R, Baron, R (1988). A 115-kD polypeptide immunologically related to erythrocyte band 3 is present in Golgi membranes. Science 242: 1308-1311 [Abstract]  
• Fraser, P J, Curtis, P J (1987). Specific pattern of gene expression during induction of mouse erythroleukemia cells.. Genes Dev. 1: 855-861 [Abstract]  
• Drenckhahn, D, Schluter, K, Allen, D., Bennett, V (1985). Colocalization of band 3 with ankyrin and spectrin at the basal membrane of intercalated cells in the rat kidney. Science 230: 1287-1289 [Abstract]  

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