메뉴 건너뛰기




Volumn 42, Issue 24, 2003, Pages 7561-7570

Different biological effects of unmodified prolactin and a molecular mimic of phosphorylated prolactin involve different signaling pathways

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHORYLATION;

EID: 0038408583     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi034217s     Document Type: Article
Times cited : (46)

References (39)
  • 1
    • 0036037290 scopus 로고    scopus 로고
    • Pseudophosphorylated prolactin (S179D PRL) inhibits growth and promotes β-casein gene expression in the rat mammary gland
    • Kuo, C. B., Wu, W., Xu, X., Yang, L., Chen, C., Coss, D., Birdsall, B., Nasseri, D., and Walker, A. M. (2002) Pseudophosphorylated prolactin (S179D PRL) inhibits growth and promotes β-casein gene expression in the rat mammary gland, Cell Tissue Res. 309, 429-437.
    • (2002) Cell Tissue Res. , vol.309 , pp. 429-437
    • Kuo, C.B.1    Wu, W.2    Xu, X.3    Yang, L.4    Chen, C.5    Coss, D.6    Birdsall, B.7    Nasseri, D.8    Walker, A.M.9
  • 2
    • 0033303811 scopus 로고    scopus 로고
    • Dissociation of Janus kinase 2 and signal transducer and activator of transcription 5 activation after treatment of Nb2 cells with a molecular mimic of phosphorylated prolactin
    • Coss, D., Kuo, C. B., Yang, L., Ingleton, P., Luben, R., and Walker, A. M. (1999) Dissociation of Janus kinase 2 and signal transducer and activator of transcription 5 activation after treatment of Nb2 cells with a molecular mimic of phosphorylated prolactin, Endocrinology 140, 5087-5094.
    • (1999) Endocrinology , vol.140 , pp. 5087-5094
    • Coss, D.1    Kuo, C.B.2    Yang, L.3    Ingleton, P.4    Luben, R.5    Walker, A.M.6
  • 3
    • 0025837418 scopus 로고
    • A prolactin-dependent immune cell line (Nb2) expresses a mutant form of prolactin receptor
    • Ali, S., Pellegrini, I., and Kelly, P. A. (1991) A prolactin-dependent immune cell line (Nb2) expresses a mutant form of prolactin receptor, J. Biol. Chem. 266, 20110-20117.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20110-20117
    • Ali, S.1    Pellegrini, I.2    Kelly, P.A.3
  • 4
    • 0028200640 scopus 로고
    • Tissue distribution and regulation of rat prolactin receptor gene expression. Quantitative analysis by polymerase chain reaction
    • Nagano, M., and Kelly, P. A. (1994) Tissue distribution and regulation of rat prolactin receptor gene expression. Quantitative analysis by polymerase chain reaction, J. Biol. Chem. 269, 13337-13345.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13337-13345
    • Nagano, M.1    Kelly, P.A.2
  • 6
    • 0028956974 scopus 로고
    • Proline-rich sequence-mediated Jak 2 association to the prolactin receptor is required but not sufficient for signal transduction
    • Lebrun, J. J., Ali, S., Ulrich, A., and Kelly, P. A. (1995) Proline-rich sequence-mediated Jak 2 association to the prolactin receptor is required but not sufficient for signal transduction, J. Biol. Chem. 270, 10664-10670.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10664-10670
    • Lebrun, J.J.1    Ali, S.2    Ulrich, A.3    Kelly, P.A.4
  • 7
  • 8
    • 0033967439 scopus 로고    scopus 로고
    • Effect of PRL on MAPK activation: Negative regulatory role of the C-terminal part of the PRL receptor
    • Goupille, O., Barnier, J. V., Guibert, B., Paly, J., and Djiane, J. (2000) Effect of PRL on MAPK activation: negative regulatory role of the C-terminal part of the PRL receptor, Mol. Cell. Endocrinol. 159, 133-146.
    • (2000) Mol. Cell. Endocrinol. , vol.159 , pp. 133-146
    • Goupille, O.1    Barnier, J.V.2    Guibert, B.3    Paly, J.4    Djiane, J.5
  • 9
    • 0029834929 scopus 로고    scopus 로고
    • Involvement of SHC, GRB2, SOS, and RAS in prolactin signal transduction in mam-mary epithelial cells
    • Das, R., and Vonderhaar, B. K. (1996) Involvement of SHC, GRB2, SOS, and RAS in prolactin signal transduction in mam-mary epithelial cells, Oncogene 13, 1139-1145.
