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Volumn 57, Issue 4, 1997, Pages 894-900

In vivo study of prolactin (PRL) intracellular signalling during lactogenesis in the rat: JAK/STAT pathway is activated by PRL in the mammary gland but not in the liver

Author keywords

[No Author keywords available]

Indexed keywords

PROLACTIN; PROLACTIN RECEPTOR;

EID: 0030886808     PISSN: 00063363     EISSN: None     Source Type: Journal    
DOI: 10.1095/biolreprod57.4.894     Document Type: Article
Times cited : (59)

References (45)
  • 2
    • 0019188943 scopus 로고
    • Ontogeny and evolution of prolactin's functions
    • Nicoll CS. Ontogeny and evolution of prolactin's functions. Fed Proc 1980; 39:2563-2566.
    • (1980) Fed Proc , vol.39 , pp. 2563-2566
    • Nicoll, C.S.1
  • 3
    • 0027057982 scopus 로고
    • Prolactin receptor triggering. Evidence for rapid tyrosine kinase activation
    • Rui H, Djeu JY, Evans GA, Kelly PA, Farrar WL. Prolactin receptor triggering. Evidence for rapid tyrosine kinase activation. J Biol Chem 1992; 267:24076-24081.
    • (1992) J Biol Chem , vol.267 , pp. 24076-24081
    • Rui, H.1    Djeu, J.Y.2    Evans, G.A.3    Kelly, P.A.4    Farrar, W.L.5
  • 4
    • 0027941433 scopus 로고
    • Activation of receptor-associated tyrosine kinase JAK2 by prolactin
    • Rui H, Kirken RA, Farrar WL. Activation of receptor-associated tyrosine kinase JAK2 by prolactin. J Biol Chem 1994; 269:5364-5368.
    • (1994) J Biol Chem , vol.269 , pp. 5364-5368
    • Rui, H.1    Kirken, R.A.2    Farrar, W.L.3
  • 5
    • 0026782391 scopus 로고
    • Evidence for a rapid stimulation of tyrosine kinase activity by prolactin in Nb2 rat lymphoma cells
    • Rillema JA, Campbell GB, Lawson DM, Carter-Su C. Evidence for a rapid stimulation of tyrosine kinase activity by prolactin in Nb2 rat lymphoma cells. Endocrinology 1992; 131:973-975.
    • (1992) Endocrinology , vol.131 , pp. 973-975
    • Rillema, J.A.1    Campbell, G.B.2    Lawson, D.M.3    Carter-Su, C.4
  • 7
    • 0027993605 scopus 로고
    • Prolactin induces phosphorylation of Tyr694 of StatS (MGF), a prerequisite for DNA binding and induction of transcription
    • Gouilleux F, Wakao H, Mundt M, Groner B. Prolactin induces phosphorylation of Tyr694 of StatS (MGF), a prerequisite for DNA binding and induction of transcription. EMBO J 1994; 13:4361-4369.
    • (1994) EMBO J , vol.13 , pp. 4361-4369
    • Gouilleux, F.1    Wakao, H.2    Mundt, M.3    Groner, B.4
  • 8
    • 0028174290 scopus 로고
    • Prolactin-induced proliferation of Nb2 cells involves tyrosine kinase phosphorylation of the prolactin receptor and its associated tyrosine kinase JAK2
    • Lebrun JJ, Ali S, Sofer L, Ullrich A, Kelly PA. Prolactin-induced proliferation of Nb2 cells involves tyrosine kinase phosphorylation of the prolactin receptor and its associated tyrosine kinase JAK2. J Biol Chem 1994; 269:14021-14026.
    • (1994) J Biol Chem , vol.269 , pp. 14021-14026
    • Lebrun, J.J.1    Ali, S.2    Sofer, L.3    Ullrich, A.4    Kelly, P.A.5
  • 9
    • 0028200640 scopus 로고
    • Tissue distribution and regulation of rat prolactin receptor gene expression. Quantitative analysis by polymerase chain reaction
    • Nagano M, Kelly PA. Tissue distribution and regulation of rat prolactin receptor gene expression. Quantitative analysis by polymerase chain reaction. J Biol Chem 1994; 269:13337-13345.
