The Prostate Plasma Membrane as an Androgen Receptor

References

• Akera T., Brody T.M. Membrane adenosinetriphosphatase. The effect of potassium on the formation and dissociation of the ouabain-enzyme complex. J. Pharmacol. Exp. Ther. 1971; 176: 545–557
   PubMedGoogle Scholar
• Allen J.C., Harris R.A., Schwartz A. The nature of the transport ATPase-digitalis complex. I. Formation and reversibility in the presence and absence of a phosphorylated enzyme. Biochem. Biophys. Res. Commun. 1971; 42: 366–370
   PubMed Web of Science ®Google Scholar
• Amler E., Tseisinger J., Svoboda P. Mg2+-induced changes of lipid order and conformation of (Na+ + K+)-ATPase. Biochim. Biophys. Acta 1987; 905: 376–382
   PubMedGoogle Scholar
• Askari A., Kakar S.S., Huang W.-H. Ligand binding sites of ouabain-complexed (Na+ + K+)-ATPase. J. Biol. Chem. 1988; 263: 235–242
   PubMed Web of Science ®Google Scholar
• Bannerjee S.P., Wong S.M.E., Kana V.K., Sen A.K. Inhibitors of sodium and potassium-dependent adenosine triphosphatase by N-ethylmaleimide. I. Effect on sodiumsensitive phosphorylation and potassium-sensitive dephosphorylation. Mol. Pharmacol. 1972; 9: 8–17
   Google Scholar
• Barnett R.E. Effect of monovalent cations on the ouabain inhibition of the sodium and potassium ion activated adenosine triphosphatase. Biochemistry 1970; 9: 4644–4648
   PubMed Web of Science ®Google Scholar
• Benarous R., Gacom G. Ca2+-induced spectral changes in human prothrombin. Biochim. Biophys. Acta 1980; 622: 179–188
   PubMedGoogle Scholar
• Brinkmann A.O., Klaasen P., Kuiper G. G.J.M., van der Korput J. A.G.M., Bolt J., de Boer W., Smit A., Faber P.W., van Rooij H.C.J., van Kessel A.G., Voorhorst M.M., Mulder E., Trapman J. Structure and function of the androgen receptor. Urol. Res. 1989; 17: 87–93
   PubMedGoogle Scholar
• Bruchovsky N., Lesser B., Van Doom E., Craven S. Hormonal effects on cell proliferation in rat prostate. Vit. Horm. 1975; 33: 61–100
   PubMedGoogle Scholar
• Eicinger J., Feuer B., Lamola A.A. Intramolecular energy transfer in adrenocorticotropin. Biochemistry 1969; 8: 3908–3915
   PubMedGoogle Scholar
• Farnsworth W.E. Activities of the androgen-responsive receptor of the prostatic plasma membrane. Invest. Urol. 1977; 15: 75–77
   PubMedGoogle Scholar
• Fortes P.A.G. Anthroyl ouabain: A specific fluorescent probe for the cardiac glycoside receptor of the Na-K ATPase. Biochemistry 1977; 16: 531–540
   PubMedGoogle Scholar
• Giotta G.J. Quaternary structure of (Na+ + K+)-dependent adenosine triphosphatase. J. Biol. Chem. 1976; 251: 1247–1252
   PubMedGoogle Scholar
• Hansen O. Reactive states of the Na,K-ATPase demonstrated by the stability of the enzyme-ouabain complex. Na,K-ATPase. Structure and Kinetics, J.C. Skou, J.G. Nørby. Academic Press, New York 1979; 169–180
   Google Scholar
• Hokin L.E., Dahl J.L., Deupree J.D., Dixon J.F., Hackney J.F., Perdue J.F. Studies on the characterization of the sodium-potassium transport of the enzyme from the rectal gland of Squalus acanthius. J. Biol. Chem. 1973; 248: 2593–2605
   PubMedGoogle Scholar
• Jørgensen P.L. Mechanism of Na+,K+ pump. Protein structure and conformations of the pure (Na+ + K +)-ATPase. Biochim. Biophys. Acta 1982; 694: 27–68
   PubMed Web of Science ®Google Scholar
• Kaniike K., Lindenmayer G.E., Wallick E.T., Lane L.K., Schwartz A. Specific sodium-22 binding to purified sodium + potassium adenosine triphosphatase. J. Biol. Chem. 1977; 251: 4794–4795
   Google Scholar
