ARE THERE SEVERAL ISOFORMS OF NA,K-ATPASE ALPHA-SUBUNIT IN THE RABBITKIDNEY

Previous pharmacologic and kinetic studies have demonstrated the axial heterogeneity of the rabbit kidney tubule with regard to Na,K-ATPase. To evaluate whether this heterogeneity might reflect the presence of distinct isoforms of the alpha subunit of Na,K-ATPase, we used two mon oclonal antibodies, IIC9 and IIE2 (G8), specific for the alpha1 and al pha3 isoforms, respectively, as probes for changes in the specific act ivity of Na,K-ATPase at the level of successive segments of the rabbit nephron. Single, well defined nephron segments were obtained by micro dissection of collagenase-treated kidney. Results indicate that IIC9 a ntibody inhibited Na,K-ATPase activity by >90% in all the segments of the nephron except the collecting duct. Conversely, IIE2 (G8) antibody abolished Na,K-ATPase activity in the collecting duct, whereas it had no effect in other nephron segments. These findings suggest that the rabbit collecting duct preferentially expresses a distinct isoform of Na,K-ATPase catalytic subunit, which is presumably alpha3-like, in agr eement with previous pharmacologic and kinetic observations, whereas o ther nephron segments would express the alpha1 isoform.