    • (1994) J Biol Chem , vol.269 , pp. 13337-13345
    • Nagano, M.1    Kelly, P.A.2
  • 10
    • 0026013468 scopus 로고
    • Comparison of long and short forms of the prolactin receptor on prolactin-induced milk protein gene transcription
    • Lesueur L, Edery M, Ali S, Paly J, Kelly PA, Djiane J. Comparison of long and short forms of the prolactin receptor on prolactin-induced milk protein gene transcription. Proc Natl Acad Sci USA 1991; 88: 824-828.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 824-828
    • Lesueur, L.1    Edery, M.2    Ali, S.3    Paly, J.4    Kelly, P.A.5    Djiane, J.6
  • 11
    • 0028801323 scopus 로고
    • Transduction of prolactin's (PRL) growth signal through both long and short forms of the PRL receptor
    • Das R, Vonderhaar BK. Transduction of prolactin's (PRL) growth signal through both long and short forms of the PRL receptor. Mol Endocrinol 1995; 9:1750-1759.
    • (1995) Mol Endocrinol , vol.9 , pp. 1750-1759
    • Das, R.1    Vonderhaar, B.K.2
  • 12
    • 0027973435 scopus 로고    scopus 로고
    • Differential signal transduction of the short, Nb2, and long prolactin receptors
    • O'Neal KD, Yu-Lee L. Differential signal transduction of the short, Nb2, and long prolactin receptors. J Biol Chem 1996; 269:26076-26082.
    • (1996) J Biol Chem , vol.269 , pp. 26076-26082
    • O'Neal, K.D.1    Yu-Lee, L.2
  • 13
    • 0027532279 scopus 로고
    • Effect of various protein kinase inhibitors on the induction of milk protein gene expression by prolactin
    • Bayat-Sarmadi M, Houdebine LM. Effect of various protein kinase inhibitors on the induction of milk protein gene expression by prolactin. Mol Cell Endocrinol 1993; 92:127-134.
    • (1993) Mol Cell Endocrinol , vol.92 , pp. 127-134
    • Bayat-Sarmadi, M.1    Houdebine, L.M.2
  • 14
    • 0026543465 scopus 로고
    • Effect of tyrosine kinase inhibitor, genistein, on the actions of prolactin on cultured mammary tissues
    • Fan G, Rillema JA. Effect of tyrosine kinase inhibitor, genistein, on the actions of prolactin on cultured mammary tissues. Mol Cell Endocrinol 1992; 83:51-55.
    • (1992) Mol Cell Endocrinol , vol.83 , pp. 51-55
    • Fan, G.1    Rillema, J.A.2
  • 15
    • 0029978341 scopus 로고    scopus 로고
    • Involvement of a subset of tyrosine kinase and phosphatase in regulation of the β-lactoglobulin promoter by prolactin
    • Daniel N, Waters MJ, Bignon C, Djiane J. Involvement of a subset of tyrosine kinase and phosphatase in regulation of the β-lactoglobulin promoter by prolactin. Mol Cell Endocrinol 1996; 118:25-35.
    • (1996) Mol Cell Endocrinol , vol.118 , pp. 25-35
    • Daniel, N.1    Waters, M.J.2    Bignon, C.3    Djiane, J.4
  • 16
    • 0029152254 scopus 로고
    • Activation of STAT factors by prolactin, interferon-gamma, growth hormones, and a tyrosine phosphatase inhibitor in rabbit primary mammary epithelial cells
    • Tourkine N, Schindler C, Larose M, Houdebine LM. Activation of STAT factors by prolactin, interferon-gamma, growth hormones, and a tyrosine phosphatase inhibitor in rabbit primary mammary epithelial cells. J Biol Chem 1995; 270:20952-20961.
    • (1995) J Biol Chem , vol.270 , pp. 20952-20961
    • Tourkine, N.1    Schindler, C.2    Larose, M.3    Houdebine, L.M.4
  • 17
    • 0028956974 scopus 로고
    • Proline-rich sequence-mediated JAK2 association to the prolactin receptor is required but not sufficient for signal transduction
    • Lebrun JJ, Ali S, Ullrich A, Kelly PA. Proline-rich sequence-mediated JAK2 association to the prolactin receptor is required but not sufficient for signal transduction. J Biol Chem 1995; 270:10664-10670.
    • (1995) J Biol Chem , vol.270 , pp. 10664-10670
    • Lebrun, J.J.1    Ali, S.2    Ullrich, A.3    Kelly, P.A.4
  • 18
    • 0021924126 scopus 로고
    • Hormonal regulation of casein synthesis at the end of pregnancy
    • Bussmann LE, Deis RP Hormonal regulation of casein synthesis at the end of pregnancy. Mol Cell Endocrinol 1984; 39:115-118.
    • (1984) Mol Cell Endocrinol , vol.39 , pp. 115-118
    • Bussmann, L.E.1    Deis, R.P.2
  • 19
    • 0021033608 scopus 로고
    • Effect of estrogen and placental lactogen on lactogenesis in pregnant rats
    • Bussmann LE, Koninckx A, Deis RP. Effect of estrogen and placental lactogen on lactogenesis in pregnant rats. Biol Reprod 1983; 29:535-541.
