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Vol. 11, Issue 7, 1211-1220, July 2001

LETTER
The Repertoire of Na,K-ATPase alpha  and beta  Subunit Genes Expressed in the Zebrafish, Danio rerio

S. Johannes R. Rajarao,1 Victor A. Canfield,1 Manzoor-Ali P.K. Mohideen,2 Yi-Lin Yan,3 John H. Postlethwait,3 Keith C. Cheng,2 and Robert Levenson1,4

1 Department of Pharmacology and 2 The Jake Gittlen Cancer Research Institute and Department of Pathology, Pennsylvania State College of Medicine, Hershey, Pennsylvania 17033, USA; 3 Institute of Neuroscience, University of Oregon, Eugene, Oregon 97403, USA

We have identified a cohort of zebrafish expressed sequence tags encoding eight Na,K-ATPase alpha  subunits and five beta  subunits. Sequence comparisons and phylogenetic analysis indicate that five of the zebrafish alpha  subunit genes comprise an alpha 1-like gene subfamily and two are orthologs of the mammalian alpha 3 subunit gene. The remaining alpha  subunit clone is most similar to the mammalian alpha 2 subunit. Among the five beta  subunit genes, two are orthologs of the mammalian beta 1 isoform, one represents a beta 2 ortholog, and two are orthologous to the mammalian beta 3 subunit. Using zebrafish radiation hybrid and meiotic mapping panels, we determined linkage assignments for each alpha  and beta  subunit gene. Na,K-ATPase genes are dispersed in the zebrafish genome with the exception of four of the alpha 1-like genes, which are tightly clustered on linkage group 1. Comparative mapping studies indicate that most of the zebrafish Na,K-ATPase genes localize to regions of conserved synteny between zebrafish and humans. The expression patterns of Na,K-ATPase alpha  and beta  subunit genes in zebrafish are quite distinctive. No two alpha  or beta  subunit genes exhibit the same expression profile. Together, our data imply a very high degree of Na,K-ATPase isoenzyme heterogeneity in zebrafish, with the potential for 40 structurally distinct alpha /beta subunit combinations. Differences in expression patterns of alpha  and beta  subunits suggest that many of the isoenzymes are also likely to exhibit differences in functional properties within specific cell and tissue types. Our studies form a framework for analyzing structure function relationships for sodium pump isoforms using reverse genetic approaches.

4 Corresponding author.

11:1211-1220 ©2001 by Cold Spring Harbor Laboratory Press  ISSN 1088-9051/01 $5.00
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