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Volumn 111, Issue 3-5, 2008, Pages 255-261

Estrogen and progesterone regulate the IL-6 signal transduction pathway in antibody secreting cells

Author keywords

Estrogen; Hybridoma; Interleukin 6; PIBF; Progesterone; Signal transduction

Indexed keywords

ESTROGEN; GLYCOPROTEIN GP 130; INTERLEUKIN 6; JANUS KINASE 1; PROGESTERONE; PROGESTERONE INDUCED BLOCKING FACTOR; PROTEIN; STAT3 PROTEIN;

EID: 49449097808     PISSN: 09600760     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jsbmb.2008.06.009     Document Type: Article
Times cited : (29)

References (57)
  • 1
    • 0035026467 scopus 로고    scopus 로고
    • Sex hormones as immunomodulators in health and disease
    • Verthelyi D. Sex hormones as immunomodulators in health and disease. Int. Immunopharmacol. 1 (2001) 983-993
    • (2001) Int. Immunopharmacol. , vol.1 , pp. 983-993
    • Verthelyi, D.1
  • 5
    • 0024389227 scopus 로고
    • Fetus as an allograft: noncytotoxic maternal antibodies to HLA-linked paternal antigens
    • Innes A., Cunningham C., Power D.A., and Catto G.R. Fetus as an allograft: noncytotoxic maternal antibodies to HLA-linked paternal antigens. Am. J. Reprod. Immunol. 19 (1989) 146-150
    • (1989) Am. J. Reprod. Immunol. , vol.19 , pp. 146-150
    • Innes, A.1    Cunningham, C.2    Power, D.A.3    Catto, G.R.4
  • 6
    • 0025776877 scopus 로고
    • IgG asymmetric molecules with anti-paternal activity isolated from sera and placenta of pregnant human
    • Malan Borel I., Gentile T., Angelucci J., Pividori J., and Margni R. IgG asymmetric molecules with anti-paternal activity isolated from sera and placenta of pregnant human. J. Reprod. Immunol. 20 (1991) 129-140
    • (1991) J. Reprod. Immunol. , vol.20 , pp. 129-140
    • Malan Borel, I.1    Gentile, T.2    Angelucci, J.3    Pividori, J.4    Margni, R.5
  • 10
    • 0022640619 scopus 로고
    • Structure of asymmetric non-precipitating antibodies. Presence of a carbohydrate residue in only one Fab region of the molecule
    • Labeta M., Margni R., Leoni J., and Binaghi R. Structure of asymmetric non-precipitating antibodies. Presence of a carbohydrate residue in only one Fab region of the molecule. Immunology 57 (1986) 314-317
    • (1986) Immunology , vol.57 , pp. 314-317
    • Labeta, M.1    Margni, R.2    Leoni, J.3    Binaghi, R.4
  • 11
    • 0022969786 scopus 로고
    • The asymmetric IgG non-precipitating antibody. Localization of the oligosaccharide involved by Concanavalin A interaction
    • Leoni J., Labeta M., and Margni R.A. The asymmetric IgG non-precipitating antibody. Localization of the oligosaccharide involved by Concanavalin A interaction. Mol. Immunol. 23 (1986) 1397-1400
    • (1986) Mol. Immunol. , vol.23 , pp. 1397-1400
    • Leoni, J.1    Labeta, M.2    Margni, R.A.3
  • 12
    • 0024392175 scopus 로고
    • Effects of monocytic products, recombinant interleukin-1, and recombinant interleukin-6 on glycosylation of alpha 1-acid glycoprotein: studies with primary human hepatocyte cultures and rats
    • Pos O., Moshage H.J., Yap S.H., Snieders J.P., Aarden L.A., van Gool J., Boers W., Brugman A.M., and van Dijk W. Effects of monocytic products, recombinant interleukin-1, and recombinant interleukin-6 on glycosylation of alpha 1-acid glycoprotein: studies with primary human hepatocyte cultures and rats. Inflammation 13 (1989) 415-427
    • (1989) Inflammation , vol.13 , pp. 415-427
    • Pos, O.1    Moshage, H.J.2    Yap, S.H.3    Snieders, J.P.4    Aarden, L.A.5    van Gool, J.6    Boers, W.7    Brugman, A.M.8    van Dijk, W.9