    • (1983) Biol Reprod , vol.29 , pp. 535-541
    • Bussmann, L.E.1    Koninckx, A.2    Deis, R.P.3
  • 20
    • 0014243153 scopus 로고
    • Oxytocin test to demonstrate the initiation and end of lactation in the rat
    • Deis RP. Oxytocin test to demonstrate the initiation and end of lactation in the rat. J Endocrinol 1968; 40:133-134.
    • (1968) J Endocrinol , vol.40 , pp. 133-134
    • Deis, R.P.1
  • 21
    • 0024465898 scopus 로고
    • Suckling-induced prolactin release potentiates RU 486-induced lactogenesis in pregnant rats
    • Deis RP, Carrizo DG, Jahn GA. Suckling-induced prolactin release potentiates RU 486-induced lactogenesis in pregnant rats. J Reprod Fertil 1989; 87:147-153.
    • (1989) J Reprod Fertil , vol.87 , pp. 147-153
    • Deis, R.P.1    Carrizo, D.G.2    Jahn, G.A.3
  • 22
    • 0027993792 scopus 로고
    • Lactogenic actions of different GHs in pregnant and lactating rats
    • Carón RW, Jahn GA, Deis RP. Lactogenic actions of different GHs in pregnant and lactating rats. J Endocrinol 1994; 142:535-545.
    • (1994) J Endocrinol , vol.142 , pp. 535-545
    • Carón, R.W.1    Jahn, G.A.2    Deis, R.P.3
  • 23
    • 0021349721 scopus 로고
    • Differential biological activities between mono- and bivalent fragments of anti-prolactin receptor antibodies
    • Dusanter-Fourt I, Djiane J, Kelly PA, Houdebine LM, Teyssot B. Differential biological activities between mono- and bivalent fragments of anti-prolactin receptor antibodies. Endocrinology 1984; 114:1021-1027.
    • (1984) Endocrinology , vol.114 , pp. 1021-1027
    • Dusanter-Fourt, I.1    Djiane, J.2    Kelly, P.A.3    Houdebine, L.M.4    Teyssot, B.5
  • 24
    • 0028901527 scopus 로고
    • The rabbit mammary gland prolactin receptor is tyrosine phosphorylated in response to prolactin in vivo and in vitro
    • Waters MJ, Daniel N, Bignon C, Djiane J. The rabbit mammary gland prolactin receptor is tyrosine phosphorylated in response to prolactin in vivo and in vitro. J Biol Chem 1995; 270:5136-5143.
    • (1995) J Biol Chem , vol.270 , pp. 5136-5143
    • Waters, M.J.1    Daniel, N.2    Bignon, C.3    Djiane, J.4
  • 25
    • 0026769565 scopus 로고
    • A rapid method for the isolation of DNA-binding proteins from purified nuclei of tissues and cells in culture
    • Hagenbüchle O, Wellauer PK. A rapid method for the isolation of DNA-binding proteins from purified nuclei of tissues and cells in culture. Nucleic Acids Res 1992; 20:3555-3559.
    • (1992) Nucleic Acids Res , vol.20 , pp. 3555-3559
    • Hagenbüchle, O.1    Wellauer, P.K.2
  • 26
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam JD, Lebovitz RM, Roeder RG. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res 1983; 11:1474-1489.
    • (1983) Nucleic Acids Res , vol.11 , pp. 1474-1489
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3
  • 27
    • 0025817299 scopus 로고
    • β-Casein gene promoter activity is regulated by the hormone-mediated relief of transcriptional repression and a mammary-gland-specific nuclear factor
    • Schmitt-Ney M, Doppler W, Ball RK, Groner B. β-Casein gene promoter activity is regulated by the hormone-mediated relief of transcriptional repression and a mammary-gland-specific nuclear factor. Mol Cell Biol 1991; 11:3745-3755.
    • (1991) Mol Cell Biol , vol.11 , pp. 3745-3755
    • Schmitt-Ney, M.1    Doppler, W.2    Ball, R.K.3    Groner, B.4
  • 28
    • 0028607387 scopus 로고
    • A combination of distal and proximal regions is required for efficient prolactin regulation of transfected rabbit αs 1-casein chloramphenicol acetyltransferase constructs
    • Pierre S, Jolivet G, Devinoy E, Houdebine LM. A combination of distal and proximal regions is required for efficient prolactin regulation of transfected rabbit αs 1-casein chloramphenicol acetyltransferase constructs. Mol Endocrinol 1994; 8:1720-1730.
