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Abstract:

The binding of aldosterone (ALDO) to the mineralocorticoid receptor (MR) induces a conformational change of the protein referred to as 'transformation'. This feature can be evidenced in vivo by the capacity of the MR to interact with chromatin, and in vitro by the ability of the MR to bind to DNA strands or to shift the sedimentation coefficient (S) to lower values. The transformation process allows MR to work as a transcription factor after interacting with specific sequences of DNA. The signal transduction pathway for the MR transformation remains unknown. As a first step towards elucidating the mechanism of steroid-dependent MR transformation, we asked if the MR-signaling pathway is affected by the phosphorylation status of the MR-heterocomplex, and how that pathway may be regulated. Incubation of preformed [3H]ALDO-MR complex with bovine intestinal alkaline phosphatase led to an increase in the rate of MR-transformation (measured as 9.4-5.4S shift). This alkaline phosphatase-dependent MR transformation was inhibited by the specific alkaline phosphatase-type inhibitor levamisole, and was not evident in incubations performed with acid phosphatases. A direct correlation between the DNA-cellulose binding capacity of the [3H]ALDO-MR complex and the percentage of transformed 5.4S MR form was also observed. When rat kidney cytosol was incubated in the absence of both exogenous phosphatase and stabilizing agents (such as molybdate or vanadate), MR transformation also took place, in a time- and temperature-dependent process. In contrast with the inhibitory effect observed upon alkaline phosphatase-promoted transformation, levamisole was unable to inhibit the endogenous transforming activity of MR, suggesting that an endogenous phosphatase other than those which belong to the alkaline-type may be responsible for that transformation. Tautomycin, a polyketide produced by the soil bacteria Streptomyces which inhibits serine/threonine phosphatases of the PP1/PP2A subgroup, was able to inhibit the endogenous phosphatase activity in a concentration-dependent form (K(i(app))=7.35 nM). These results support the idea that the endogenous renal activity involved in the regulation of rat kidney MR transformation may be a protein phosphatase which belongs to the PP1/PP2A subgroup. Copyright (C) 1998 Elsevier Science Ireland Ltd.

Registro:

Documento: Artículo
Título:Tautomycin inhibits phosphatase-dependent transformation of the rat kidney mineralocorticoid receptor
Autor:Piwien-Pilipuk, G.; Galigniana, M.D.
Filiación:Depto. de Quim. Biológica, Fac. Cie. Exact. Y Nat., Univ. B., 1428 Buenos Aires, Argentina
Palabras clave:Mineralocorticoid receptor; Protein phosphatases; Receptor transformation; Tautomycin (rat kidney); acid phosphatase; aldosterone; alkaline phosphatase; levamisole; mineralocorticoid receptor; phosphoprotein phosphatase; tautomycin; transcription factor; animal tissue; article; complex formation; conformational transition; controlled study; cytosol; enzyme activity; enzyme inhibition; kidney; male; nonhuman; phosphorylation; priority journal; protein conformation; rat; reaction time; signal transduction; temperature dependence; Aldosterone; Alkaline Phosphatase; Animals; Antibiotics, Antifungal; Cell Nucleus; Cellulose; Centrifugation, Density Gradient; Chromatography, Ion Exchange; Cytoplasm; DNA; Dose-Response Relationship, Drug; Kidney; Kinetics; Levamisole; Male; Phosphoprotein Phosphatase; Protein Conformation; Pyrans; Rats; Rats, Sprague-Dawley; Receptors, Mineralocorticoid; Spiro Compounds; Temperature
Año:1998
Volumen:144
Número:1-2
Página de inicio:119
Página de fin:130
DOI: http://dx.doi.org/10.1016/S0303-7207(98)00142-7
Título revista:Molecular and Cellular Endocrinology
Título revista abreviado:Mol. Cell. Endocrinol.