• Karlish S.J.D., Yates D.W. Tryptophan fluorescence of (Na+ + K+)-ATPase as a tool for study of the enzyme mechanism. Biochim. Biophys. Acta 1978; 527: 115–130
   PubMedGoogle Scholar
• Kowarski A., Shalf J., Migeon C.J. Concentration of testosterone and dihydrotestosterone in subcellular fractions of liver, kidney, prostate and muscle in the male dog. J. Biol. Chem. 1969; 244: 5269–5272
   PubMedGoogle Scholar
• Lane L.K., Gupte S.S., Collins J.H., Wallick E.T., Johnson J.D., Schwartz A. Purification and characterization of lamb kidney Na,K-ATPase. Na,K-ATPase. Structure and Kinetics, J.C. Skou, J.G. Nørby. Academic Press, New York 1979; 33–44
   Google Scholar
• Lee J.A., Fortes P.A.G. Spatial relationship and conformational changes between the cardiac glycoside site and beta-subunit oligosaccharides in sodium plus potassium activated adenosine triphosphatase. Biochemistry 1986; 25: 8133–8141
   PubMedGoogle Scholar
• Liao S., Tymoczko J.L., Castaneda E., Liang T. Vit. Horm. 1975; 33: 297–317
   PubMedGoogle Scholar
• Marshall M.O. Studies on the glycoprotein component of the (Na+ + K+)-ATPase from dogfish salt gland. Binding to concanavalin A and removal of sialic acid by neuraminidase. Biochim. Biophys. Acta 1976; 455: 837–848
   PubMedGoogle Scholar
• Muldoon T.G., Watson G.H., Evans A. C., Jr., Steinsapir U.J. Microsomal receptors for steroid hormones: functional implications for nuclear activity. J. Steroid Biochem. 1988; 30: 23–31
   PubMedGoogle Scholar
• Orlowski J., Lingrel J.B. Tissue-specific and developmental regulation of rat Na,K-ATPase catalytic α-isoform and β subunit mRNAs. J. Biol. Chem. 1988; 263: 10436–10442
   PubMed Web of Science ®Google Scholar
• Post R.L., Toda G., Rogers F.N. Phosphorylation by inorganic phosphate of sodium plus potassium ion transport adenosine triphosphatase: Four reactive states. J. Biol. Chem. 1975; 250: 691–701
   PubMedGoogle Scholar
• Repke K.R.H. A model for allosteric regulation of Na+/K+-transporting ATPase. Biochim. Biophys. Acta 1986; 864: 195–212
   PubMedGoogle Scholar
• Rosner W., Smith R.N. Isolation and characterization of the testosterone-oestradiol binding globulin from human plasma. Use of a novel affinity column. Biochemistry 1975; 14: 4813–4821
   PubMed Web of Science ®Google Scholar
• Scatchard G. The attractions of proteins for small molecules and ions. Ann. N.Y. Acad. Sci. 1949; 51: 660–672
   Web of Science ®Google Scholar
• Siegel G.J., Desmond T., Ernst S.A. Immunoreactivity and ouabain-dependent phosphorylation of (Na+ + K+)-adenosinetriphosphatase catalytic subunit doublets. J. Biol. Chem. 1986; 261: 13768–13776
   PubMedGoogle Scholar
• Steinberg I.Z. Long-range nonradiative transfer of electronic excitation energy in proteins and polypeptides. Annu. Rev. Biochem. 1971; 40: 83–114
   PubMed Web of Science ®Google Scholar
• Steinsapir J., Evans A. C., Jr., McDonald T., Muldoon T.G. Association of androgen binding sites with the endoplasmic reticulum of rat ventral prostate. Biol. Reprod. 1990; 42: 337–349
   PubMedGoogle Scholar
• Teale F.W.J., Weber G. Ultraviolet fluorescence of the aromatic amino acids. Biochem. J. 1957; 65: 476–482
   PubMedGoogle Scholar
• Tobin T., Akera T., Baskin S.I., Brody T.M. Calcium ion and sodium and potassium-dependent adenosine triphosphatase: Its mechanism of inhibition and identification of the E-P intermediate. Mol. Pharmacol. 1973; 9: 336–349
   PubMedGoogle Scholar
• Yoda A., Yoda S. Formation of ADP-sensitive phosphorylated intermediates in the electric eel Na,K-ATPase preparation. Mol. Pharmacol. 1982; 22: 693–699
   PubMedGoogle Scholar