    • (1994) Mol Endocrinol , vol.8 , pp. 1720-1730
    • Pierre, S.1    Jolivet, G.2    Devinoy, E.3    Houdebine, L.M.4
  • 29
    • 0027441586 scopus 로고
    • Acute-phase response factor, a nuclear factor binding to acute-phase response elements, is rapidly activated by interleukin-6 at the post-translational level
    • Wegenka UM, Buschmann J, Lutticken C, Heinrich PC, Horn F. Acute-phase response factor, a nuclear factor binding to acute-phase response elements, is rapidly activated by interleukin-6 at the post-translational level. Mol Cell Biol 1993; 13:276-288.
    • (1993) Mol Cell Biol , vol.13 , pp. 276-288
    • Wegenka, U.M.1    Buschmann, J.2    Lutticken, C.3    Heinrich, P.C.4    Horn, F.5
  • 30
    • 0028211553 scopus 로고
    • The signaling pathways of interleukin-6 and gamma Interferon converge by the activation of different transcription factors which bind to common responsive DNA elements
    • Yuan J, Wegenka UM, Lutticken C, Buschmann J, Decker T, Schindler C, Heinrich PC, Horn F. The signaling pathways of interleukin-6 and gamma Interferon converge by the activation of different transcription factors which bind to common responsive DNA elements. Mol Cell Biol 1994; 14:1657-1668.
    • (1994) Mol Cell Biol , vol.14 , pp. 1657-1668
    • Yuan, J.1    Wegenka, U.M.2    Lutticken, C.3    Buschmann, J.4    Decker, T.5    Schindler, C.6    Heinrich, P.C.7    Horn, F.8
  • 31
    • 0025639009 scopus 로고
    • The SIF binding element confers sis/PDGF inducibility onto the c-fos promoter
    • Wagner BJ, Hayes TE, Hoban CJ, Cochran BH. The SIF binding element confers sis/PDGF inducibility onto the c-fos promoter. EMBO J 1990; 9:4477-4484.
    • (1990) EMBO J , vol.9 , pp. 4477-4484
    • Wagner, B.J.1    Hayes, T.E.2    Hoban, C.J.3    Cochran, B.H.4
  • 32
    • 0027496114 scopus 로고
    • A common nuclear signal transduction pathway activated by growth factor and cytokine receptors
    • Sadowski HB, Shuai K, Darnell JE, Gilman MZ. A common nuclear signal transduction pathway activated by growth factor and cytokine receptors. Science 1993; 261:1739-1743.
    • (1993) Science , vol.261 , pp. 1739-1743
    • Sadowski, H.B.1    Shuai, K.2    Darnell, J.E.3    Gilman, M.Z.4
  • 33
    • 0023712739 scopus 로고
    • Phosphorylation-induced binding and transcriptional efficacy of nuclear factor CREB
    • Yamamoto KK, Gonzales GA, Biggs WH, Montminy MR. Phosphorylation-induced binding and transcriptional efficacy of nuclear factor CREB. Nature 1988; 334:494-498.
    • (1988) Nature , vol.334 , pp. 494-498
    • Yamamoto, K.K.1    Gonzales, G.A.2    Biggs, W.H.3    Montminy, M.R.4
  • 34
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P, Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 1987; 162:156-159.
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 35
    • 0025137467 scopus 로고
    • An improvement of the single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Puissant C, Houdebine L-M. An improvement of the single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Biotechniques 1990; 8:148-149.
    • (1990) Biotechniques , vol.8 , pp. 148-149
    • Puissant, C.1    Houdebine, L.-M.2
  • 36
    • 0018600137 scopus 로고
    • Rapid down regulation of prolactin receptors in mammary gland and liver
    • Djiane J, Clauser H, Kelly PA. Rapid down regulation of prolactin receptors in mammary gland and liver. Biochem Biophys Res Commun 1979; 90:1371-1378.
    • (1979) Biochem Biophys Res Commun , vol.90 , pp. 1371-1378
    • Djiane, J.1    Clauser, H.2    Kelly, P.A.3
  • 37
    • 0028217452 scopus 로고
    • Mammary gland factor (MGF) is a novel member of the cytokine regulated transcription factor gene family and confers the prolactin response
    • Wakao H, Gouilleux F, Groner B, Mammary gland factor (MGF) is a novel member of the cytokine regulated transcription factor gene family and confers the prolactin response. EMBO J 1994; 13:2182-2191.
