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Volumn 48, Issue 29, 2009, Pages 6887-6897

A molecular mimic of phosphorylated prolactin (S179D PRL) secreted by eukaryotic cells has a conformation with an increased positive surface charge compared to that of unmodified prolactin (Biochemistry (2009) 48, (6887) DOI: 10.1021/bi9004864);A molecular mimic of phosphorylated prolactin (S179D PRL) secreted by eukaryotic cells has a conformation with an increased positive surface charge compared to that of unmodified prolactin

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELL CULTURE; DIMERS; ESCHERICHIA COLI; LIGANDS; MAMMALS; MOLECULES;

EID: 67651210820     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi901399d     Document Type: Erratum
Times cited : (5)

References (48)
  • 1
    • 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
  • 2
    • 0345257112 scopus 로고    scopus 로고
    • Inhibition of prolactin (PRL)-induced proliferative signals in breast cancer cells by a molecular mimic of phosphorylated PRL, S179D PRL
    • Schroeder, M. D., Brockman, J. L., Walker, A. M., and Schuler, L. A. (2003) Inhibition of prolactin (PRL)-induced proliferative signals in breast cancer cells by a molecular mimic of phosphorylated PRL, S179D PRL. Endocrinology 144, 5300-5307.
    • (2003) Endocrinology , vol.144 , pp. 5300-5307
    • Schroeder, M.D.1    Brockman, J.L.2    Walker, A.M.3    Schuler, L.A.4
  • 3
    • 23844481360 scopus 로고    scopus 로고
    • S179D prolactin increases vitamin D receptor and p21 through upregulation of short 1b prolactin receptor in human prostate cancer cells
    • Wu, W., Ginsburg, E., Vonderhaar, B. K., and Walker, A. M. (2005) S179D prolactin increases vitamin D receptor and p21 through upregulation of short 1b prolactin receptor in human prostate cancer cells. Cancer Res. 65, 7509-7515.
    • (2005) Cancer Res , vol.65 , pp. 7509-7515
    • Wu, W.1    Ginsburg, E.2    Vonderhaar, B.K.3    Walker, A.M.4
  • 4
    • 0035881316 scopus 로고    scopus 로고
    • A molecular mimic of phosphorylated prolactin markedly reduced tumor incidence and size when DU145 human prostate cancer cells were grown in nude mice
    • Xu, X., Kreye, E., Kuo, C. B., and Walker, A. M. (2001) A molecular mimic of phosphorylated prolactin markedly reduced tumor incidence and size when DU145 human prostate cancer cells were grown in nude mice. Cancer Res. 61, 6098-6114.
    • (2001) Cancer Res , vol.61 , pp. 6098-6114
    • Xu, X.1    Kreye, E.2    Kuo, C.B.3    Walker, A.M.4
  • 6
    • 33748747780 scopus 로고    scopus 로고
    • S179D prolactin primarily uses the extrinsic pathway and mitogen-activated protein kinase signaling to induce apoptosis in human endothelial cells
    • Ueda, E. K., Lo, H. L., Bartolini, P., and Walker, A. M. (2006) S179D prolactin primarily uses the extrinsic pathway and mitogen-activated protein kinase signaling to induce apoptosis in human endothelial cells. Endocrinology 147, 4627-4637.
    • (2006) Endocrinology , vol.147 , pp. 4627-4637
    • Ueda, E.K.1    Lo, H.L.2    Bartolini, P.3    Walker, A.M.4
  • 7
    • 33750234935 scopus 로고    scopus 로고
    • Therapeutic potential of S179D prolactin: From prostate cancer to angioproliferative disorders: The first selective prolactin receptor modulator
    • Walker, A. M. (2006) Therapeutic potential of S179D prolactin: From prostate cancer to angioproliferative disorders: The first selective prolactin receptor modulator. Expert Opin. Invest. Drugs 15, 1257-1267.
    • (2006) Expert Opin. Invest. Drugs , vol.15 , pp. 1257-1267
    • Walker, A.M.1
  • 8
    • 34548286394 scopus 로고    scopus 로고
    • S179D Prolactin: Antagonistic Agony!
    • Walker, A. M. (2007) S179D Prolactin: Antagonistic Agony!. Mol. Cell. Endocrinol. 276, 1-9.
    • (2007) Mol. Cell. Endocrinol , vol.276 , pp. 1-9
    • Walker, A.M.1
  • 9
  • 10
    • 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.-Y. 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.-Y.B.2    Yang, L.3    Ingleton, P.4    Luben, R.5    Walker, A.M.6
  • 11
    • 17644413692 scopus 로고    scopus 로고
    • Unmodified prolactin (PRL) and S179D PRL-initiated bioluminescence resonance energy transfer between homo- and hetero-pairs of long and short human PRL receptors in living human cells
    • Tan, D., Johnson, D. A., Wu, W., Zeng, L., Chen, Y. H., Chen,W. Y., Vonderhaar, B. K., and Walker, A. M. (2005) Unmodified prolactin (PRL) and S179D PRL-initiated bioluminescence resonance energy transfer between homo- and hetero-pairs of long and short human PRL receptors in living human cells. Mol. Endocrinol. 19, 1291-1303.