ISSN:03037207
CODEN:MCEND
CAS:Aldosterone, 52-39-1; Alkaline Phosphatase, EC 3.1.3.1; Antibiotics, Antifungal; Cellulose, 9004-34-6; DNA, 9007-49-2; DNA-cellulose; Levamisole, 14769-73-4; Phosphoprotein Phosphatase, EC 3.1.3.16; Pyrans; Receptors, Mineralocorticoid; Spiro Compounds; tautomycin, 109946-35-2
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03037207_v144_n1-2_p119_PiwienPilipuk

Referencias:

  • Alnemri, E.S., Maksymowych, A.B., Robertson, N.M., Litwack, G., Overexpression and characterization of the human mineralocorticoid receptor (1991) J. Biol. Chem., 266, pp. 18072-18081
  • Arnold, S.F., Obouron, J.D., Yudt, M.R., Carter, T.H., Notides, A.C., In vivo and in vitro phosphorylation of the human estrogen receptor (1995) J. Steroid Biochem. Mol. Biol., 52, pp. 159-171
  • Arriza, J.L., Weinberger, C., Cerelli, G., Cloning of human mineralocorticoid receptor complementary DNA: Structure and functional kinship with the glucocorticoid receptor (1987) Science, 237, pp. 268-275
  • Bamberger, C.M., Wald, M., Bamberger, A.M., Schulte, H.M., Inhibition of mineralocorticoid and glucocorticoid receptor function by the heat shock protein 90-binding agent geldanamycin (1997) Mol. Cell. Endocrinol., 131, pp. 233-240
  • Bamberger, C.M., Bamberger, A.M., Wald, M., Chrousos, G.P., Schulte, H.M., Inhibition of mineralocorticoid activity by the β-isoform of the human glucocorticoid receptor (1997) J. Steroid Biochem. Mol. Biol., 60, pp. 43-50
  • Barnett, C.A., Schmidt, T.J., Litwack, G., Effects of calf intestinal alkaline phosphatase, phosphatase inhibitors and phosphorylated compounds on the rate of activation of glucocorticoid-receptor complexes (1980) Biochemistry, 19, pp. 5446-5455
  • Beato, M., Gene regulation by steroids hormones (1989) Cell, 56, pp. 335-344
  • Becker, W., Kentrup, H., Klumpp, S., Schultz, J.E., Joost, H.G., Molecular cloning of a protein serine/threonine phosphatase containing a putative regulatory tetratricopeptide repeat domain (1994) J. Biol. Chem., 269, pp. 22586-22592
  • Binart, N., Lomès, M., Rafestin-Oblin, M., Baulieu, E.E., Characterization of the human mineralocorticoid receptor expressed in baculovirus system (1991) Proc. Natl. Acad. Sci. USA, 88, pp. 10681-10685
  • Bodwell, J.E., Ortí, E., Coull, J.M., Identification of phosphorylated sites in the mouse glucocorticoid receptor (1991) J. Biol. Chem., 266, pp. 7549-7555
  • Burton, G., Galigniana, M.D., Delavallaz, S., Sodium-retaining activity of some natural and synthetic 21-deoxysteroids (1995) Mol. Pharmacol., 47, pp. 535-543
  • Caamaño, C.A., Morano, M.I., Patel, P.D., Watson, S.J., Akil, H., A bacterially expressed mineralocorticoid receptor is associated in vitro with the 90-kilodalton heat shock protein and shows typical hormone- And DNA-binding characteristics (1993) Biochemistry, 32, pp. 8589-8595
  • Chen, M.X., McPartlin, A.E., Brown, L., Chen, Y.H., Barker, H.M., Cohen, P.T., A novel human protein serine/threonine phosphatase which possesses four tetratricopeptide repeated motifs and colocalizes to the nucleus (1994) EMBO J., 13, pp. 4278-4290
  • Chen, S., Prapapanich, V., Rimerman, R.A., Honoré, B., Smith, D.F., Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70 (1996) Mol. Endocrinol., 10, pp. 682-693