    • (1994) EMBO J , vol.13 , pp. 2182-2191
    • Wakao, H.1    Gouilleux, F.2    Groner, B.3
  • 38
    • 8944247747 scopus 로고    scopus 로고
    • Growth hormone stimulates tyrosine phosphorylation of JAK2 and STAT5, but not insulin receptor substrate-1 or SHC proteins in liver and skeletal muscle of normal rats in vivo
    • Chow JC, Ling PR, Zhensheng Q, Laviola L, Ciccarones A, Bistrian BR, Smith RJ. Growth hormone stimulates tyrosine phosphorylation of JAK2 and STAT5, but not insulin receptor substrate-1 or SHC proteins in liver and skeletal muscle of normal rats in vivo. Endocrinology 1996; 137:2880-2886.
    • (1996) Endocrinology , vol.137 , pp. 2880-2886
    • Chow, J.C.1    Ling, P.R.2    Zhensheng, Q.3    Laviola, L.4    Ciccarones, A.5    Bistrian, B.R.6    Smith, R.J.7
  • 39
    • 0030013232 scopus 로고    scopus 로고
    • Modulation of growth factor receptor function by isoform heterodimerization
    • Chang W-P, Clevenger CV. Modulation of growth factor receptor function by isoform heterodimerization. Proc Natl Acad Sci USA 1996; 93:5947-5952.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5947-5952
    • Chang, W.-P.1    Clevenger, C.V.2
  • 40
    • 0029032210 scopus 로고
    • Intermittent plasma growth hormone triggers tyrosine phosphorylation and nuclear translocation of a liver-expressed, stat 5-related DNA binding protein - Proposed role as an intracellular regulator of male-specific liver gene transcription
    • Waxman DJ, Ram PA, Park SH, Choi HK, Intermittent plasma growth hormone triggers tyrosine phosphorylation and nuclear translocation of a liver-expressed, stat 5-related DNA binding protein - proposed role as an intracellular regulator of male-specific liver gene transcription. J Biol Chem 1995; 270:13262-13270.
    • (1995) J Biol Chem , vol.270 , pp. 13262-13270
    • Waxman, D.J.1    Ram, P.A.2    Park, S.H.3    Choi, H.K.4
  • 41
    • 0027328016 scopus 로고
    • Correlation of growth hormone secretion during pregnancy with circulating prolactin in rats
    • Jahn GA, Rastrilla AM, Deis RP. Correlation of growth hormone secretion during pregnancy with circulating prolactin in rats. J Reprod Fertil 1993; 98:327-333.
    • (1993) J Reprod Fertil , vol.98 , pp. 327-333
    • Jahn, G.A.1    Rastrilla, A.M.2    Deis, R.P.3
  • 42
    • 0022182440 scopus 로고
    • Biological activities of binding site specific monoclonal antibodies to prolactin receptors of rabbit mammary gland
    • Djiane J, Dusanter-Fourt I, Katoh M, Kelly PA. Biological activities of binding site specific monoclonal antibodies to prolactin receptors of rabbit mammary gland. J Biol Chem 1985; 260:11430-11435.
    • (1985) J Biol Chem , vol.260 , pp. 11430-11435
    • Djiane, J.1    Dusanter-Fourt, I.2    Katoh, M.3    Kelly, P.A.4
  • 43
    • 0029012232 scopus 로고
    • Prolactin receptor antagonists that inhibit the growth of breast cancer cell lines
    • Fuh G, Wells JA. Prolactin receptor antagonists that inhibit the growth of breast cancer cell lines. J Biol Chem 1995; 270:13133-13137.
    • (1995) J Biol Chem , vol.270 , pp. 13133-13137
    • Fuh, G.1    Wells, J.A.2
  • 44
    • 0027536507 scopus 로고
    • Mechanism-based design of prolactin receptor antagonists
    • Fuh G, Colosi P, Wood WI, Wells JA. Mechanism-based design of prolactin receptor antagonists. J Biol Chem 1993; 268:5376-5381.
    • (1993) J Biol Chem , vol.268 , pp. 5376-5381
    • Fuh, G.1    Colosi, P.2    Wood, W.I.3    Wells, J.A.4
  • 45
    • 0030013632 scopus 로고    scopus 로고
    • Cloning and characterisation of an ovarian-specific protein that associates with the short form of the prolactin receptor
    • Duan WR, Linzer DI, Gibori G. Cloning and characterisation of an ovarian-specific protein that associates with the short form of the prolactin receptor. J Biol Chem 1996; 271:15602-15607.
    • (1996) J Biol Chem , vol.271 , pp. 15602-15607
    • Duan, W.R.1    Linzer, D.I.2    Gibori, G.3


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