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Volumn 4, Issue 1, 2003, Pages 46-56

Nongenomic actions of steroid hormones

Author keywords

[No Author keywords available]

Indexed keywords

17ALPHA ESTRADIOL; 4 AMINOBUTYRIC ACID; ALDOSTERONE; ANTIESTROGEN; CALCIUM ION; COLECALCIFEROL; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN BINDING PROTEIN; CYCLOHEXIMIDE; DACTINOMYCIN; DNA; ESTRADIOL; ESTROGEN; FULVESTRANT; G PROTEIN COUPLED RECEPTOR; GLUCOCORTICOID; LIOTHYRONINE; MITOGEN ACTIVATED PROTEIN KINASE; N METHYL DEXTRO ASPARTIC ACID; NEUROSTEROID; NITRIC OXIDE SYNTHASE; PHOSPHATIDYLINOSITOL 3 KINASE; PROGESTERONE; PROTEIN KINASE C; STEROID; STEROID RECEPTOR; THYROID HORMONE; THYROXINE; VITAMIN D;

EID: 0037224484     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm1009     Document Type: Review
Times cited : (740)

References (123)
  • 1
    • 84995910795 scopus 로고
    • Correlations between the chemical structure and the pharmacological actions of the steroids
    • Selye, H. Correlations between the chemical structure and the pharmacological actions of the steroids. Endocrinology 30, 437-453 (1942). The first detailed report of rapid steroid action in addition to a delayed action - a fine example of careful scientific work that was unbiased by preconceived ideas.
    • (1942) Endocrinology , vol.30 , pp. 437-453
    • Selye, H.1
  • 2
    • 75449139797 scopus 로고
    • Klinisch-experimentelle untersuchungen über den einfluβ von aldosteron auf hämodynamik und gerinnung
    • Klein, K. & Henk, W. Klinisch-experimentelle Untersuchungen über den Einfluβ von Aldosteron auf Hämodynamik und Gerinnung. Z. Kreisl. Forsch. 52, 40-53 (1963).
    • (1963) Z. Kreisl. Forsch. , vol.52 , pp. 40-53
    • Klein, K.1    Henk, W.2
  • 3
    • 0001239914 scopus 로고
    • Retardation of sodium exchange in dog erythrocytes by physiological concentrations of aldosterene, in vitro
    • Spach, C. & Streeten, D. H. Retardation of sodium exchange in dog erythrocytes by physiological concentrations of aldosterene, in vitro. J. Clin. Invest. 43, 217-227 (1964).
    • (1964) J. Clin. Invest. , vol.43 , pp. 217-227
    • Spach, C.1    Streeten, D.H.2
  • 4
    • 0024545638 scopus 로고
    • Gene regulation by steroid hormones
    • Beato, M. Gene regulation by steroid hormones. Cell 56, 335-344 (1989). An excellent account of the direct genomic action of classical steroid receptors.
    • (1989) Cell , vol.56 , pp. 335-344
    • Beato, M.1
  • 5
    • 0037662032 scopus 로고    scopus 로고
    • Nongenomic steroid action: Controversies, questions and answers?
    • in the press
    • Losel, R. M. et al. Nongenomic steroid action: controversies, questions and answers? Physiol. Rev. (in the press).
    • Physiol. Rev.
    • Losel, R.M.1
  • 6
    • 0029900104 scopus 로고    scopus 로고
    • Purification and partial sequencing of high affinity progesterone-binding site(s) from porcine liver membranes
    • Meyer, C., Schmid, R., Scriba, P. C. & Wehling, M. Purification and partial sequencing of high affinity progesterone-binding site(s) from porcine liver membranes. Eur. J. Biochem. 239. 726-731 (1996).
    • (1996) Eur. J. Biochem. , vol.239 , pp. 726-731
    • Meyer, C.1    Schmid, R.2    Scriba, P.C.3    Wehling, M.4
  • 7
    • 0034457060 scopus 로고    scopus 로고
    • Mannheim classification of nongenomically initiated (rapid) steroid action(s)
    • Falkenstein, E., Norman, A. W. & Wehling, M. Mannheim classification of nongenomically initiated (rapid) steroid action(s). J Clin. Endocrinol Metab. 85, 2072-2075 (2000). The classification scheme outlined in this work should enable nongenomic responses to be categorized.
    • (2000) J Clin. Endocrinol Metab. , vol.85 , pp. 2072-2075
    • Falkenstein, E.1    Norman, A.W.2    Wehling, M.3
  • 8
    • 0015076873 scopus 로고
    • Cytoplasmic control of nuclear behavior during meiotic maturation of frog oocytes
    • Masui, Y. & Markert, C. L. Cytoplasmic control of nuclear behavior during meiotic maturation of frog oocytes. J. Exp. Zool. 177, 129-145 (1971).
    • (1971) J. Exp. Zool. , vol.177 , pp. 129-145
    • Masui, Y.1    Markert, C.L.2
  • 9
    • 0019724780 scopus 로고
    • Progesterone inhibits membrane-bound adenylate cyclase in Xenopus laevis oocytes
    • Finidori-Lepicard, J., Schorderet-Slatkine, S., Hanoune, J. & Baulieu, E. E. Progesterone inhibits membrane-bound adenylate cyclase in Xenopus laevis oocytes. Nature 292, 255-257 (1981).
    • (1981) Nature , vol.292 , pp. 255-257
    • Finidori-Lepicard, J.1    Schorderet-Slatkine, S.2    Hanoune, J.3    Baulieu, E.E.4
  • 10
    • 0019860035 scopus 로고
    • Progesterone inhibits adenylate cyclase in Xenopus oocytes. Action on the guanine nucleotide regulatory protein
    • Sadler, S. E. & Maller, J. L. Progesterone inhibits adenylate cyclase in Xenopus oocytes. Action on the guanine nucleotide regulatory protein. J. Biol. Chem. 256, 6368-6373 (1981).
    • (1981) J. Biol. Chem. , vol.256 , pp. 6368-6373
    • Sadler, S.E.1    Maller, J.L.2
  • 11
    • 0017340457 scopus 로고
    • Progesterone-stimulated meiotic cell division in Xenopus oocytes. Induction by regulatory subunit and inhibition by catalytic subunit of adenosine 3′:5′-monophosphate-dependent protein kinase
    • Maller, J. L. & Krebs, E. G. Progesterone-stimulated meiotic cell division in Xenopus oocytes. Induction by regulatory subunit and inhibition by catalytic subunit of adenosine 3′:5′-monophosphate-dependent protein kinase. J. Biol. Chem. 252, 1712-1718 (1977).