  • Chinkers, M., Targeting of a distinctive protein-serine phosphatase to the protein kinase-like domain of the atrial natriuretic peptide receptor (1994) Proc. Natl. Acad. Sci. USA, 91, pp. 11075-11079
  • Cohen, P., Classification of protein-serine/threonine phosphatases: Identification and quantitation in cell extracts (1991) Methods Enzymol., 201, pp. 389-398
  • Couette, B., Lombès, M., Baulieu, E.E., Rafestin-Oblin, M.E., Aldosterone antagonists destabilize the mineralocorticoid receptor (1992) Biochem. J., 282, pp. 697-702
  • Czar, M.J., Galigniana, M.D., Silverstein, A.M., Pratt, W.B., Geldanamycin, a heat shock protein 90-binding benzoquinone ansamycin, inhibits steroid-dependent translocation of the glucocorticoid receptor from cytoplasm to the nucleus (1997) Biochemistry, 36, pp. 7776-7785
  • Denton, R.R., Koszewski, N.J., Notides, A.C., Estrogen receptor phosphorylation: Hormonal dependence and consequence on specific DNA binding (1992) J. Biol. Chem., 267, pp. 7263-7268
  • Dittmar, K.D., Demady, D.R., Stancato, L.F., Krishna, P., Pratt, W.B., Folding of the glucocorticoid receptor by the hsp90-based chaperone machinery: The role of p23 is to dynamically stabilize receptor-hsp90 heterocomplexes formed by hsp90,·p60,·hsp70 (1997) J. Biol. Chem., 272, pp. 21213-21220
  • Easom, R.A., Tarpley, J.L., Filler, N.R., Bhatt, H., Dephosphorylation and deactivation of Ca2+/calmodulin-dependent protein kinase II in βtC3-cells is mediated by Mg2+- And okadaic acid-sensitive protein phosphatases (1998) Biochem. J., 329, pp. 283-288
  • Emadian, S.M., Luttge, W.G., Effects of polyhydric and monohydric compounds on the stability of type I receptors for adrenal steroids in brain cytosol (1988) J. Neurochem., 50, pp. 1456-1460
  • Enmark, E., Gustafsson, J.A., Orphan nuclear receptors: The first eight years (1996) Mol. Endocrinol., 10, pp. 1293-1307
  • Evans, R.M., The steroid and thyroid hormone receptor superfamily (1988) Science, 240, pp. 889-895
  • Faure, R., Daussault, J.H., Effects of adenosine triphosphate and alkaline phosphatase in solubilized 3,5,3′-triiodothyronine-binding activity (1988) Endocrinology, 123, pp. 1245-1252
  • Funder, J.W., Pearce, P., Smith, R., Smith, I.A., Mineralocorticoid action: Target tissue specificity is enzyme, not receptor, mediated (1988) Science, 242, pp. 583-585
  • Galigniana, M.D., Stability study on renal type I mineralocorticoid receptor (1996) Life Sci., 59, pp. 511-521
  • Galigniana, M.D., Vicent, G.P., Burton, G., Lantos, C.P., Features of the shuttle pair 11β-hydroxyprogesterone/11-ketoprogesterone (1997) Steroids, 62, pp. 358-364
  • Grahame Hardie, D., Haystead, T.A., Sim, A.T., Use of okadaic acid to inhibit protein phosphatases in intact cells (1991) Methods Enzymol., 201, pp. 469-476
  • Hsieh, J.C., Jurutka, P.W., Nakajima, S., Phosphorylation of the vitamin D receptor by protein kinase C: Biochemical and functional evaluation of the serine 51 recognition site (1993) J. Biol. Chem., 268, pp. 15118-15126
  • Hu, J.M., Bodwell, J.E., Munck, A., Control by basal phosphorylation of cell cycle-dependent, hormone-induced glucocorticoid receptor hyperphosphorylation (1997) Mol. Endocrinol., 11, pp. 305-311
  • Hunter, T., Protein kinases and phosphatases: The ying and yang of protein phosphorylation and signaling (1995) Cell, 80, pp. 225-236
  • Johnson, J.L., Toft, D.O., Binding of p23 and hsp90 during assembly with the progesterone receptor (1995) Mol. Endocrinol., 9, pp. 670-678