    • (1996) Oncogene , vol.13 , pp. 1139-1145
    • Das, R.1    Vonderhaar, B.K.2
  • 10
    • 0002695172 scopus 로고    scopus 로고
    • Prolactin receptor signal transduction
    • (Horseman, N., Ed.), Kluwer Academic Press, Norwell, MA
    • Clevenger, C. V., Rycyzyn, M. A., Syed, F., and Kline, J. B. (2001) Prolactin receptor signal transduction, in Prolactin (Horseman, N., Ed.) pp 355-379, Kluwer Academic Press, Norwell, MA.
    • (2001) Prolactin , pp. 355-379
    • Clevenger, C.V.1    Rycyzyn, M.A.2    Syed, F.3    Kline, J.B.4
  • 11
    • 0031790107 scopus 로고    scopus 로고
    • Development of recombinant human prolactin receptor antagonists by molecular mimicry of the phosphorylated hormone
    • Chen, T. J., Kuo, C. B., Tsai, K. F., Liu, J. W., Chen, D. Y., and Walker, A. M. (1998) Development of recombinant human prolactin receptor antagonists by molecular mimicry of the phosphorylated hormone, Endocrinology 139, 609-616.
    • (1998) Endocrinology , vol.139 , pp. 609-616
    • Chen, T.J.1    Kuo, C.B.2    Tsai, K.F.3    Liu, J.W.4    Chen, D.Y.5    Walker, A.M.6
  • 12
    • 0030028521 scopus 로고    scopus 로고
    • Identification of the major site of rat prolactin phosphorylation as serine 177
    • Wang, Y. F., Liu, J. W., Mamidi, M., and Walker, A. M. (1996) Identification of the major site of rat prolactin phosphorylation as serine 177, J. Biol. Chem. 271, 2462-2469.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2462-2469
    • Wang, Y.F.1    Liu, J.W.2    Mamidi, M.3    Walker, A.M.4
  • 13
    • 0037181513 scopus 로고    scopus 로고
    • p21-apactivated protein kinase gamma-PAK in pituitary secretory granules phosphorylates prolactin
    • Tuazon, P. T., Lorenson, M. Y., Walker, A. M., and Traugh, J. A. (2002) p21-Activated protein kinase gamma-PAK in pituitary secretory granules phosphorylates prolactin, FEBS Lett. 515, 84-88.
    • (2002) FEBS Lett. , vol.515 , pp. 84-88
    • Tuazon, P.T.1    Lorenson, M.Y.2    Walker, A.M.3    Traugh, J.A.4
  • 14
    • 0024792738 scopus 로고
    • Common structural changes accompany the functional inactivation of HPr by seryl phosphorylation or by serine to aspartate substitution
    • Wittekind, M., Reizer, J., Deutscher, J., Saier, M. H., and Klevit, R. E. (1989) Common structural changes accompany the functional inactivation of HPr by seryl phosphorylation or by serine to aspartate substitution, Biochemistry 28, 9908-9912.
    • (1989) Biochemistry , vol.28 , pp. 9908-9912
    • Wittekind, M.1    Reizer, J.2    Deutscher, J.3    Saier, M.H.4    Klevit, R.E.5
  • 15
    • 0026128206 scopus 로고    scopus 로고
    • Epidermal growth factor receptor, platelet-derived growth factor receptor and C-erbB-2 receptor activation all promote growth, but have distinctive effects upon mouse mammary epithelial cell differentiation
    • Taverna, D., Groner, B., and Hynes, N. (1999) Epidermal growth factor receptor, platelet-derived growth factor receptor and C-erbB-2 receptor activation all promote growth, but have distinctive effects upon mouse mammary epithelial cell differentiation, Cell Growth Differ. 2, 145-154.