    • (1977) J. Biol. Chem. , vol.252 , pp. 1712-1718
    • Maller, J.L.1    Krebs, E.G.2
  • 12
    • 0035813093 scopus 로고    scopus 로고
    • The classical progesterone receptor associates with p42 MAPK and is involved in phosphatidylinositol 3-kinase signaling in Xenopus oocytes
    • Bagowski, C. P., Myers, J. W. & Ferrell, J. E. Jr. The classical progesterone receptor associates with p42 MAPK and is involved in phosphatidylinositol 3-kinase signaling in Xenopus oocytes. J. Biol. Chem. 276, 37708-37714 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 37708-37714
    • Bagowski, C.P.1    Myers, J.W.2    Ferrell J.E., Jr.3
  • 13
    • 0024384140 scopus 로고
    • Steroid induced exocytosis: The human sperm acrosome reaction
    • Osman, R. A., Andria, M. L., Jones, A. D. & Meizel, S. Steroid induced exocytosis: the human sperm acrosome reaction. Biochem. Biophys. Res. Commun. 160, 828-833 (1989). This study reports on the identification of progesterone as an acrosome-reaction-inducing compound present in human follicular fluid.
    • (1989) Biochem. Biophys. Res. Commun. , vol.160 , pp. 828-833
    • Osman, R.A.1    Andria, M.L.2    Jones, A.D.3    Meizel, S.4
  • 14
    • 0025908271 scopus 로고
    • Progesterone acts at the plasma membrane of human sperm
    • , Meizel, S. & Turner, K. O. Progesterone acts at the plasma membrane of human sperm. Mol. Cell. Endocrinol. 77, R1-R5 (1991).
    • (1991) Mol. Cell. Endocrinol. , vol.77
    • Meizel, S.1    Turner, K.O.2
  • 15
    • 0029159997 scopus 로고
    • Undetectable expression of genomic progesterone receptor in human spermatozoa
    • Castilla, J. A. et al. Undetectable expression of genomic progesterone receptor in human spermatozoa. Hum. Reprod. 10, 1757-1760 (1995).
    • (1995) Hum. Reprod. , vol.10 , pp. 1757-1760
    • Castilla, J.A.1
  • 16
    • 0031732318 scopus 로고    scopus 로고
    • Identification and characterization of functional nongenomic progesterone receptors on human sperm membrane
    • Luconi, M. et al. Identification and characterization of functional nongenomic progesterone receptors on human sperm membrane. J. Clin. Endocrinol. Metab. 83, 877-885 (1998).
    • (1998) J. Clin. Endocrinol. Metab. , vol.83 , pp. 877-885
    • Luconi, M.1
  • 17
    • 0029869830 scopus 로고    scopus 로고
    • Human sperm plasma membrane progesterone receptor(s) and the acrosome reaction
    • Sabeur, K. Edwards, D. P. & Meizel, S. Human sperm plasma membrane progesterone receptor(s) and the acrosome reaction. Biol. Reprod. 54, 993-1001 (1996).
    • (1996) Biol. Reprod. , vol.54 , pp. 993-1001
    • Sabeur, K.1    Edwards, D.P.2    Meizel, S.3
  • 18
    • 0034083916 scopus 로고    scopus 로고
    • Detection of progesterone receptor transcript in human spermatozoa
    • Sachdeva, G., Shah, C. A., Kholkute, S. D. & Puri, C. P. Detection of progesterone receptor transcript in human spermatozoa. Biol Reprod. 62, 1610-1614 (2000).
    • (2000) Biol Reprod. , vol.62 , pp. 1610-1614
    • Sachdeva, G.1    Shah, C.A.2    Kholkute, S.D.3    Puri, C.P.4
  • 19
    • 0029871761 scopus 로고    scopus 로고
    • Unusual steroid specificity of the cell surface progesterone receptor on human sperm
    • Blackmore, P. F., Fisher, J. F., Spilman, C. H. & Bleasdale, J. E. Unusual steroid specificity of the cell surface progesterone receptor on human sperm. Mol. Pharmacol. 49, 727-739 (1996). The differences in steroid selectivity between the classical and the nonclassical sperm progesterone receptors have been studied with a large set of steroids.
    • (1996) Mol. Pharmacol. , vol.49 , pp. 727-739
    • Blackmore, P.F.1    Fisher, J.F.2    Spilman, C.H.3    Bleasdale, J.E.4
  • 20
    • 0026005122 scopus 로고
    • Cell surface-binding sites for progesterone mediate calcium uptake in human sperm
    • Blackmore, P. F., Neulen, J., Lattanzio, F., & Beebe, S. J. Cell surface-binding sites for progesterone mediate calcium uptake in human sperm. J. Biol. Chem. 268, 18655-18659 (1991).
    • (1991) J. Biol. Chem. , vol.268 , pp. 18655-18659
    • Blackmore, P.F.1    Neulen, J.2    Lattanzio, F.3    Beebe, S.J.4
  • 21
    • 0025943491 scopus 로고
    • Intracellular calcium accumulation and responsiveness to progesterone in capacitating human spermatozoa
    • Baldi, E. et al. Intracellular calcium accumulation and responsiveness to progesterone in capacitating human spermatozoa. J. Androl. 12, 323-330 (1991).
    • (1991) J. Androl. , vol.12 , pp. 323-330
    • Baldi, E.1
  • 23
    • 0026318851 scopus 로고
    • Cell surface localization of a novel non-genomic progesterone receptor on the head of human sperm
    • Blackmore, P. F. & Lattanzio, F. A. Cell surface localization of a novel non-genomic progesterone receptor on the head of human sperm. Biochem Biophys. Res. Commun. 181, 331-336 (1991).
    • (1991) Biochem Biophys. Res. Commun. , vol.181 , pp. 331-336
    • Blackmore, P.F.1    Lattanzio, F.A.2
  • 24
    • 0033305449 scopus 로고    scopus 로고
    • 2+-fluxes in sperm
    • 2+-fluxes in sperm. Endocrinology 140, 5999-6002 (1999).
    • (1999) Endocrinology , vol.140 , pp. 5999-6002
    • Falkenstein, E.1
  • 25
    • 0030569560 scopus 로고    scopus 로고
    • Full-length cDNA sequence of a progesterone membrane-binding protein from porcine vascular smooth muscle cells
    • Falkenstein, E., Meyer, C., Eisen, C., Scriba, P. C. & Wehling, M. Full-length cDNA sequence of a progesterone membrane-binding protein from porcine vascular smooth muscle cells. Biochem. Biophys. Res. Commun. 229, 86-89 (1996).