  • Lin, K.H., Ashizawa, K., Cheng, S.Y., Phosphorylation stimulates the transcriptional activity of the human β1 thyroid hormone nuclear receptor (1992) Proc. Natl. Acad. Sci. USA, 89, pp. 7737-7741
  • Litswak, S.J., Gold, P.W., Whitfield, H.J., The human mineralocorticoid receptor gene promotor: Its structure and expression (1996) J. Steroid Biochem. Mol. Biol., 58, pp. 495-506
  • Lombès, M., Binart, N., Delahaye, F., Baulieu, E.E., Rafestin-Oblin, M.E., Differential intracellular localization of human mineralocorticoid receptor on binding of agonists and antagonists (1994) Biochem. J., 302, pp. 191-197
  • Luttge, W., Emadian, S., Transformation of the [3H]aldosterone-type I receptor complex to a DNA-binding species (1988) Life Sci., 43, pp. 837-843
  • MacKintosh, C., Klumpp, S., Tautomycin from the bacterium Streptomyces verticillatus: Another potent and specific inhibitor of protein phosphatases 1 and 2A (1990) FEBS Lett., 277, pp. 137-140
  • Mulkey, R.M., Endo, S., Shenollkar, S., Malenka, R.C., Involvement of a calcineurin/inhibitor 1 phosphatase cascade in hippocampal long-term depression (1994) Nature, 369, pp. 486-488
  • Nielsen, C.J., Sando, J.J., Pratt, W.B., Evidence that dephosphorylation inactivated glucocorticoid receptors (1977) Proc. Natl. Acad. Sci. USA, 74, pp. 1398-1402
  • Ortí, E., Mendel, D.B., Smith, L.I., Munck, A., Agonist-dependent phosphorylation and nuclear dephosphorylation of glucocorticoid receptors in intact cells (1989) J. Biol. Chem., 263, pp. 9728-9731
  • Ortí, E., Bodwell, J., Munck, A., Phosphorylation of steroid hormone receptors (1992) Endocr. Rev., 13, pp. 105-128
  • Ortí, E., Hu, L.M., Munck, A., Kinetics of glucocorticoid receptor in intact cells (1993) J. Biol. Chem., 268, pp. 7779-7784
  • Patel, P.D., Sherman, T.G., Goldman, D.J., Watson, S.J., Molecular cloning of a mineralocorticoid (type I) receptor complementary DNA from rat hippocampus (1989) Mol. Endocrinol., 3, pp. 1877-1885
  • Pratt, W.B., Toft, D.O., Steroid receptor interactions with heat shock protein and immunophilin chaperones (1997) Endocr. Rev., 18, pp. 306-360
  • Ragolia, L., Cherpalis, B., Srinivasan, M., Begum, N., Role of serine/threonine protein phosphatases in insulin regulation of Na+/K+-ATPase activity in cultured rat skeletal muscle cells (1997) J. Biol. Chem., 272, pp. 23653-23658
  • Reker, C.E., Lapointe, M.C., Kovacic-Milivojevic, B., Chiou, W.J.H., Vedeckis, W.V., A possible role for dephosphorylation in glucocorticoid receptor transformation (1987) J. Steroid Biochem., 26, pp. 653-665
  • Sasahara, Y., Kobayashi, T., Onodera, H., Okadaic acid suppresses neural differentiation-dependent expression of the neurofilament-L gene in P19 embryonal carcinoma cells by post-transcriptional modification (1996) J. Biol. Chem., 271, pp. 25950-25957
  • Scherrer, L.C., Dalman, F.C., Massa, E., Meshinchi, S., Pratt, W.B., Structural and functional reconstitution of the glucocorticoid receptor-hsp90 complex (1990) J. Biol. Chem., 265, pp. 21397-21400
  • Silverstein, A.M., Galigniana, M.D., Chen, M.S., Owens-Grillo, J.K., Chinkers, M., Pratt, W.B., Protein Phosphatase 5 is a major component of glucocorticoid receptor-hsp90 complexes with properties of an FK506 binding immunophilin (1997) J. Biol. Chem., 272, pp. 16224-16230
