High impact information on nrv1

• The highly conserved cardiac glycoside binding site of Na,K-ATPase plays a role in blood pressure regulation [1].
• The Na,K-ATPase contains a binding site for cardiac glycosides, such as ouabain, digoxin, and digitoxin, which is highly conserved among species ranging from Drosophila to humans [1].
• Nrv1 and Nrv2.1/2.2 have open reading frames of 309 and 322/323 amino acids, respectively, and they are 43.4% identical at the amino acid level [2].
• The heterodimeric Na,K-ATPase has been implicated in vertebrate and invertebrate epithelial cell junctions, morphogenesis and oncogenesis, but the mechanisms involved are unclear [3].
• Only 3kb of DNA separate the 3' end of Nrv2 from Nrv1 [4].

Biological context of nrv1

• P-element transformation vectors were constructed, which contained either 7.7kb of Nrv2 or 3.5kb Nrv1 5' flanking DNA driving expression of a lacZ reporter gene [4].
• Taken together these results demonstrate that the cardiac glycoside binding site of the alpha isoforms of the Na,K-ATPase have a physiological function and supports the hypothesis for a role of the endogenous cardiac glycosides [1].
• Using the Gal4-UAS system we have limited expression of alpha transgenes to cell types that normally express a particular Drosophila Na(+),K(+)-ATPase beta (Nervana) subunit isoform (Nrv1 or 2) [5].

Analytical, diagnostic and therapeutic context of nrv1

• Three cDNA clones (designated Nrv1, Nrv2.1, and Nrv2.2) were isolated that code for proteins recognized by anti-Nrv mAbs on Western blots [2].

References