    • (1996) Biochem. Biophys. Res. Commun. , vol.229 , pp. 86-89
    • Falkenstein, E.1    Meyer, C.2    Eisen, C.3    Scriba, P.C.4    Wehling, M.5
  • 26
    • 0033741196 scopus 로고    scopus 로고
    • A membrane-associated progesterone-binding protein, 25-Dx, is regulated by progesterone in brain regions involved in female reproductive behaviors
    • Krebs, C. J., Jarvis, E. D., Chan, J., Lydon, J. P., Ogawa, S. & Pfaff, D. W. A membrane-associated progesterone-binding protein, 25-Dx, is regulated by progesterone in brain regions involved in female reproductive behaviors. Proc. Natl Acad. Sci. USA 97, 12816-12821 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12816-12821
    • Krebs, C.J.1    Jarvis, E.D.2    Chan, J.3    Lydon, J.P.4    Ogawa, S.5    Pfaff, D.W.6
  • 27
    • 0034852802 scopus 로고    scopus 로고
    • Progesterone receptor contains a proline-rich motif that directly interacts with SH3 domains and activates c-Src family tyrosine kinases
    • Boonyaratanakornkit, V. et al. Progesterone receptor contains a proline-rich motif that directly interacts with SH3 domains and activates c-Src family tyrosine kinases. Mol. Cell 8, 269-280 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 269-280
    • Boonyaratanakornkit, V.1
  • 28
    • 0016436966 scopus 로고
    • Endometrial cell calcium and oestrogen action
    • Pietras, R. J. & Szego, C. M. Endometrial cell calcium and oestrogen action. Nature 253, 357-359 (1975).
    • (1975) Nature , vol.253 , pp. 357-359
    • Pietras, R.J.1    Szego, C.M.2
  • 30
    • 0026788056 scopus 로고
    • A new, nongenomic estrogen action: The rapid release of intracellular calcium
    • Morley, P., Whitfield, J. F., Vanderhyden, B. C., Tsang, B. K. & Schwartz, J. L. A new, nongenomic estrogen action: the rapid release of intracellular calcium. Endocrinology 131, 1305-1312 (1992).
    • (1992) Endocrinology , vol.131 , pp. 1305-1312
    • Morley, P.1    Whitfield, J.F.2    Vanderhyden, B.C.3    Tsang, B.K.4    Schwartz, J.L.5
  • 31
    • 0028986329 scopus 로고
    • Nongenomic effects of 17β-estradiol on maturing human occytes: Relationship to oocyte developmental potential
    • Tesarik, J. & Mendoza, C. Nongenomic effects of 17β-estradiol on maturing human occytes: relationship to oocyte developmental potential. J. Clin. Endocrinol. Metab. 80, 1438-1443 (1995).
    • (1995) J. Clin. Endocrinol. Metab. , vol.80 , pp. 1438-1443
    • Tesarik, J.1    Mendoza, C.2
  • 32
    • 0017354142 scopus 로고
    • Specific binding sites for oestrogen at the outer surfaces of isolated endometrial cells
    • Pietras, R. J. & Szego, C. M. Specific binding sites for oestrogen at the outer surfaces of isolated endometrial cells. Nature 265, 69-72 (1977).
    • (1977) Nature , vol.265 , pp. 69-72
    • Pietras, R.J.1    Szego, C.M.2
  • 33
    • 0028154102 scopus 로고
    • Ethinyl estradiol acutely attenuates abnormal coronary vasomotor responses to acetylcholine in postmenopausal women
    • Reis, S. E. et al. Ethinyl estradiol acutely attenuates abnormal coronary vasomotor responses to acetylcholine in postmenopausal women. Circulation 89, 52-60 (1994).
    • (1994) Circulation , vol.89 , pp. 52-60
    • Reis, S.E.1
  • 34
    • 0028178237 scopus 로고
    • Endothelium-independent relaxation by 17-α-estradiol of pig coronary arteries
    • Salas, E. et al. Endothelium-independent relaxation by 17-α-estradiol of pig coronary arteries. Eur. J. Pharmacol. 258, 47-55 (1994).
    • (1994) Eur. J. Pharmacol. , vol.258 , pp. 47-55
    • Salas, E.1
  • 35
    • 0032898708 scopus 로고    scopus 로고
    • Rapid activation of endothelial nitric oxide synthase by estrogen
    • Shaul, P. W. Rapid activation of endothelial nitric oxide synthase by estrogen. Steroids 64, 28-34 (1999). An overview of the essential properties of NOS activation by oestradiol.
    • (1999) Steroids , vol.64 , pp. 28-34
    • Shaul, P.W.1
  • 37
    • 0032589745 scopus 로고    scopus 로고
    • Estrogen receptor α mediates the nongenomic activation of endothelial nitric oxide synthase by estrogen
    • Chen, Z. et al. Estrogen receptor α mediates the nongenomic activation of endothelial nitric oxide synthase by estrogen. J. Clin. Invest. 103, 401-406 (1999).
    • (1999) J. Clin. Invest. , vol.103 , pp. 401-406
    • Chen, Z.1
  • 38
    • 0034644608 scopus 로고    scopus 로고
    • Membrane estrogen receptor engagement activates endothelial nitric oxide synthase via the PI3-kinase-Akt pathway in human endothelial cells
    • Haynes, M. P. et al. Membrane estrogen receptor engagement activates endothelial nitric oxide synthase via the PI3-kinase-Akt pathway in human endothelial cells. Circ. Res. 87, 677-682 (2000).
    • (2000) Circ. Res. , vol.87 , pp. 677-682
    • Haynes, M.P.1
  • 39
    • 0035920110 scopus 로고    scopus 로고
    • Plasma membrane estrogen receptors are coupled to endothelial nitric-oxide synthase through Gα(i)
    • Wyckoff, M. H. et al. Plasma membrane estrogen receptors are coupled to endothelial nitric-oxide synthase through Gα(i). J. Biol. Chem. 276, 27071-27076 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 27071-27076
    • Wyckoff, M.H.1
  • 40
    • 0034705168 scopus 로고    scopus 로고
    • Human vascular endothelial cells contain membrane binding sites for estradiol, which mediate rapid intracellular signaling
    • Russell, K. S., Haynes, M. P., Shina, D., Clensme, E. & Bender, J. R. Human vascular endothelial cells contain membrane binding sites for estradiol, which mediate rapid intracellular signaling. Proc. Natl Acad. Sci. USA 97, 5930-5935 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5930-5935
    • Russell, K.S.1    Haynes, M.P.2    Shina, D.3    Clensme, E.4    Bender, J.R.5
  • 41
    • 0036139164 scopus 로고    scopus 로고
    • ERs associate with and regulate the production of caveolin: Implications for signaling and cellular actions
    • Rasandi, M., Oh, P., Pedram, A., Schnitzer, J. & Levin, E. R. ERs associate with and regulate the production of caveolin: implications for signaling and cellular actions. Mol. Endocrinol. 16, 100-115 (2002).
    • (2002) Mol. Endocrinol. , vol.16 , pp. 100-115
    • Rasandi, M.1    Oh, P.2    Pedram, A.3    Schnitzer, J.4    Levin, E.R.5
  • 42
    • 0034711335 scopus 로고    scopus 로고
    • Estrogen receptor α and endothelial nitric oxide synthase are organized into a functional signaling module in caveclae
    • Chambliss, K. L. et al. Estrogen receptor α and endothelial nitric oxide synthase are organized into a functional signaling module in caveclae. Circ. Res. 87, E44-E52 (2000).