  • 13
    • 0026632640 scopus 로고
    • Soluble human interleukin-6-receptor modulates interleukin-6-dependent N-glycosylation of alpha 1-protease inhibitor secreted by HeP42 cells
    • Mackiewicz A., Rose-John S., Schooltink H., Laciak M., Gorny A., and Heinrich P.C. Soluble human interleukin-6-receptor modulates interleukin-6-dependent N-glycosylation of alpha 1-protease inhibitor secreted by HeP42 cells. FEBS Lett. 306 (1992) 257-261
    • (1992) FEBS Lett. , vol.306 , pp. 257-261
    • Mackiewicz, A.1    Rose-John, S.2    Schooltink, H.3    Laciak, M.4    Gorny, A.5    Heinrich, P.C.6
  • 14
    • 0035180380 scopus 로고    scopus 로고
    • The placental regulatory factor involved in the asymmetric IgG antibody synthesis responds to IL-6 features
    • Gutierrez G., Malan Borel I., and Margni R.A. The placental regulatory factor involved in the asymmetric IgG antibody synthesis responds to IL-6 features. J. Reprod. Immunol. 49 (2001) 21-32
    • (2001) J. Reprod. Immunol. , vol.49 , pp. 21-32
    • Gutierrez, G.1    Malan Borel, I.2    Margni, R.A.3
  • 15
    • 0010444195 scopus 로고    scopus 로고
    • During pregnancy, in the context of a Th2-type cytokine profile, IL-6 levels might condition the quality of the synthesized antibodies
    • Margni R.A., and Zenclussen A.C. During pregnancy, in the context of a Th2-type cytokine profile, IL-6 levels might condition the quality of the synthesized antibodies. Am. J. Reprod. Immunol. 44 (2000) 22-29
    • (2000) Am. J. Reprod. Immunol. , vol.44 , pp. 22-29
    • Margni, R.A.1    Zenclussen, A.C.2
  • 16
    • 0036829288 scopus 로고    scopus 로고
    • In vitro modulation of protective antibody responses by estrogen, progesterone and interleukin-6
    • Canellada A., Blois S., Gentile T., and Margni R.A. In vitro modulation of protective antibody responses by estrogen, progesterone and interleukin-6. Am. J. Reprod. Immunol. 48 (2002) 333-343
    • (2002) Am. J. Reprod. Immunol. , vol.48 , pp. 333-343
    • Canellada, A.1    Blois, S.2    Gentile, T.3    Margni, R.A.4
  • 17
    • 0030069904 scopus 로고    scopus 로고
    • A progesterone-induced protein increases the synthesis of asymmetric antibodies
    • Kelemen K., Bognar I., Paal M., and Szekeres-Bartho J. A progesterone-induced protein increases the synthesis of asymmetric antibodies. Cell. Immunol. 167 (1996) 129-134
    • (1996) Cell. Immunol. , vol.167 , pp. 129-134
    • Kelemen, K.1    Bognar, I.2    Paal, M.3    Szekeres-Bartho, J.4
  • 19
    • 0027618650 scopus 로고
    • Regulation of the NF-kappa B/rel transcription factor and I kappa B inhibitor system
    • Liou H.C., and Baltimore D. Regulation of the NF-kappa B/rel transcription factor and I kappa B inhibitor system. Curr. Opin. Cell. Biol. 5 (1993) 477-487
    • (1993) Curr. Opin. Cell. Biol. , vol.5 , pp. 477-487
    • Liou, H.C.1    Baltimore, D.2
  • 20
    • 0032711250 scopus 로고    scopus 로고
    • IL-6 up-regulates Mcl-1 in human myeloma cells through JAK/STAT rather than ras/MAP kinase pathway
    • Puthier D., Bataille R., and Amiot M. IL-6 up-regulates Mcl-1 in human myeloma cells through JAK/STAT rather than ras/MAP kinase pathway. Eur. J. Immunol. 29 (1999) 3945-3950
    • (1999) Eur. J. Immunol. , vol.29 , pp. 3945-3950
    • Puthier, D.1    Bataille, R.2    Amiot, M.3
  • 21
    • 0034548453 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase/AKT kinase pathway in multiple myeloma plasma cells: roles in cytokine-dependent survival and proliferative responses
