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Volumn 102, Issue 1-5 SPEC. ISS., 2006, Pages 180-183

Non-genomic steroid hormone effects: Membrane or intracellular receptors?

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALS; CELL MEMBRANE; GENE EXPRESSION REGULATION; GENOME; HORMONES; HUMANS; RECEPTORS, STEROID;

EID: 33751210104     PISSN: 09600760     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jsbmb.2006.09.016     Document Type: Article
Times cited : (85)

References (31)
  • 2
    • 0034711337 scopus 로고    scopus 로고
    • Nongenomic, ER-mediated activation of endothelial nitric oxide synthase: how does it work? What does it mean?
    • Mendelsohn M.E. Nongenomic, ER-mediated activation of endothelial nitric oxide synthase: how does it work? What does it mean?. Circ. Res. 87 (2000) 956-960
    • (2000) Circ. Res. , vol.87 , pp. 956-960
    • Mendelsohn, M.E.1
  • 3
    • 23744447497 scopus 로고    scopus 로고
    • Integration of the extranuclear and nuclear actions of estrogen
    • Levin E.R. Integration of the extranuclear and nuclear actions of estrogen. Mol. Endocrinol. 19 (2005) 1951-1959
    • (2005) Mol. Endocrinol. , vol.19 , pp. 1951-1959
    • Levin, E.R.1
  • 4
    • 0037069418 scopus 로고    scopus 로고
    • Estrogen receptor-interacting protein that modulates its nongenomic activity-crosstalk with Src/Erk phosphorylation cascade
    • Wong C.W., McNally C., Nickbarg E., Komm B.S., and Cheskis B.J. Estrogen receptor-interacting protein that modulates its nongenomic activity-crosstalk with Src/Erk phosphorylation cascade. Proc. Natl. Acad. Sci. USA 99 (2002) 14783-14788
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14783-14788
    • Wong, C.W.1    McNally, C.2    Nickbarg, E.3    Komm, B.S.4    Cheskis, B.J.5
  • 6
    • 2342539826 scopus 로고    scopus 로고
    • Estren (4-estren-3alpha, 17beta-diol) is a prohormone that regulates both androgenic and estrogenic transcriptional effects through the androgen receptor
    • Centrella M., McCarthy T.L., Chang W.Z., Labaree D.C., and Hochberg R.B. Estren (4-estren-3alpha, 17beta-diol) is a prohormone that regulates both androgenic and estrogenic transcriptional effects through the androgen receptor. Mol. Endocrinol. 18 (2004) 1120-1130
    • (2004) Mol. Endocrinol. , vol.18 , pp. 1120-1130
    • Centrella, M.1    McCarthy, T.L.2    Chang, W.Z.3    Labaree, D.C.4    Hochberg, R.B.5
  • 7
    • 0032898877 scopus 로고    scopus 로고
    • Rapid and genomic biological responses are mediated by different shapes of the agonist steroid hormone, 1alpha, 25(OH)2vitamin D3
    • Norman A.W., Song X., Zanello L., Bula C., and Okamura W.H. Rapid and genomic biological responses are mediated by different shapes of the agonist steroid hormone, 1alpha, 25(OH)2vitamin D3. Steroids 64 (1999) 120-128
    • (1999) Steroids , vol.64 , pp. 120-128
    • Norman, A.W.1    Song, X.2    Zanello, L.3    Bula, C.4    Okamura, W.H.5
  • 8
    • 1242274642 scopus 로고    scopus 로고
    • Rapid modulation of osteoblast ion channel responses by 1alpha, 25(OH)2-Vitamin D3 requires the presence of a functional Vitamin D nuclear receptor
    • Zanello L.P., and Norman A.W. Rapid modulation of osteoblast ion channel responses by 1alpha, 25(OH)2-Vitamin D3 requires the presence of a functional Vitamin D nuclear receptor. Proc. Natl. Acad. Sci. USA 101 (2004) 1589-1594
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 1589-1594
    • Zanello, L.P.1    Norman, A.W.2
  • 9
    • 17144428054 scopus 로고    scopus 로고
    • Nongenotropic, anti-apoptotic signaling of 1alpha, 25(OH)2-Vitamin D3 and analogs through the ligand binding domain of the Vitamin D receptor in osteoblasts and osteocytes. Mediation by Src, phosphatidylinositol 3-, and JNK kinases
    • Vertino A.M., Bula C.M., Chen J.R., Almeida M., Han L., Bellido T., Kousteni S., Norman A.W., and Manolagas S.C. Nongenotropic, anti-apoptotic signaling of 1alpha, 25(OH)2-Vitamin D3 and analogs through the ligand binding domain of the Vitamin D receptor in osteoblasts and osteocytes. Mediation by Src, phosphatidylinositol 3-, and JNK kinases. J. Biol. Chem. 280 (2005) 14130-14137