    • (2000) Circ. Res. , vol.87
    • Chambliss, K.L.1
  • 43
    • 0032907868 scopus 로고    scopus 로고
    • Novel mechanisms of estrogen action in the brain: New players in an old story
    • Toran-Allerand, C. D., Singh, M. & Setalo, G. Jr. Novel mechanisms of estrogen action in the brain: new players in an old story. Front. Neuroendocrinol. 20, 97-121 (1999).
    • (1999) Front. Neuroendocrinol. , vol.20 , pp. 97-121
    • Toran-Allerand, C.D.1    Singh, M.2    Setalo G., Jr.3
  • 45
    • 0036225088 scopus 로고    scopus 로고
    • Estrogen-binding sites and their functional capacity in estrogen receptor double knockout mouse brain
    • Shughrue, P. J., Askew, G. R. Dellovade, T. L. & Merchenthaler, I. Estrogen-binding sites and their functional capacity in estrogen receptor double knockout mouse brain. Endocrinology 143, 1643-1650 (2002).
    • (2002) Endocrinology , vol.143 , pp. 1643-1650
    • Shughrue, P.J.1    Askew, G.R.2    Dellovade, T.L.3    Merchenthaler, I.4
  • 46
    • 0037184912 scopus 로고    scopus 로고
    • Integration of the non-genomic and genomic actions of estrogen: Membrane initiated signaling by steroid (MISS) to transcription and cell biology
    • in the press
    • Pedram, A., Razandi, M., Aitkenhead, M., Hughes, C. C. & Levin, E. R. Integration of the non-genomic and genomic actions of estrogen: membrane initiated signaling by steroid (MISS) to transcription and cell biology. J. Biol Chem. (in the press).
    • J. Biol Chem.
    • Pedram, A.1    Razandi, M.2    Aitkenhead, M.3    Hughes, C.C.4    Levin, E.R.5
  • 47
    • 0023227668 scopus 로고
    • Effect of aldosterone on sodium and potassium concentrations in human mononuclear leukocytes
    • Wehling, M., Armanini, D., Strasser, T. & Weber, P. C. Effect of aldosterone on sodium and potassium concentrations in human mononuclear leukocytes. Am. J. Physiol. 252, E505-E508 (1987).
    • (1987) Am. J. Physiol. , vol.252
    • Wehling, M.1    Armanini, D.2    Strasser, T.3    Weber, P.C.4
  • 48
    • 0025890009 scopus 로고
    • Rapid effects of mineralocorticoids on sodium-proton exchanger: Genomic or nongenomic pathway?
    • Wehling, M., Käsmayr, J. & Theisen, K. Rapid effects of mineralocorticoids on sodium-proton exchanger: genomic or nongenomic pathway? Am. J. Physiol. 260, E719-E726 (1991).
    • (1991) Am. J. Physiol. , vol.260
    • Wehling, M.1    Käsmayr, J.2    Theisen, K.3
  • 49
    • 0024461860 scopus 로고
    • Volume regulation of human lymphocytes by aldosterone in isotonic media
    • Wehling, M., Kuhls, S. & Armanini, D. Volume regulation of human lymphocytes by aldosterone in isotonic media. Am. J. Physiol. 257, E170-E174 (1989).
    • (1989) Am. J. Physiol. , vol.257
    • Wehling, M.1    Kuhls, S.2    Armanini, D.3
  • 50
    • 0027960069 scopus 로고
    • Rapid effects of aldosterone on free intracellular calcium in vascular smooth muscle and endothelial cells: Subcellular localization of calcium elevations by single cell imaging
    • Wehling, M., Ulsenheimer, A., Schneider, M., Neylon, C. & Christ, M. Rapid effects of aldosterone on free intracellular calcium in vascular smooth muscle and endothelial cells: subcellular localization of calcium elevations by single cell imaging. Biochem. Biophys. Res. Commun. 204, 475-481 (1994).
    • (1994) Biochem. Biophys. Res. Commun. , vol.204 , pp. 475-481
    • Wehling, M.1    Ulsenheimer, A.2    Schneider, M.3    Neylon, C.4    Christ, M.5
  • 51
    • 0031000789 scopus 로고    scopus 로고
    • Specific, nongenomic actions of steroid hormones
    • Wehling, M. Specific, nongenomic actions of steroid hormones. Annu. Rev. Physiol. 59, 365-393 (1997).
    • (1997) Annu. Rev. Physiol. , vol.59 , pp. 365-393
    • Wehling, M.1
  • 52
    • 0033539910 scopus 로고    scopus 로고
    • Rapid nongenomic effects of aldosterone in mineralcoorticoid-receptor-knockout mice
    • Haseroth, K. et al. Rapid nongenomic effects of aldosterone in mineralcoorticoid-receptor-knockout mice. Biochem. Biophys. Res. Commun. 266, 257-261 (1999).
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 257-261
    • Haseroth, K.1
  • 53
    • 0033625558 scopus 로고    scopus 로고
    • Role of 11β-hydroxysteroid dehydrogenase in nongenomic aldosterone effects in human arteries
    • Alzamora, R., Michea, L. & Marusic, E. T. Role of 11β-hydroxysteroid dehydrogenase in nongenomic aldosterone effects in human arteries. Hypertension 35, 1099-1104 (2000).
    • (2000) Hypertension , vol.35 , pp. 1099-1104
    • Alzamora, R.1    Michea, L.2    Marusic, E.T.3
  • 55
    • 0033854046 scopus 로고    scopus 로고
    • Aldosterone- and testosterone-mediated intracellular calcium response in skeletal muscle cell cultures
    • Estrada, M., Liberona, J. L., Miranda, M. & Jaimovich, E. Aldosterone- and testosterone-mediated intracellular calcium response in skeletal muscle cell cultures. Am. J. Physiol. Endocrinol. Metab. 279, E132-E139 (2000).
    • (2000) Am. J. Physiol. Endocrinol. Metab. , vol.279
    • Estrada, M.1    Liberona, J.L.2    Miranda, M.3    Jaimovich, E.4
  • 56
    • 0034074476 scopus 로고    scopus 로고
    • 2+ in M-1 cortical collecting duct cells
    • 2+ in M-1 cortical collecting duct cells. Kidney Int. 57, 1395-1403 (2000).
    • (2000) Kidney Int. , vol.57 , pp. 1395-1403
    • Harvey, B.J.1    Higgins, M.2
  • 57
    • 0032928841 scopus 로고    scopus 로고
    • Aldosterone and nuclear signaling in kidney
    • Oberleithner, H. Aldosterone and nuclear signaling in kidney. Steroids 64, 42-50 (1999).
    • (1999) Steroids , vol.64 , pp. 42-50
    • Oberleithner, H.1
  • 58
    • 0036330326 scopus 로고    scopus 로고
    • Rapid effects of aldosterone and spironolactone in the isolated working rat heart
    • Barbato, J. C., Mulrow, P. J., Shapiro, J. I. & Franco-Saenz, R. Rapid effects of aldosterone and spironolactone in the isolated working rat heart. Hypertension 40, 130-135 (2002). In this paper, aldosterone and spironolactone are shown to rapidly modulate cardiac function, which might have significance for cardiac diseases.