    • Tu Y., Gardner A., and Lichtenstein A. The phosphatidylinositol 3-kinase/AKT kinase pathway in multiple myeloma plasma cells: roles in cytokine-dependent survival and proliferative responses. Cancer Res. 60 (2000) 6763-6770
    • (2000) Cancer Res. , vol.60 , pp. 6763-6770
    • Tu, Y.1    Gardner, A.2    Lichtenstein, A.3
  • 22
    • 0035921689 scopus 로고    scopus 로고
    • Biologic sequelae of interleukin-6 induced PI3-K/Akt signaling in multiple myeloma
    • Hideshima T., Nakamura N., Chauhan D., and Anderson K.C. Biologic sequelae of interleukin-6 induced PI3-K/Akt signaling in multiple myeloma. Oncogene 20 (2001) 5991-6000
    • (2001) Oncogene , vol.20 , pp. 5991-6000
    • Hideshima, T.1    Nakamura, N.2    Chauhan, D.3    Anderson, K.C.4
  • 23
    • 2442715069 scopus 로고    scopus 로고
    • Interleukin-6 activates phosphoinositol-3′ kinase in multiple myeloma tumor cells by signaling through RAS dependent and, separately, through p85-dependent pathways
    • Hsu J.H., Shi Y., Frost P., Yan H., Hoang B., Sharma S., Gera J., and Lichtenstein A. Interleukin-6 activates phosphoinositol-3′ kinase in multiple myeloma tumor cells by signaling through RAS dependent and, separately, through p85-dependent pathways. Oncogene 23 (2004) 3368-3375
    • (2004) Oncogene , vol.23 , pp. 3368-3375
    • Hsu, J.H.1    Shi, Y.2    Frost, P.3    Yan, H.4    Hoang, B.5    Sharma, S.6    Gera, J.7    Lichtenstein, A.8
  • 24
    • 2442679239 scopus 로고    scopus 로고
    • Critical role for hematopoietic cell kinase (Hck)-mediated phosphorylation of Gab1 and Gab2 docking proteins in interleukin 6-induced proliferation and survival of multiple myeloma cells
    • Podar K., Mostoslavsky G., Sattler M., Tai Y.T., Hayashi T., Catley L.P., Hideshima T., Mulligan R.C., Chauhan D., and Anderson K.C. Critical role for hematopoietic cell kinase (Hck)-mediated phosphorylation of Gab1 and Gab2 docking proteins in interleukin 6-induced proliferation and survival of multiple myeloma cells. J. Biol. Chem. 279 (2004) 21658-21665
    • (2004) J. Biol. Chem. , vol.279 , pp. 21658-21665
    • Podar, K.1    Mostoslavsky, G.2    Sattler, M.3    Tai, Y.T.4    Hayashi, T.5    Catley, L.P.6    Hideshima, T.7    Mulligan, R.C.8    Chauhan, D.9    Anderson, K.C.10
  • 25
    • 0028234529 scopus 로고
    • Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins
    • Darnell J.E., Kerr I.M., and Stark G.R. Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins. Science 264 (1994) 1415-1421
    • (1994) Science , vol.264 , pp. 1415-1421
    • Darnell, J.E.1    Kerr, I.M.2    Stark, G.R.3
  • 26
    • 0028921573 scopus 로고
    • Jaks and Stats in signaling by the cytokine receptor superfamily
    • Ihle J.N., and Kerr I.M. Jaks and Stats in signaling by the cytokine receptor superfamily. Trends Genet. 11 (1995) 69-74
    • (1995) Trends Genet. , vol.11 , pp. 69-74
    • Ihle, J.N.1    Kerr, I.M.2
  • 27
    • 0027493650 scopus 로고
    • A single phosphotyrosine residue of Stat91 required for gene activation by interferon-gamma
    • Shuai K., Stark G.R., Kerr I.M., and Darnell J.E. A single phosphotyrosine residue of Stat91 required for gene activation by interferon-gamma. Science 261 (1993) 1744-1746
    • (1993) Science , vol.261 , pp. 1744-1746
    • Shuai, K.1    Stark, G.R.2    Kerr, I.M.3    Darnell, J.E.4
  • 31
    • 0028349735 scopus 로고
    • Stat3: a STAT family member activated by tyrosine phosphorylation in response to epidermal growth factor and interleukin-6
    • Zhong Z., Wen Z., and Darnell J.E. Stat3: a STAT family member activated by tyrosine phosphorylation in response to epidermal growth factor and interleukin-6. Science 264 (1994) 95-98