    • (1999) Cell Growth Differ. , vol.2 , pp. 145-154
    • Taverna, D.1    Groner, B.2    Hynes, N.3
  • 16
    • 0029731413 scopus 로고    scopus 로고
    • Lactogenic hormone activation of Stat5 and transcription of the beta-casein gene in mammary epithelial cells is independent of p42 ERK2 mitogen-activated protein kinase activity
    • Wartmann, M., Cella, N., Hofer, P., Groner, B., Liu, X., Hennighausen, L., and Hynes, N. E. (1996) Lactogenic hormone activation of Stat5 and transcription of the beta-casein gene in mammary epithelial cells is independent of p42 ERK2 mitogen-activated protein kinase activity, J. Biol. Chem. 271, 31863-31868.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31863-31868
    • Wartmann, M.1    Cella, N.2    Hofer, P.3    Groner, B.4    Liu, X.5    Hennighausen, L.6    Hynes, N.E.7
  • 17
    • 0029822055 scopus 로고    scopus 로고
    • Brca 2 is coordinately regulated with Brca1 during proliferation and differentiation in mammary epithelial cells
    • Rajan, J. V., Wang, M., Marquis, S. T., and Chodosh, L. A. (1996) Brca 2 is coordinately regulated with Brca1 during proliferation and differentiation in mammary epithelial cells, Proc. Natl. Acad. Sci. U.S.A. 93, 13078-13083.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 13078-13083
    • Rajan, J.V.1    Wang, M.2    Marquis, S.T.3    Chodosh, L.A.4
  • 18
    • 0027453895 scopus 로고
    • Secretion of specific nonphosphorylated and phosphorylated rat prolactin isoforms at different stages of the estrous cycle
    • Ho, T. W. C., Leong, F. S., Olaso, C. H., and Walker, A. M. (1993) Secretion of specific nonphosphorylated and phosphorylated rat prolactin isoforms at different stages of the estrous cycle, Neuroendocrinol. 58, 160-165.
    • (1993) Neuroendocrinol , vol.58 , pp. 160-165
    • Ho, T.W.C.1    Leong, F.S.2    Olaso, C.H.3    Walker, A.M.4
  • 19
    • 0027141169 scopus 로고
    • Secretion of phosphorylated and nonphosphorylated monomer prolactin isoforms during rat pregnancy and pseudopregnancy
    • Ho, T. W. C., Kawaminami, M., and Walker, A. M. (1993) Secretion of phosphorylated and nonphosphorylated monomer prolactin isoforms during rat pregnancy and pseudopregnancy, Endocrine J. 1, 435-439.
    • (1993) Endocrine J. , vol.1 , pp. 435-439
    • Ho, T.W.C.1    Kawaminami, M.2    Walker, A.M.3
  • 20
    • 0034615929 scopus 로고    scopus 로고
    • Stat 5a serine phosphorylation. Serine 779 is constitutively phosphorylated in the mammary gland, and serine 725 phosphorylation influences prolactin-stimulated in vitro DNA binding activity
    • Beuvink, I., Hess, D., Flotow, H., Hofsteenge, J., Groner, B., and Hynes, N. E. (2000) Stat 5a serine phosphorylation. Serine 779 is constitutively phosphorylated in the mammary gland, and serine 725 phosphorylation influences prolactin-stimulated in vitro DNA binding activity, J. Biol. Chem. 275, 10247-10255.
    • (2000) J. Biol. Chem. , vol.275 , pp. 10247-10255
    • Beuvink, I.1    Hess, D.2    Flotow, H.3    Hofsteenge, J.4    Groner, B.5    Hynes, N.E.6
  • 23
    • 0027515128 scopus 로고
    • Isolation and characterization of phosphorylated bovine prolactin
    • Kim, B. G., and Brooks, C. L. (1993) Isolation and characterization of phosphorylated bovine prolactin, Biochem. J. 296, 41-47.
    • (1993) Biochem. J. , vol.296 , pp. 41-47
    • Kim, B.G.1    Brooks, C.L.2
  • 24
    • 0028963516 scopus 로고
    • Expression of prolactin and prolactin receptor in human breast carcinoma. Evidence for an autocrine/paracrine loop
    • Clevenger, C. V., Chang, W. P., Ngo, W., Pasha, T. L. M., Montone, K., and Tomaszewski, J. E. (1995) Expression of prolactin and prolactin receptor in human breast carcinoma. Evidence for an autocrine/paracrine loop, Am. J. Pathol. 146, 695-705.