  • Smith, D.F., Schowalter, D.B., Kost, S.L., Toft, D.O., Reconstitution of progesterone receptor with heat shock proteins (1990) Mol. Endocrinol., 4, pp. 1704-1711
  • Smith, D.F., Stensgard, B.A., Welch, W.J., Toft, D.O., Assembly of progesterone receptor with heat shock proteins and receptor activation are ATP mediated events (1992) J. Biol. Chem., 269, pp. 1350-1356
  • Smith, D.F., Whitesell, L., Nair, S.C., Chen, S., Prapapanich, V., Rimerman, R.A., Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent (1995) Mol. Cell. Biol., 15, pp. 6804-6812
  • Takimoto, G.S., Hovland, A.R., Tasset, D.M., Melville, M.Y., Tung, L., Horwitz, K.B., Role of phosphorylation on DNA binding and transcriptional functions of human progesterone receptor (1996) J. Biol. Chem., 271, pp. 13308-13316
  • Trapp, T., Holsboer, F., Ligand-induced conformational changes in the mineralocorticoid receptor analyzed by protease mapping (1995) BBRC, 215, pp. 286-291
  • Veleiro, A.S., Nevado, M.V., Monteserín, M.C., Burton, G., Syntheses of 21-hydroxy-11,19-oxidopregnan-4-ene-3,20-dione and 21-hydroxy-6,19-oxidopregnan-4-ene-3,20-dione (1996) Steroids, 60, pp. 268-271
  • Vicent, G.P., Monteserín, M.C., Veleiro, A.S., Burton, G., Lantos, C.P., Galigniana, M.D., 21-Hydroxy-6,19-oxidoprogesterone: A novel synthetic steroid with specific antiglucocorticoid properties in the rat (1997) Mol. Pharmacol., 52, pp. 749-753
  • Webster, J.C., Jewell, C.M., Bodwell, J.E., Munck, A., Sar, M., Cidlowski, J.A., Mouse glucocorticoid receptor phosphorylation status influences multiple functions of the receptor protein (1997) J. Biol. Chem., 272, pp. 9287-9293
  • Weigel, N.L., Carter, N.H., Schrader, W.T., O.'. Malley, B.W., Chicken progesterone receptor is phosphorylated by a DNA-dependent protein kinase during in vitro transcription assays (1992) Mol. Endocrinol., 6, pp. 8-14
  • Whitesell, L., Cook, P., Stable and specific binding of hsp90 by geldanamycin disrupts glucocorticoid receptor function in intact cells (1996) Mol. Endocrinol., 10, pp. 705-712
  • Zhang, Y., Beck, C.A., Poletti, A., Edwards, D.P., Weigel, N.L., Identification of a group of Ser-Pro motif hormone-inducible phosphorylation sites in the human progesterone receptor (1995) Mol. Endocrinol., 9, pp. 1029-1040

Citas:

---------- APA ----------
Piwien-Pilipuk, G. & Galigniana, M.D. (1998) . Tautomycin inhibits phosphatase-dependent transformation of the rat kidney mineralocorticoid receptor. Molecular and Cellular Endocrinology, 144(1-2), 119-130.
http://dx.doi.org/10.1016/S0303-7207(98)00142-7
---------- CHICAGO ----------
Piwien-Pilipuk, G., Galigniana, M.D. "Tautomycin inhibits phosphatase-dependent transformation of the rat kidney mineralocorticoid receptor" . Molecular and Cellular Endocrinology 144, no. 1-2 (1998) : 119-130.
http://dx.doi.org/10.1016/S0303-7207(98)00142-7
---------- MLA ----------
Piwien-Pilipuk, G., Galigniana, M.D. "Tautomycin inhibits phosphatase-dependent transformation of the rat kidney mineralocorticoid receptor" . Molecular and Cellular Endocrinology, vol. 144, no. 1-2, 1998, pp. 119-130.
http://dx.doi.org/10.1016/S0303-7207(98)00142-7
---------- VANCOUVER ----------
Piwien-Pilipuk, G., Galigniana, M.D. Tautomycin inhibits phosphatase-dependent transformation of the rat kidney mineralocorticoid receptor. Mol. Cell. Endocrinol. 1998;144(1-2):119-130.
http://dx.doi.org/10.1016/S0303-7207(98)00142-7