    • (2005) J. Biol. Chem. , vol.280 , pp. 14130-14137
    • Vertino, A.M.1    Bula, C.M.2    Chen, J.R.3    Almeida, M.4    Han, L.5    Bellido, T.6    Kousteni, S.7    Norman, A.W.8    Manolagas, S.C.9
  • 10
    • 0345874610 scopus 로고    scopus 로고
    • Steroid-hormone rapid actions, membrane receptors and a conformational ensemble model
    • Norman A.W., Mizwicki M.T., and Norman D.P. Steroid-hormone rapid actions, membrane receptors and a conformational ensemble model. Nat. Rev. Drug. Discov. 3 (2004) 27-41
    • (2004) Nat. Rev. Drug. Discov. , vol.3 , pp. 27-41
    • Norman, A.W.1    Mizwicki, M.T.2    Norman, D.P.3
  • 11
    • 21544445248 scopus 로고    scopus 로고
    • Rapid, nongenomic responses to ecdysteroids and catecholamines mediated by a novel Drosophila G-protein-coupled receptor
    • Srivastava D.P., Yu E.J., Kennedy K., Chatwin H., Reale V., Hamon M., Smith T., and Evans P.D. Rapid, nongenomic responses to ecdysteroids and catecholamines mediated by a novel Drosophila G-protein-coupled receptor. J. Neurosci. 25 (2005) 6145-6155
    • (2005) J. Neurosci. , vol.25 , pp. 6145-6155
    • Srivastava, D.P.1    Yu, E.J.2    Kennedy, K.3    Chatwin, H.4    Reale, V.5    Hamon, M.6    Smith, T.7    Evans, P.D.8
  • 12
    • 0034633656 scopus 로고    scopus 로고
    • Nongenomic actions of estrogens and xenoestrogens by binding at a plasma membrane receptor unrelated to estrogen receptor alpha and estrogen receptor beta
    • Nadal A., Ropero A.B., Laribi O., Maillet M., Fuentes E., and Soria B. Nongenomic actions of estrogens and xenoestrogens by binding at a plasma membrane receptor unrelated to estrogen receptor alpha and estrogen receptor beta. Proc. Natl. Acad. Sci. USA 97 (2000) 11603-11608
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11603-11608
    • Nadal, A.1    Ropero, A.B.2    Laribi, O.3    Maillet, M.4    Fuentes, E.5    Soria, B.6
  • 13
    • 0033780783 scopus 로고    scopus 로고
    • Estrogen-induced activation of Erk-1 and Erk-2 requires the G protein-coupled receptor homolog, GPR30, and occurs via trans-activation of the epidermal growth factor receptor through release of HB-EGF
    • Filardo E.J., Quinn J.A., Bland K.I., and Frackelton Jr. A.R. Estrogen-induced activation of Erk-1 and Erk-2 requires the G protein-coupled receptor homolog, GPR30, and occurs via trans-activation of the epidermal growth factor receptor through release of HB-EGF. Mol. Endocrinol. 14 (2000) 1649-1660
    • (2000) Mol. Endocrinol. , vol.14 , pp. 1649-1660
    • Filardo, E.J.1    Quinn, J.A.2    Bland, K.I.3    Frackelton Jr., A.R.4
  • 14
    • 0036140032 scopus 로고    scopus 로고
    • Estrogen action via the G protein-coupled receptor, GPR30: stimulation of adenylyl cyclase and cAMP-mediated attenuation of the epidermal growth factor receptor-to-MAPK signaling axis
    • Filardo E.J., Quinn J.A., Frackelton Jr. A.R., and Bland K.I. Estrogen action via the G protein-coupled receptor, GPR30: stimulation of adenylyl cyclase and cAMP-mediated attenuation of the epidermal growth factor receptor-to-MAPK signaling axis. Mol. Endocrinol. 16 (2002) 70-84
    • (2002) Mol. Endocrinol. , vol.16 , pp. 70-84
    • Filardo, E.J.1    Quinn, J.A.2    Frackelton Jr., A.R.3    Bland, K.I.4
  • 15
    • 14844343093 scopus 로고    scopus 로고
    • A transmembrane intracellular estrogen receptor mediates rapid cell signaling
    • Revankar C.M., Cimino D.F., Sklar L.A., Arterburn J.B., and Prossnitz E.R. A transmembrane intracellular estrogen receptor mediates rapid cell signaling. Science 307 (2005) 1625-1630
    • (2005) Science , vol.307 , pp. 1625-1630
    • Revankar, C.M.1    Cimino, D.F.2    Sklar, L.A.3    Arterburn, J.B.4    Prossnitz, E.R.5
  • 17
    • 4243538525 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of a putative membrane progestin receptor in a fish model, spotted seatrout (Abstract)
    • The Endocrine Society, San Francisco