    • (1995) Am. J. Pathol. , vol.146 , pp. 695-705
    • Clevenger, C.V.1    Chang, W.P.2    Ngo, W.3    Pasha, T.L.M.4    Montone, K.5    Tomaszewski, J.E.6
  • 25
    • 0027792150 scopus 로고
    • Prolactin variants in term and preterm human milk: Altered structural characteristics, biological activity and immunoreactivity
    • Ellis, L., and Picciano, M. F. (1993) Prolactin variants in term and preterm human milk: altered structural characteristics, biological activity and immunoreactivity, Endocr. Regul. 27, 181-192.
    • (1993) Endocr. Regul. , vol.27 , pp. 181-192
    • Ellis, L.1    Picciano, M.F.2
  • 26
    • 0027426142 scopus 로고
    • Bioactive and immunoreactive variants of prolactin in milk and serum of lactating rats and their pups
    • Kacsoh, B., Veress, Z., Toth, B. E., Avery, L. M., and Grosvenor, C. E. (1993) Bioactive and immunoreactive variants of prolactin in milk and serum of lactating rats and their pups, J. Endocrinol. 13, 243-257.
    • (1993) J. Endocrinol. , vol.13 , pp. 243-257
    • Kacsoh, B.1    Veress, Z.2    Toth, B.E.3    Avery, L.M.4    Grosvenor, C.E.5
  • 27
    • 0020059615 scopus 로고
    • Estradiol inhibits prolactin induced alpha-lactalbumin production in normal primate mammary tissue in vitro
    • Kleinberg, D. L., Todd, J., Babitsky, G., and Greising, J. (1982) Estradiol inhibits prolactin induced alpha-lactalbumin production in normal primate mammary tissue in vitro, Endocrinology 110, 279-281.
    • (1982) Endocrinology , vol.110 , pp. 279-281
    • Kleinberg, D.L.1    Todd, J.2    Babitsky, G.3    Greising, J.4
  • 28
    • 0015417407 scopus 로고
    • The effect of progesterone on biosynthetic pathways in mammary tissue
    • Davis, J. W., Wilkman-Coffelt, J., and Eddington, C. L. (1972) The effect of progesterone on biosynthetic pathways in mammary tissue, Endocrinology 91, 1011-1019.
    • (1972) Endocrinology , vol.91 , pp. 1011-1019
    • Davis, J.W.1    Wilkman-Coffelt, J.2    Eddington, C.L.3
  • 29
    • 0037670687 scopus 로고    scopus 로고
    • Transcription factors, cofactors and target genes mediating prolactin signals
    • (Horseman, N, Ed.), Kluwer Academic Press, Norwell, MA
    • Shemanko, C. S., and Groner, B. (2001) Transcription factors, cofactors and target genes mediating prolactin signals, in Prolactin (Horseman, N, Ed.) pp 381-404, Kluwer Academic Press, Norwell, MA.
    • (2001) Prolactin , pp. 381-404
    • Shemanko, C.S.1    Groner, B.2
  • 30
    • 0028942656 scopus 로고
    • Requirement of serine phosphorylation for formation of STAT-promoter complexes
    • Zhang, J. J., Blenis, J., Li, H. C., Schindler, C., and Chen-Kiang, S. (1995) Requirement of serine phosphorylation for formation of STAT-promoter complexes, Science 267, 1990-1994.
    • (1995) Science , vol.267 , pp. 1990-1994
    • Zhang, J.J.1    Blenis, J.2    Li, H.C.3    Schindler, C.4    Chen-Kiang, S.5
  • 31
    • 0032515146 scopus 로고    scopus 로고
    • Differential control of the phosphorylation state of proline-juxtaposed serine residues Ser725 of Stat5a and Ser730 of Stat5b in prolactin-sensitive cells
    • Yamashita, H., Xu, J., Erwin, R. A., Farrar, W. L., Kirken, R. A., and Rui, H (1998) Differential control of the phosphorylation state of proline-juxtaposed serine residues Ser725 of Stat5a and Ser730 of Stat5b in prolactin-sensitive cells, J. Biol. Chem. 273, 30218-30224.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30218-30224
    • Yamashita, H.1    Xu, J.2    Erwin, R.A.3    Farrar, W.L.4    Kirken, R.A.5    Rui, H.6
  • 32
    • 0035215369 scopus 로고    scopus 로고
    • Serine phosphorylation of GH-activated signal transducer and activator of transcription 5a (STAT 5a) and STAT 5b: Impact on STAT 5 transcriptional activity
    • Park, S. H., Yamashita, H., Rui, H., and Waxman, D. J. (2001) Serine phosphorylation of GH-activated signal transducer and activator of transcription 5a (STAT 5a) and STAT 5b: impact on STAT 5 transcriptional activity, Mol. Endocrinol. 15, 2157-2171.