    • (2002) Hypertension , vol.40 , pp. 130-135
    • Barbato, J.C.1    Mulrow, P.J.2    Shapiro, J.I.3    Franco-Saenz, R.4
  • 59
    • 0025735847 scopus 로고
    • A corticosteroid receptor in neuronal membranes
    • Orchinik, M., Murray, T. F. & Moore, F. L. A corticosteroid receptor in neuronal membranes. Science 252, 1848-1851 (1991).
    • (1991) Science , vol.252 , pp. 1848-1851
    • Orchinik, M.1    Murray, T.F.2    Moore, F.L.3
  • 60
    • 84989656751 scopus 로고
    • Amphibian model system for problems in behavioral neuroendocrinology
    • Moore, F. L. Amphibian model system for problems in behavioral neuroendocrinology. J. Exp. Zool. Suppl. 4, 157-158 (1990).
    • (1990) J. Exp. Zool. Suppl. , vol.4 , pp. 157-158
    • Moore, F.L.1
  • 61
    • 0034455585 scopus 로고    scopus 로고
    • A subset of κ opioid ligands bind to the membrane glucocorticoid receptor in an amphibian brain
    • Evans, S. J., Searcy, B. T. & Moore, F. L. A subset of κ opioid ligands bind to the membrane glucocorticoid receptor in an amphibian brain. Endocrinology 141, 2294-2300 (2000).
    • (2000) Endocrinology , vol.141 , pp. 2294-2300
    • Evans, S.J.1    Searcy, B.T.2    Moore, F.L.3
  • 62
    • 0034176552 scopus 로고    scopus 로고
    • Partial purification and biochemical characterization of a membrane glucocorticoid receptor from an amphibian brain
    • Evans, S. J., Murray, T. F. & Moore, F. L. Partial purification and biochemical characterization of a membrane glucocorticoid receptor from an amphibian brain. J. Steroid Biochem. Mol. Biol. 72, 209-221 (2000).
    • (2000) J. Steroid Biochem. Mol. Biol. , vol.72 , pp. 209-221
    • Evans, S.J.1    Murray, T.F.2    Moore, F.L.3
  • 63
    • 0033638251 scopus 로고    scopus 로고
    • Rapid non-genomic feedback effects of glucocorticoids on CRF-induced ACTH secretion in rats
    • Hinz, B. & Hirschelmann, R. Rapid non-genomic feedback effects of glucocorticoids on CRF-induced ACTH secretion in rats. Pharm. Res. 17, 1273-1277 (2000).
    • (2000) Pharm. Res. , vol.17 , pp. 1273-1277
    • Hinz, B.1    Hirschelmann, R.2
  • 64
    • 0034177660 scopus 로고    scopus 로고
    • Bioenergetics of immune functions: Fundamental and therapeutic aspects
    • Buttgereit, F., Burmester, G. R. & Brand, M. D. Bioenergetics of immune functions: fundamental and therapeutic aspects. Immunol. Today 21, 192-199 (2000).
    • (2000) Immunol. Today , vol.21 , pp. 192-199
    • Buttgereit, F.1    Burmester, G.R.2    Brand, M.D.3
  • 65
    • 0023234403 scopus 로고
    • Glucocorticoid receptor-like antigen in lymphoma cell membranes: Correlation to cell lysis
    • Gametchu, B. Glucocorticoid receptor-like antigen in lymphoma cell membranes: correlation to cell lysis. Science 236, 456-461 (1987).
    • (1987) Science , vol.236 , pp. 456-461
    • Gametchu, B.1
  • 66
    • 0027436146 scopus 로고
    • Use of receptor antibodies to demonstrate membrane glucocorticoid receptor in cells from human leukemic patients
    • Gametchu, B., Watson, C. S. & Wu, S. Use of receptor antibodies to demonstrate membrane glucocorticoid receptor in cells from human leukemic patients. FASEB J. 7, 1283-1292 (1993).
    • (1993) FASEB J. , vol.7 , pp. 1283-1292
    • Gametchu, B.1    Watson, C.S.2    Wu, S.3
  • 67
    • 0035022926 scopus 로고    scopus 로고
    • Membrane estrogen and glucocorticoid receptors - Implications for hormonal control of immune function and autoimmunity
    • Watson, C. S. & Gametchu, B. Membrane estrogen and glucocorticoid receptors - implications for hormonal control of immune function and autoimmunity. Int. Immunopharmacol. 1, 1049-1063 (2001).
    • (2001) Int. Immunopharmacol. , vol.1 , pp. 1049-1063
    • Watson, C.S.1    Gametchu, B.2
  • 68
    • 0033566281 scopus 로고    scopus 로고
    • Equivalent doses and relative drug potencies for non-genomic glucocorticoid effects: A novel glucocorticoid hierarchy
    • Buttgereit, F., Brand, M. D. & Burmester, G. R. Equivalent doses and relative drug potencies for non-genomic glucocorticoid effects: a novel glucocorticoid hierarchy. Biochem. Pharmacol. 58, 363-368 (1999).
    • (1999) Biochem. Pharmacol. , vol.58 , pp. 363-368
    • Buttgereit, F.1    Brand, M.D.2    Burmester, G.R.3
  • 69
    • 0036108564 scopus 로고    scopus 로고
    • Acute cardiovascular protective effects of corticosteroids are mediated by nontranscriptional activation of endothelial nitric oxide synthase
    • Hafezi-Moghadam, A. et al. Acute cardiovascular protective effects of corticosteroids are mediated by nontranscriptional activation of endothelial nitric oxide synthase. Nature Med 8, 473-479 (2002).
    • (2002) Nature Med. , vol.8 , pp. 473-479
    • Hafezi-Moghadam, A.1
  • 71
    • 0027213820 scopus 로고
    • 3
    • 3. J. Biol. Chem. 268, 20022-20030 (1993). This is the first description of a selective antagonist for nongenomic vitamin D responses.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20022-20030
    • Norman, A.W.1
  • 73
    • 0031942938 scopus 로고    scopus 로고
    • 3 signal response pathways in osteoblasts: Cross-talk between genomic and membrane-initiated pathways
    • 3 signal response pathways in osteoblasts: cross-talk between genomic and membrane-initiated pathways. Am. J. Kidney Dis 31, 729-742 (1998).
    • (1998) Am. J. Kidney Dis. , vol.31 , pp. 729-742
    • Farach-Carson, M.C.1    Ridall, A.L.2
  • 74
    • 0035342720 scopus 로고    scopus 로고
    • 3 act as agonists for two different receptors in the vitamin D endocrine system to mediate genomic and rapid responses
    • 3 act as agonists for two different receptors in the vitamin D endocrine system to mediate genomic and rapid responses. Steroids 66, 147-158 (2001).
