Ouabain-Resistant Mutants of the Rat Na,K-ATPase α2 Isoform Identified by Using an Episomal Expression Vector

Literature Cited

• Ahmed, K., D. C. Rohrer, D. S. Fullerton, T. Deffo, E. Kitatsuji, and A. H. L. From. 1983. Interaction of (Na+)-ATPase and digitalis genins. J. Biol. Chem. 258:8092–8097.
   PubMed Web of Science ®Google Scholar
• Cantley, L. C. 1981. Structure and mechanism of the (Na,K)- ATPase. Curr. Top. Bioenerg. 11:201–237.
   Google Scholar
• Emanuel, J. R., S. Garetz, L. Stone, and R. Levenson. 1987. Differential expression of Na,K-ATPase a- and β-subunit mR-NAs in rat tissues and cell lines. Proc. Natl. Acad. Sci. USA 84:9030–9034.
   PubMedGoogle Scholar
• Emanuel, J. R., S. Graw, D. Housman, and R. Levenson. 1989. Identification of a region within the Na,K-ATPase α subunit that contributes to differential ouabain sensitivity. Mol. Cell. Biol. 9:3744–3749.
   PubMedGoogle Scholar
• Emanuel, J. R., J. Schulz, X.-M. Zhou, R. B. Kent, D. Housman, L. Cantley, and R. Levenson. 1988. Expression of an ouabain-resistant Na,K-ATPase in CV-1 cells after transfection with a cDNA encoding the rat Na,K-ATPase al subunit. J. Biol. Chem. 263:7726–7733.
   PubMedGoogle Scholar
• Forbush, B., III. 1983. Cardiotonic steroid binding to Na,K- ATPase. Curr. Topics Membr. Transp. 19:167–201.
   Google Scholar
• Fortes, P. A. G. 1977. Anthroylouabain: a specific fluorescent probe for the cardiac glycoside receptor of the Na,K-ATPase. Biochemistry 16:531–540.
   PubMedGoogle Scholar
• Glassy, M. C., H. H. Handley, H. Hagiwara, and I. Royston. 1983. UC 729-6, A human lymphoblastoid B-cell line useful for generating antibody-secreting human-human hybridomas. Proc. Natl. Acad. Sci. USA 80:6327–6331.
   PubMed Web of Science ®Google Scholar
• Goeldner, M. P., C. G. Hirth, B. Rossi, G. Ponzio, and M. Lazdunski. 1983. Specific photoaffinity labeling of the digitalis binding site of the sodium and potassium activated adenosinetriphosphatase induced by energy transfer. Biochemistry 22:4685–4690.
   PubMedGoogle Scholar
• Graham, F. L., J. Smiley, W. C. Russell, and R. Nairn. 1977. Characteristics of a human cell line transformed by DNA from human adenovirus type 5. J. Gen. Virol. 36:59–72.
   PubMed Web of Science ®Google Scholar
• Hara, Y., A. Nikamoto, T. Kojima, A. Matsumoto, and M. Nakao. 1988. Expression of sodium pump activities in BALB/c 3T3 cells transfected with cDNA encoding a3 subunits of rat brain Na,K-ATPase. FEBS Lett. 238:27–30.
   PubMedGoogle Scholar
• Hattori, M., and Y. Sakaki. 1986. Dideoxy sequencing method using denatured plasmid templates. Anal. Biochem. 152:232–238.
   PubMed Web of Science ®Google Scholar
• Herrera, V. L. M., J. R. Emanuel, N. Ruiz-Opazo, R. Levenson, and B. Nadal-Ginard. 1987. Three differentially expressed Na,K-ATPase a subunit isoforms: structural and functional implications. J. Cell Biol. 105:1855–1865.
   PubMedGoogle Scholar
• Kawakami, K., T. Ohta, H. Nojima, and K. Nagano. 1986. Primary structure of the a subunit of human Na,K-ATPase deduced from cDNA sequence. J. Biochem. 100:389–397.