    • (1994) Science , vol.264 , pp. 95-98
    • Zhong, Z.1    Wen, Z.2    Darnell, J.E.3
  • 32
    • 0029887373 scopus 로고    scopus 로고
    • Differential activation of acute phase response factor/STAT3 and STAT1 via the cytoplasmic domain of the interleukin 6 signal transducer gp130, I. Definition of a novel phosphotyrosine motif mediating STAT1 activation
    • Gerhartz C., Heesel B., Sasse J., Hemmann U., Landgraf C., Schneider-Mergener J., Horn F., Heinrich P.C., and Graeve L. Differential activation of acute phase response factor/STAT3 and STAT1 via the cytoplasmic domain of the interleukin 6 signal transducer gp130, I. Definition of a novel phosphotyrosine motif mediating STAT1 activation. J. Biol. Chem. 271 (1996) 12991-12998
    • (1996) J. Biol. Chem. , vol.271 , pp. 12991-12998
    • Gerhartz, C.1    Heesel, B.2    Sasse, J.3    Hemmann, U.4    Landgraf, C.5    Schneider-Mergener, J.6    Horn, F.7    Heinrich, P.C.8    Graeve, L.9
  • 33
  • 35
    • 25444489843 scopus 로고    scopus 로고
    • Nuclear receptors as negative modulators of STAT3 in multiple myeloma
    • Wang L.H., Yang X.Y., Zhang X., and Farrar W.L. Nuclear receptors as negative modulators of STAT3 in multiple myeloma. Cell Cycle 4 (2005) 242-245
    • (2005) Cell Cycle , vol.4 , pp. 242-245
    • Wang, L.H.1    Yang, X.Y.2    Zhang, X.3    Farrar, W.L.4
  • 37
    • 0036510548 scopus 로고    scopus 로고
    • Activation of the androgen receptor N-terminal domain by interleukin-6 via MAPK and STAT3 signal transduction pathways
    • Ueda T., Bruchovsky N., and Sadar M.D. Activation of the androgen receptor N-terminal domain by interleukin-6 via MAPK and STAT3 signal transduction pathways. J. Biol. Chem. 277 (2002) 7076-7085
    • (2002) J. Biol. Chem. , vol.277 , pp. 7076-7085
    • Ueda, T.1    Bruchovsky, N.2    Sadar, M.D.3
  • 38
    • 0037064106 scopus 로고    scopus 로고
    • Ligand-independent activation of the androgen receptor by interleukin-6 and the role of steroid receptor coactivator-1 in prostate cancer cells
    • Ueda T., Mawji N.R., Bruchovsky N., and Sadar M.D. Ligand-independent activation of the androgen receptor by interleukin-6 and the role of steroid receptor coactivator-1 in prostate cancer cells. J. Biol. Chem. 277 (2002) 38087-38094
    • (2002) J. Biol. Chem. , vol.277 , pp. 38087-38094
    • Ueda, T.1    Mawji, N.R.2    Bruchovsky, N.3    Sadar, M.D.4
  • 39
    • 0027154239 scopus 로고
    • Analysis of oligosaccharides involved in the asymmetrical glycosylation of IgG monoclonal antibodies
    • Morelli L., Plotkin L., Leoni J., Fossati C., and Margni R. Analysis of oligosaccharides involved in the asymmetrical glycosylation of IgG monoclonal antibodies. Mol. Immunol. 30 (1993) 695-700
    • (1993) Mol. Immunol. , vol.30 , pp. 695-700
    • Morelli, L.1    Plotkin, L.2    Leoni, J.3    Fossati, C.4    Margni, R.5
  • 40
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the determination of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the determination of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 41
    • 0029075875 scopus 로고
    • Cooperative transcriptional activity of Jun and Stat3 beta, a short form of Stat3
    • Schaefer T.S., Sanders L.K., and Nathans D. Cooperative transcriptional activity of Jun and Stat3 beta, a short form of Stat3. Proc. Natl. Acad. Sci. U.S.A. 92 (1995) 9097-9101
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 9097-9101
    • Schaefer, T.S.1    Sanders, L.K.2    Nathans, D.3
  • 42
    • 0030221341 scopus 로고    scopus 로고