    • (2001) Steroids , vol.66 , pp. 147-158
    • Norman, A.W.1
  • 75
    • 0030762823 scopus 로고    scopus 로고
    • 3 regulate chondrocyte proliferation and proteoglycan production as well as protein kinase C through a nongenomic pathway
    • 3 regulate chondrocyte proliferation and proteoglycan production as well as protein kinase C through a nongenomic pathway. J. Cell Biochem. 66, 457-470 (1997).
    • (1997) J. Cell Biochem. , vol.66 , pp. 457-470
    • Boyan, B.D.1
  • 77
    • 0023665124 scopus 로고
    • 3 metabolites on cytosolic free calcium in confluent mouse osteoblasts
    • 3 metabolites on cytosolic free calcium in confluent mouse osteoblasts. J. Biol. Chem. 262, 13168-13173 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 13168-13173
    • Lieberherr, M.1
  • 78
    • 0024471717 scopus 로고
    • 3 metabolites modulate dihydropyridine-sensitive calcium currents in clonal rat osteosarcoma cells
    • 3 metabolites modulate dihydropyridine-sensitive calcium currents in clonal rat osteosarcoma cells. J. Biol. Chem. 264, 20265-20274 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 20265-20274
    • Caffrey, J.M.1    Farach-Carson, M.C.2
  • 79
    • 0025059416 scopus 로고
    • Nongenomic activation of the calcium message system by vitamin D metabolites in osteoblast-like cells
    • Civitelli, R. et al. Nongenomic activation of the calcium message system by vitamin D metabolites in osteoblast-like cells. Endocrinology 127, 2253-2262 (1990).
    • (1990) Endocrinology , vol.127 , pp. 2253-2262
    • Civitelli, R.1
  • 80
    • 0026353657 scopus 로고
    • 3 rapidly increases cytosolic calcium in clonal rat osteosarcoma cells lacking the vitamin D receptor
    • 3 rapidly increases cytosolic calcium in clonal rat osteosarcoma cells lacking the vitamin D receptor. J. Bone Miner. Res. 6, 1269-1275 (1991).
    • (1991) J. Bone Miner. Res. , vol.6 , pp. 1269-1275
    • Baran, D.T.1
  • 81
    • 0030978912 scopus 로고    scopus 로고
    • Phospholipase Cβ membrane action of calcitriol and estradiol
    • Le Mellay, V., Grosse, B. & Lieberherr, M. Phospholipase Cβ and membrane action of calcitriol and estradiol. J. Biol. Chem. 272, 11902-11907 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 11902-11907
    • Le Mellay, V.1    Grosse, B.2    Lieberherr, M.3
  • 83
    • 0025323383 scopus 로고
    • 3 stimulates membrane phosphoinositide turnover, activates protein kinase C, and increases cytosolic calcium in rat colonic epithelium
    • 3 stimulates membrane phosphoinositide turnover, activates protein kinase C, and increases cytosolic calcium in rat colonic epithelium. J. Clin. Invest. 85, 1296-1303 (1990).
    • (1990) J. Clin. Invest. , vol.85 , pp. 1296-1303
    • Wali, R.K.1    Baum, C.L.2    Sitrin, M.D.3    Brasitus, T.A.4
  • 84
    • 0344301937 scopus 로고    scopus 로고
    • 3 induced activation and subsequent nuclear translocation of MAPK is upstream regulated by PKC in HL-60 cells
    • 3 induced activation and subsequent nuclear translocation of MAPK is upstream regulated by PKC in HL-60 cells. Biochem. Biophys. Res. Commun. 241, 419-426 (1997).
    • (1997) Biochem. Biophys. Res. Commun. , vol.241 , pp. 419-426
    • Marcinkowska, E.1    Wiedlocha, A.2    Radzikowski, C.3
  • 85
    • 0025336751 scopus 로고
    • 3-mediated rapid stimulation of intestinal calcium transport, (transcaltachia)
    • 3-mediated rapid stimulation of intestinal calcium transport, (transcaltachia). Endocrinology 127, 39-45 (1990).
    • (1990) Endocrinology , vol.127 , pp. 39-45
    • De Boland, A.R.1    Norman, A.2
  • 89
    • 0028341427 scopus 로고
    • 3 stimulation of calcium uptake by rat intestinal cells involves a dihydropyndine-sensitive cAMP-dependent pathway
    • 3 stimulation of calcium uptake by rat intestinal cells involves a dihydropyndine-sensitive cAMP-dependent pathway. Cell Signal. 6, 299-304 (1994).
    • (1994) Cell Signal. , vol.6 , pp. 299-304
    • Massheimer, V.1    Boland, R.2    De Boland, A.R.3
  • 90
    • 0017669336 scopus 로고
    • 3H)glucose uptake in cultured chick embryo heart cells
    • 3H)glucose uptake in cultured chick embryo heart cells. Endocrinology 101, 143-149 (1977).
    • (1977) Endocrinology , vol.101 , pp. 143-149
    • Segal, J.1    Schwartz, H.2    Gordon, A.3
  • 91
    • 0024339850 scopus 로고
    • A rapid, extranuclear effect of 3,5,3′-triiodothyronine on sugar uptake by several tissues in the rat in vivo. Evidence for a physiological role for the thyroid hormone action at the level of the plasma membrane
    • Segal, J. A rapid, extranuclear effect of 3,5,3′-triiodothyronine on sugar uptake by several tissues in the rat in vivo. Evidence for a physiological role for the thyroid hormone action at the level of the plasma membrane. Endocrinology 124, 2755-2764 (1989).
    • (1989) Endocrinology , vol.124 , pp. 2755-2764
    • Segal, J.1
  • 92
    • 0025336750 scopus 로고
    • In vivo effect of 3,5,3′-triiodothyronine on calcium uptake in several tissues in the rat: Evidence for a physiological role for calcium as the first messenger for the prompt action of thyroid hormone at the level of the plasma membrane
    • Segal, J. In vivo effect of 3,5,3′-triiodothyronine on calcium uptake in several tissues in the rat: evidence for a physiological role for calcium as the first messenger for the prompt action of thyroid hormone at the level of the plasma membrane. Endocrinology 127, 17-24 (1990).
    • (1990) Endocrinology , vol.127 , pp. 17-24
    • Segal, J.1
  • 93
    • 0021032292 scopus 로고
    • 2+-ATPase activity in vitro Correlations between hormone structure and biological activity in a human cell system
    • 2+-ATPase activity in vitro Correlations between hormone structure and biological activity in a human cell system. J. Biol. Chem. 258, 12373-12377 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 12373-12377
    • Davis, F.B.1    Cody, V.2    Davis, P.J.3    Borzynski, L.J.4    Blas, S.D.5
  • 96
    • 0024524319 scopus 로고
    • Stimulation in vitro of rabbit erythrocyte cytosol phospholipid-dependent protein kinase activity. A novel action of thyroid hormone
    • Lawrence, W. D., Schoenl, M. & Davis, P. J. Stimulation in vitro of rabbit erythrocyte cytosol phospholipid-dependent protein kinase activity. A novel action of thyroid hormone. J. Biol. Chem. 264, 4766-4768 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 4766-4768
    • Lawrence, W.D.1    Schoenl, M.2    Davis, P.J.3
  • 97
    • 0029859219 scopus 로고    scopus 로고
    • Potentiation by thyroxine of interferon-γ-induced antiviral state requires PKA and PKC activities
    • Lin, H. Y., Thacorf, H. R., Davis, F. B. & Davis, P. J. Potentiation by thyroxine of interferon-γ-induced antiviral state requires PKA and PKC activities. Am. J. Physiol. 271, C1256-C1261 (1996).