   PubMed Web of Science ®Google Scholar
• Kent, R. B., J. R. Emanuel, Y. Ben Neriah, R. Levenson, and D. E. Houseman. 1987. Ouabain resistance conferred by expression of the cDNA for a murine Ka+,K+-ATPase a subunit. Science 237:901–903.
   PubMedGoogle Scholar
• Kent, R. B., D. A. Fallows, E. Geissler, T. Glaser, J. R. Emanuel, P. A. Lalley, R. Levenson, and D. E. Housman. 1987. Genes encoding α and β subunits of the Na,K-ATPase are located on three different chromosomes in the mouse. Proc. Natl. Acad. Sci. USA 84:5369–5373.
   PubMedGoogle Scholar
• Kunkel, T. A. 1985. Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA 82:488–492.
   PubMed Web of Science ®Google Scholar
• Margolskee, R. F., P. Kavathas, and P. Berg. 1988. Epstein-Barr virus shuttle vector for stable episomal replication of cDNA expression libraries in human cells. Mol. Cell. Biol. 8:2837–2847.
   PubMed Web of Science ®Google Scholar
• Okayama, H., and P. Berg. 1983. A cDNA cloning vector that permits expression of cDNA inserts in mammalian cells. Mol. Cell. Biol. 3:280–289.
   PubMed Web of Science ®Google Scholar
• Ovchinnikov, Y. A., N. N. Modyanov, N. E. Broude, K. E. Petrukhin, A. V. Grishin, N. A. Arzamazova, N. A. Aldanova, and E. D. Sverdlov. 1986. Pig kidney Na+,K+-ATPase. FEBS Lett. 201:237–245.
   PubMed Web of Science ®Google Scholar
• Price, E. M., and J. B. Lingrel. 1988. Structure-function relationships in the Na,K-ATPase a subunit: site directed mutagenesis of glutamine-111 to argine and asparagine 122 to aspartic acid generates a ouabain-resistant enzyme. Biochemistry 27:8400–8408.
   PubMed Web of Science ®Google Scholar
• Shull, G. E., J. Greeb, and J. B. Lingrel. 1986. Molecular cloning of three distinct forms of the Na+,K+-ATPase a subunit from rat brain. Biochemistry 25:8125–8132.
   PubMed Web of Science ®Google Scholar
• Shull, G. E., A. Schwartz, and J. B. Lingrel. 1985. Amino-acid sequence of the catalytic subunit of the (Na+ + K+)ATPase deduced from a complementary DNA. Nature (London) 316:691–695.
   PubMed Web of Science ®Google Scholar
• Sweadner, K. J. 1989. Isozymes of the Na+/K+-ATPase. Biochim. Biophys. Acta 988:185–220.
   PubMed Web of Science ®Google Scholar
• Tobin, T., and T. M. Brody. 1972. Rates of dissociation of enzyme-ouabain complexes and K0.5 values in (Na+ + K+) adenosine triphosphatase from different species. Biochem. Pharmacol. 21:1553–1560.
   PubMed Web of Science ®Google Scholar
• Wallick, E. T., B. J. R. Pitts, L. K. Lane, and A. Schwartz. 1980. A kinetic comparison of cardiac glycoside interactions with Na+,K+-ATPases from skeletal and cardiac muscle and from kidney. Arch. Biochem. Biophys. 202:442–449.
   PubMed Web of Science ®Google Scholar
• Wigler, M., S. Silverstein, L. S. Lee, A. Pellicer, Y.-C. Cheng, and R. Axel. 1977. Transfer of purified herpes virus thymidine kinase gene to cultured mouse cells. Cell 11:223–232.
   PubMed Web of Science ®Google Scholar
• Yates, J. L., N. Warren, and B. Sugden. 1985. Stable replication of plasmids derived from Epstein-Barr virus in various mammalian cells. Nature (London) 313:812–815.
   PubMed Web of Science ®Google Scholar