    • Zhu Y., Rice C.D., and Thomas P. Cloning, expression, and characterization of a putative membrane progestin receptor in a fish model, spotted seatrout (Abstract). Proceedings of the 84th Annual Meeting. The Endocrine Society, San Francisco (2002) P1-P448
    • (2002) Proceedings of the 84th Annual Meeting
    • Zhu, Y.1    Rice, C.D.2    Thomas, P.3
  • 18
    • 23544467742 scopus 로고    scopus 로고
    • Discovery of a new family of cDNAs encoding putative membrane progesterone receptors in vertebrates (Abstract)
    • The Endocrine Society, San Francisco
    • Zhu Y., and Thomas P. Discovery of a new family of cDNAs encoding putative membrane progesterone receptors in vertebrates (Abstract). Proceedings of the 84th Annual Meeting. The Endocrine Society, San Francisco (2002) P1-P451
    • (2002) Proceedings of the 84th Annual Meeting
    • Zhu, Y.1    Thomas, P.2
  • 19
    • 33751243458 scopus 로고    scopus 로고
    • Y.T. Tang, T. Hu, M. Arterburn, B. Boyle, J.M. Bright, P.C. Emtage, W.D. Funk, PAQR proteins: a novel membrane receptor family defined by an ancient7-transmembrane pass motif, J. Mol. Evol., in press.
  • 21
    • 33646806787 scopus 로고    scopus 로고
    • Progesterone membrane receptor component 1 expression in the immature rat ovary and its role in mediating progesterone's antiapoptotic action
    • Peluso J.J., Pappalardo A., Losel R., and Wehling M. Progesterone membrane receptor component 1 expression in the immature rat ovary and its role in mediating progesterone's antiapoptotic action. Endocrinology 147 (2006) 3133-3140
    • (2006) Endocrinology , vol.147 , pp. 3133-3140
    • Peluso, J.J.1    Pappalardo, A.2    Losel, R.3    Wehling, M.4
  • 22
    • 0344011652 scopus 로고    scopus 로고
    • 2D3 are retained in growth plate cartilage cells from Vitamin D receptor knockout mice
    • 2D3 are retained in growth plate cartilage cells from Vitamin D receptor knockout mice. J. Cell. Biochem. 90 (2003) 1207-1223
    • (2003) J. Cell. Biochem. , vol.90 , pp. 1207-1223
    • Boyan, B.D.1    Sylvia, V.L.2    McKinney, N.3    Schwartz, Z.4
  • 23
    • 0037369733 scopus 로고    scopus 로고
    • Vitamin D receptor is not required for the rapid actions of 1, 25-dihydroxyvitamin D3 to increase intracellular calcium and activate protein kinase C in mouse osteoblasts
    • Wali R.K., Kong J., Sitrin M.D., Bissonnette M., and Li Y.C. Vitamin D receptor is not required for the rapid actions of 1, 25-dihydroxyvitamin D3 to increase intracellular calcium and activate protein kinase C in mouse osteoblasts. J. Cell. Biochem. 88 (2003) 794-801
    • (2003) J. Cell. Biochem. , vol.88 , pp. 794-801
    • Wali, R.K.1    Kong, J.2    Sitrin, M.D.3    Bissonnette, M.4    Li, Y.C.5
  • 25
    • 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., and Franco-Saenz R. Rapid effects of aldosterone and spironolactone in the isolated working rat heart. Hypertension 40 (2002) 130-135
    • (2002) Hypertension , vol.40 , pp. 130-135
    • Barbato, J.C.1    Mulrow, P.J.2    Shapiro, J.I.3    Franco-Saenz, R.4
  • 26
    • 0344364894 scopus 로고
    • The anaesthetic effect of steroid hormones
    • Selye H. The anaesthetic effect of steroid hormones. Proc. Soc. Exp. Biol. Med. 46 (1941) 116-121
    • (1941) Proc. Soc. Exp. Biol. Med. , vol.46 , pp. 116-121
    • Selye, H.1
  • 30
    • 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., and Ferrell Jr. J.E. The classical progesterone receptor associates with p42 MAPK and is involved in phosphatidylinositol 3-kinase signaling in Xenopus oocytes. J. Biol. Chem. 276 (2001) 37708-37714
    • (2001) J. Biol. Chem. , vol.276 , pp. 37708-37714
    • Bagowski, C.P.1    Myers, J.W.2    Ferrell Jr., J.E.3
  • 31
    • 18144392728 scopus 로고    scopus 로고
    • Vascular cell signaling by membrane estrogen receptors
    • Hisamoto K., and Bender J.R. Vascular cell signaling by membrane estrogen receptors. Steroids 70 (2005) 382-387
    • (2005) Steroids , vol.70 , pp. 382-387
    • Hisamoto, K.1    Bender, J.R.2


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