    • (1996) Am. J. Physiol. , vol.271
    • Lin, H.Y.1    Thacorf, H.R.2    Davis, F.B.3    Davis, P.J.4
  • 98
    • 0035752485 scopus 로고    scopus 로고
    • Thyroxine signal transduction in liver cells involves phospholipase C and phospholipase D activation. Genomic independent action of thyroid hormone
    • Kavok, N. S., Krasilnikova, O. A. & Babenko, N. A. Thyroxine signal transduction in liver cells involves phospholipase C and phospholipase D activation. Genomic independent action of thyroid hormone. BMC Cell. Biol. 2, 5 (2001).
    • (2001) BMC Cell. Biol. , vol.2 , pp. 5
    • Kavok, N.S.1    Krasilnikova, O.A.2    Babenko, N.A.3
  • 99
    • 0033022440 scopus 로고    scopus 로고
    • Thyroid hormone induces activation of mitogen-activated protein kinase in cultured cells
    • Lin, H. Y., Davis, F. B., Gordinier, J. K., Martino, L. J. & Davis, P. J. Thyroid hormone induces activation of mitogen-activated protein kinase in cultured cells. Am. J. Physiol. 216, C1014-C1024 (1999).
    • (1999) Am. J. Physiol. , vol.216
    • Lin, H.Y.1    Davis, F.B.2    Gordinier, J.K.3    Martino, L.J.4    Davis, P.J.5
  • 100
    • 0040316990 scopus 로고    scopus 로고
    • Thyroid hormone promotes the phosphorylation of STAT3 and potentiates the action of epidermal growth factor in cultured cells
    • Lin, H. Y., Shih, A., Davis, F. B. & Davis, P. J. Thyroid hormone promotes the phosphorylation of STAT3 and potentiates the action of epidermal growth factor in cultured cells. Biochem. J. 338, 427-432 (1999).
    • (1999) Biochem. J. , vol.338 , pp. 427-432
    • Lin, H.Y.1    Shih, A.2    Davis, F.B.3    Davis, P.J.4
  • 101
    • 0034532451 scopus 로고    scopus 로고
    • Thyroxine promotes association of mitogen-activated protein kinase and nuclear thyroid hormone receptor (TR) and causes senne phosphorylation of TR
    • Davis, P. J., Shih, A. Lin, H. Y., Martino, L. J. & Davis, F. B. Thyroxine promotes association of mitogen-activated protein kinase and nuclear thyroid hormone receptor (TR) and causes senne phosphorylation of TR. J. Biol. Chem. 275, 38032-38039 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 38032-38039
    • Davis, P.J.1    Shih, A.2    Lin, H.Y.3    Martino, L.J.4    Davis, F.B.5
  • 102
    • 0025884038 scopus 로고
    • An in vitro novel mechanism of regulating the activity of pyruvate kinase M2 by thyroid hormone and fructose 1,6-bisphosphate
    • Ashizawa, K., McPhie, P., Lin, K. H. & Cheng, S. Y. An in vitro novel mechanism of regulating the activity of pyruvate kinase M2 by thyroid hormone and fructose 1,6-bisphosphate. Biochemistry 30, 7105-7111 (1991).
    • (1991) Biochemistry , vol.30 , pp. 7105-7111
    • Ashizawa, K.1    McPhie, P.2    Lin, K.H.3    Cheng, S.Y.4
  • 103
    • 0032031485 scopus 로고    scopus 로고
    • 3,5-Diiodothyronine binds to subunit Va of cytochrome-c oxidase and abolishes the allosteric inhibition of respiration by ATP
    • Arnold, S., Goglia, F. & Kadenbach, B. 3,5-Diiodothyronine binds to subunit Va of cytochrome-c oxidase and abolishes the allosteric inhibition of respiration by ATP. Eur. J. Biochem. 252, 325-330 (1998).
    • (1998) Eur. J. Biochem. , vol.252 , pp. 325-330
    • Arnold, S.1    Goglia, F.2    Kadenbach, B.3
  • 104
    • 0025737587 scopus 로고
    • Neurosteroids: A new function in the brain
    • Baulieu, E. E. Neurosteroids: a new function in the brain. Biol. Cell 71, 3-10 (1991). An early account of the origin and action of neurosteroids.
    • (1991) Biol. Cell , vol.71 , pp. 3-10
    • Baulieu, E.E.1
  • 106
    • 0022483382 scopus 로고
    • Steroid hormone metabolites are barbiturate-like modulators of the GABA receptor
    • Majewska, M. D., Harrison, N. L., Schwartz, R. D., Barker J. L. & Paul, S. M. Steroid hormone metabolites are barbiturate-like modulators of the GABA receptor Science 232, 1004-1007 (1986).
    • (1986) Science , vol.232 , pp. 1004-1007
    • Majewska, M.D.1    Harrison, N.L.2    Schwartz, R.D.3    Barker, J.L.4    Paul, S.M.5
  • 107
    • 0030821426 scopus 로고    scopus 로고
    • The neuropsychopharmacological potential of neuroactive steroids
    • Rupprecht, R. The neuropsychopharmacological potential of neuroactive steroids. J Psychiatr Res. 31, 297-314 (1997).
    • (1997) J Psychiatr Res. , vol.31 , pp. 297-314
    • Rupprecht, R.1
  • 108
    • 0034855948 scopus 로고    scopus 로고
    • The role of neurosteroids and nongenomic effects of progestins in the ventral tegmental area in mediating sexual receptivity of rodents
    • Frye, C. A. The role of neurosteroids and nongenomic effects of progestins in the ventral tegmental area in mediating sexual receptivity of rodents. Horm. Behav. 40, 226-233 (2001).
    • (2001) Horm. Behav. , vol.40 , pp. 226-233
    • Frye, C.A.1
  • 109
    • 0028032491 scopus 로고
    • The neurosteroid pregnenolone sulfate blocks NMDA antagonist-induced deficits in a passive avoidance memory task
    • Mathis, C., Paul, S. M. & Crawley, J. N. The neurosteroid pregnenolone sulfate blocks NMDA antagonist-induced deficits in a passive avoidance memory task. Psychopharmacology (Berl.) 116, 201-206 (1994).