    • (2001) Mol. Endocrinol. , vol.15 , pp. 2157-2171
    • Park, S.H.1    Yamashita, H.2    Rui, H.3    Waxman, D.J.4
  • 34
    • 0022499493 scopus 로고
    • Transcriptional and posttranscriptional roles of glucocorticoid in the expression of the rat 25, 000 molecular weight casein gene
    • Chomczynski, P., Qasba, P., and Topper, Y. J. (1986) Transcriptional and posttranscriptional roles of glucocorticoid in the expression of the rat 25, 000 molecular weight casein gene, Biochem. Biophys. Res. Commun. 134, 812-818.
    • (1986) Biochem. Biophys. Res. Commun. , vol.134 , pp. 812-818
    • Chomczynski, P.1    Qasba, P.2    Topper, Y.J.3
  • 35
    • 0018097613 scopus 로고
    • Stabilization of casein mRNA by prolactin and glucocorticoids
    • Houdebine, L. M., Devinoy, E., and Delouis, C. (1978) Stabilization of casein mRNA by prolactin and glucocorticoids, Biochimie 60, 57-63.
    • (1978) Biochimie , vol.60 , pp. 57-63
    • Houdebine, L.M.1    Devinoy, E.2    Delouis, C.3
  • 36
    • 0024814831 scopus 로고
    • Hormonedependent beta-casein mRNA stabilization requires ongoing protein synthesis
    • Poyet, P., Henning, S. J., and Rosen, J. M. (1989) Hormonedependent beta-casein mRNA stabilization requires ongoing protein synthesis, Mol. Endocrinol. 3, 1961-1968.
    • (1989) Mol. Endocrinol. , vol.3 , pp. 1961-1968
    • Poyet, P.1    Henning, S.J.2    Rosen, J.M.3
  • 37
    • 0030754999 scopus 로고    scopus 로고
    • The short form of the prolactin (PRL) receptor silences PRL induction of the beta-casein gene promoter
    • Berlanga, J. J., Garcia-Ruiz, J. P., Perrot-Applanat, M., Kelly, P. A., and Edery, M. (1997) The short form of the prolactin (PRL) receptor silences PRL induction of the beta-casein gene promoter, Mol. Endocrinol. 11, 1449-1457.
    • (1997) Mol. Endocrinol. , vol.11 , pp. 1449-1457
    • Berlanga, J.J.1    Garcia-Ruiz, J.P.2    Perrot-Applanat, M.3    Kelly, P.A.4    Edery, M.5
  • 38
    • 0038386018 scopus 로고    scopus 로고
    • A short form of the prolactin receptor is able to rescue mammopoiesis in heterozygous prolactin receptor mice
    • in press
    • Binart, N., Imbert-Bollore, P., Baran, N., Viglietta, C., and Kelly, P. A. (2003) A short form of the prolactin receptor is able to rescue mammopoiesis in heterozygous prolactin receptor mice, Mol. Endocrinol, (in press).
    • (2003) Mol. Endocrinol.
    • Binart, N.1    Imbert-Bollore, P.2    Baran, N.3    Viglietta, C.4    Kelly, P.A.5
  • 39
    • 0030815430 scopus 로고    scopus 로고
    • The different forms of the prolactin receptor in the rat corpus luteum: Developmental expression and hormonal regulation in pregnancy
    • Telleria, C. M., Parmer, T. G., Zhong, L., Clarke, D. L., Albarracin, C. T., Duan, W. R., Linzer, D. I., and Gibori, G. (1997) The different forms of the prolactin receptor in the rat corpus luteum: developmental expression and hormonal regulation in pregnancy, Endocrinology 138, 4812-4820.
    • (1997) Endocrinology , vol.138 , pp. 4812-4820
    • Telleria, C.M.1    Parmer, T.G.2    Zhong, L.3    Clarke, D.L.4    Albarracin, C.T.5    Duan, W.R.6    Linzer, D.I.7    Gibori, G.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.