    • A progesterone-dependent immunomodulatory protein alters the Th1/Th2 balance
    • Szekeres-Barthó J., and Wegmann T.G. A progesterone-dependent immunomodulatory protein alters the Th1/Th2 balance. J. Reprod. Immunol. 31 (1996) 81-95
    • (1996) J. Reprod. Immunol. , vol.31 , pp. 81-95
    • Szekeres-Barthó, J.1    Wegmann, T.G.2
  • 44
    • 17344369783 scopus 로고    scopus 로고
    • Paradoxical behavior of asymmetric IgG antibodies
    • Margni R.A., and Malan Borel I. Paradoxical behavior of asymmetric IgG antibodies. Immunol. Rev. 163 (1998) 77-87
    • (1998) Immunol. Rev. , vol.163 , pp. 77-87
    • Margni, R.A.1    Malan Borel, I.2
  • 45
    • 0034669993 scopus 로고    scopus 로고
    • Constitutive activation of STAT3 is associated with the acquisition of an interleukin 6-independent phenotype by murine plasmacytomas and hybridomas
    • Rawat R., Rainey G.J., Thompson C.D., Frazier-Jessen M.R., Brown R.T., and Nordan R.P. Constitutive activation of STAT3 is associated with the acquisition of an interleukin 6-independent phenotype by murine plasmacytomas and hybridomas. Blood 96 (2000) 3514-3521
    • (2000) Blood , vol.96 , pp. 3514-3521
    • Rawat, R.1    Rainey, G.J.2    Thompson, C.D.3    Frazier-Jessen, M.R.4    Brown, R.T.5    Nordan, R.P.6
  • 47
    • 0030992813 scopus 로고    scopus 로고
    • Abrogation of interleukin-3 dependence of myeloid cells by the v-src oncogene requires SH2 and SH3 domains which specify activation of STATs
    • Chaturvedi P., Sharma S., and Reddy E.P. Abrogation of interleukin-3 dependence of myeloid cells by the v-src oncogene requires SH2 and SH3 domains which specify activation of STATs. Mol. Cell. Biol. 17 (1997) 3295-3304
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3295-3304
    • Chaturvedi, P.1    Sharma, S.2    Reddy, E.P.3
  • 52
    • 0034705453 scopus 로고    scopus 로고
    • The inhibition of interleukin-6-dependent STAT activation by mitogen-activated protein kinases depends on tyrosine 759 in the cytoplasmic tail of glycoprotein 130
    • Terstegen L., Gatsios P., Bode J.G., Schaper F., Heinrich P.C., and Graeve L. The inhibition of interleukin-6-dependent STAT activation by mitogen-activated protein kinases depends on tyrosine 759 in the cytoplasmic tail of glycoprotein 130. J. Biol. Chem. 275 (2000) 18810-18817
    • (2000) J. Biol. Chem. , vol.275 , pp. 18810-18817
    • Terstegen, L.1    Gatsios, P.2    Bode, J.G.3    Schaper, F.4    Heinrich, P.C.5    Graeve, L.6
  • 54
    • 0034724677 scopus 로고    scopus 로고
    • SOCS3 exerts its inhibitory function on interleukin-6 signal transduction through the SHP2 recruitment site of gp130
    • Schmitz J., Weissenbach M., Haan S., Heinrich P.C., and Schaper F. SOCS3 exerts its inhibitory function on interleukin-6 signal transduction through the SHP2 recruitment site of gp130. J. Biol. Chem. 275 (2000) 12848-12856
    • (2000) J. Biol. Chem. , vol.275 , pp. 12848-12856
    • Schmitz, J.1    Weissenbach, M.2    Haan, S.3    Heinrich, P.C.4    Schaper, F.5
  • 57
    • 23044501805 scopus 로고    scopus 로고
    • Interleukin-6 and dexamethasone modulate in vitro asymmetric antibody synthesis and UDP-Glc glycoprotein glycosyltransferase activity
    • Miranda S., Canellada A., Gentile T., and Margni R. Interleukin-6 and dexamethasone modulate in vitro asymmetric antibody synthesis and UDP-Glc glycoprotein glycosyltransferase activity. J. Reprod. Immunol. 66 (2005) 141-150
    • (2005) J. Reprod. Immunol. , vol.66 , pp. 141-150
    • Miranda, S.1    Canellada, A.2    Gentile, T.3    Margni, R.4


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