    • (1994) Psychopharmacology (Berl.) , vol.116 , pp. 201-206
    • Mathis, C.1    Paul, S.M.2    Crawley, J.N.3
  • 110
    • 0032516942 scopus 로고    scopus 로고
    • σ(σ-1) receptor mediated anti-depressant-like effects of neurosteroids in the Porsolt forced swim test
    • Reddy, D. S., Kaur, G. & Kulkarni, S. K σ(σ-1) receptor mediated anti-depressant-like effects of neurosteroids in the Porsolt forced swim test. Neurereport 9, 3069-3073 (1998).
    • (1998) Neurereport , vol.9 , pp. 3069-3073
    • Reddy, D.S.1    Kaur, G.2    Kulkarni, S.K.3
  • 111
    • 0031552508 scopus 로고    scopus 로고
    • 17β-Estradiol protects against NMDA-induced excitotoxicity by direct inhibition of NMDA receptors
    • Weaver, C. E. Jr, Park-Chung, M., Gibbs, T. T. & Farb, D. H. 17β-Estradiol protects against NMDA-induced excitotoxicity by direct inhibition of NMDA receptors. Brain Res. 761, 338-341 (1997).
    • (1997) Brain Res. , vol.761 , pp. 338-341
    • Weaver C.E., Jr.1    Park-Chung, M.2    Gibbs, T.T.3    Farb, D.H.4
  • 112
    • 0023022470 scopus 로고
    • Anxiolytic activity of an endogenous adrenal steroid
    • Crawley, J. N., Glowa, J. R., Majewska, M. D. & Paul, S. M. Anxiolytic activity of an endogenous adrenal steroid. Brain Res. 398, 382-385 (1986).
    • (1986) Brain Res. , vol.398 , pp. 382-385
    • Crawley, J.N.1    Glowa, J.R.2    Majewska, M.D.3    Paul, S.M.4
  • 114
    • 0025329137 scopus 로고
    • Inverse modulation of γ-aminobutyric acid- and glycine-induced currents by progesterone
    • Wu, F. S., Gibbs, T. T. & Farb, D. H. Inverse modulation of γ-aminobutyric acid- and glycine-induced currents by progesterone. Mol. Pharmacol. 37, 597-602 (1990).
    • (1990) Mol. Pharmacol. , vol.37 , pp. 597-602
    • Wu, F.S.1    Gibbs, T.T.2    Farb, D.H.3
  • 115
    • 0031052768 scopus 로고    scopus 로고
    • Competitive inhibition of the glycine-induced current by pregnenolone sulfate in cultured chick spinal cord neurons
    • Wu, F. S., Chen, S. C. & Tsai, J. J. Competitive inhibition of the glycine-induced current by pregnenolone sulfate in cultured chick spinal cord neurons. Brain Res. 750, 318-320 (1997).
    • (1997) Brain Res. , vol.750 , pp. 318-320
    • Wu, F.S.1    Chen, S.C.2    Tsai, J.J.3
  • 116
    • 0033989747 scopus 로고    scopus 로고
    • Non-competitive inhibition of 5-HT3 receptor-mediated currents by progesterone in rat nodose ganglion neurons
    • Wu, F. S., Lai, C. P. & Liu, B. C. Non-competitive inhibition of 5-HT3 receptor-mediated currents by progesterone in rat nodose ganglion neurons. Neurosci. Lett. 278, 37-40 (2000).
    • (2000) Neurosci. Lett. , vol.278 , pp. 37-40
    • Wu, F.S.1    Lai, C.P.2    Liu, B.C.3
  • 117
    • 0035834075 scopus 로고    scopus 로고
    • Early membrane estrogenic effects required for full expression of slower genomic actions in a nerve cell line
    • Vasudevan, N., Kow, L. M. & Pfaff, D. W. Early membrane estrogenic effects required for full expression of slower genomic actions in a nerve cell line. Proc. Natl Acad Sci. USA 98, 12267-12271 (2001). The synergy between rapid nongenomic and delayed genomic effects of the same steroid is shown in this study.
    • (2001) Proc. Natl. Acad Sci. USA , vol.98 , pp. 12267-12271
    • Vasudevan, N.1    Kow, L.M.2    Pfaff, D.W.3
  • 118
    • 0026714673 scopus 로고
    • Phosphorylation of CREB affects its binding to high and low affinity sites: Implications for cAMP induced gene transcription
    • Nichols, M. et al. Phosphorylation of CREB affects its binding to high and low affinity sites: implications for cAMP induced gene transcription. EMBO J. 11, 3337-3346 (1992).
    • (1992) EMBO J. , vol.11 , pp. 3337-3346
    • Nichols, M.1
  • 119
    • 0344959523 scopus 로고    scopus 로고
    • Aldosterone, not estradiol, is the physiological agonist for rapid increases in cAMP in vascular smooth muscle cells
    • Christ, M. et al. Aldosterone, not estradiol, is the physiological agonist for rapid increases in cAMP in vascular smooth muscle cells. Circulation 99, 1485-1491 (1999).
    • (1999) Circulation , vol.99 , pp. 1485-1491
    • Christ, M.1
  • 120
    • 0034460313 scopus 로고    scopus 로고
    • 8-Bromo-cyclic AMP induces phosphorylation of two sites in SRC-1 that facilitate ligand-independent activation of the chicken progesterone receptor and are critical for functional cooperation between SRC-1 and CREB binding protein
    • Rowan, B. G., Garrison, N., Weigel, N. L. & O'Malley, B. W. 8-Bromo-cyclic AMP induces phosphorylation of two sites in SRC-1 that facilitate ligand-independent activation of the chicken progesterone receptor and are critical for functional cooperation between SRC-1 and CREB binding protein. Mol. Cell. Biol. 20, 8720-8730 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8720-8730
    • Rowan, B.G.1    Garrison, N.2    Weigel, N.L.3    O'Malley, B.W.4
  • 121
    • 0035093262 scopus 로고    scopus 로고
    • Interaction of rapid nongenomic cardiovascular aldosterone effects with the adrenergic system
    • Schmidt, B. M. et al. Interaction of rapid nongenomic cardiovascular aldosterone effects with the adrenergic system. J. Clin. Endocrinol. Metab. 86, 761-767 (2001).
    • (2001) J. Clin. Endocrinol. Metab. , vol.86 , pp. 761-767
    • Schmidt, B.M.1
  • 122
    • 0029801046 scopus 로고    scopus 로고
    • Nongenomic effects of aldosterone on phosphocreatine levels in human calf muscle during recovery from exercise
    • Zange, J., Müller, K., Gerzer, R., Sippel, K. & Wehling, M. Nongenomic effects of aldosterone on phosphocreatine levels in human calf muscle during recovery from exercise. J. Clin. Endocrinol. Metab. 81, 4296-4300 (1996).
    • (1996) J. Clin. Endocrinol. Metab. , vol.81 , pp. 4296-4300
    • Zange, J.1    Müller, K.2    Gerzer, R.3    Sippel, K.4    Wehling, M.5


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