    • (2005) Mol. Endocrinol , vol.19 , pp. 1291-1303
    • Tan, D.1    Johnson, D.A.2    Wu, W.3    Zeng, L.4    Chen, Y.H.5    Chen, W.Y.6    Vonderhaar, B.K.7    Walker, A.M.8
  • 12
    • 33745699690 scopus 로고    scopus 로고
    • Different forms of prolactin have opposing effects on the expression of cell cycle regulatory proteins in differentiated mammary epithelial cells
    • Wu, W., Chen, Y. H., Ueda, E., Tan, D., Bartolini, P., and Walker, A. M. (2006) Different forms of prolactin have opposing effects on the expression of cell cycle regulatory proteins in differentiated mammary epithelial cells. Oncol. Res. 16, 75-84.
    • (2006) Oncol. Res , vol.16 , pp. 75-84
    • Wu, W.1    Chen, Y.H.2    Ueda, E.3    Tan, D.4    Bartolini, P.5    Walker, A.M.6
  • 13
    • 0038408583 scopus 로고    scopus 로고
    • Different biological effects of unmodified prolactin and a molecular mimic of phosphorylated prolactin involve different signaling pathways
    • Wu, W., Coss, D., Lorenson,M. Y., Kuo, C. B., Xu, X., and Walker, A. M. (2003) Different biological effects of unmodified prolactin and a molecular mimic of phosphorylated prolactin involve different signaling pathways. Biochemistry 42, 7561-7570.
    • (2003) Biochemistry , vol.42 , pp. 7561-7570
    • Wu, W.1    Coss, D.2    Lorenson, M.Y.3    Kuo, C.B.4    Xu, X.5    Walker, A.M.6
  • 14
    • 33746598625 scopus 로고    scopus 로고
    • Physico-chemical and biological characterizations of two human prolactin analogs exhibiting controversial bioactivity, synthesized in Chinese hamster ovary (CHO) cells
    • Soares, C. R., Glezer, A., Okazaki, K., Ueda, E. K., Heller, S. R., Walker, A. M., Goffin, V., and Bartolini, P. (2006) Physico-chemical and biological characterizations of two human prolactin analogs exhibiting controversial bioactivity, synthesized in Chinese hamster ovary (CHO) cells. Protein Expression Purif. 48, 182-194.
    • (2006) Protein Expression Purif , vol.48 , pp. 182-194
    • Soares, C.R.1    Glezer, A.2    Okazaki, K.3    Ueda, E.K.4    Heller, S.R.5    Walker, A.M.6    Goffin, V.7    Bartolini, P.8
  • 15
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard, L., and Helenius, A. (2003) Quality control in the endoplasmic reticulum. Nat. Rev. Mol. Cell Biol. 4, 181-191.
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 16
    • 0035854405 scopus 로고    scopus 로고
    • Ni(II)-based immobilized metal ion affinity chromatography of recombinant human prolactin from periplasmic Escherichia coli extracts
    • Ueda, E. K., Gout, P. W., and Morganti, L. (2001) Ni(II)-based immobilized metal ion affinity chromatography of recombinant human prolactin from periplasmic Escherichia coli extracts. J. Chromatogr., A 922, 165-175.
    • (2001) J. Chromatogr., A , vol.922 , pp. 165-175
    • Ueda, E.K.1    Gout, P.W.2    Morganti, L.3
  • 17
    • 1442286042 scopus 로고    scopus 로고
    • Periplasmic expression of human growth hormone via plasmid vectors containing the lambda PL promoter: Use of HPLC for product quantification
    • Soares, C. R., Gomide, F. I., Ueda, E. K., and Bartolini, P. (2003) Periplasmic expression of human growth hormone via plasmid vectors containing the lambda PL promoter: Use of HPLC for product quantification. Protein Eng. 16, 1131-1138.
    • (2003) Protein Eng , vol.16 , pp. 1131-1138
    • Soares, C.R.1    Gomide, F.I.2    Ueda, E.K.3    Bartolini, P.4
  • 20
    • 0031963473 scopus 로고    scopus 로고
    • Synthesis and characterization of recombinant, authentic human prolactin secreted into the periplasmic space of Escherichia coli
    • Morganti, L., Soares, C. R., Affonso, R., Gout, P. W., and Bartolini, P. (1998) Synthesis and characterization of recombinant, authentic human prolactin secreted into the periplasmic space of Escherichia coli. Biotechnol. Appl. Biochem. 27 (Part 1), 63-70.
    • (1998) Biotechnol. Appl. Biochem , vol.27 , Issue.PART 1 , pp. 63-70
    • Morganti, L.1    Soares, C.R.2    Affonso, R.3    Gout, P.W.4    Bartolini, P.5
  • 21
    • 0037052825 scopus 로고    scopus 로고
    • Reversed-phase high-performance liquid chromatography method for the determination of prolactin in bacterial extracts and in its purified form
    • Soares, C. R., Camargo, I. M., Morganti, L., Gimbo, E., Oliveira, J. E., Legoux, R., Ferrara, P., and Bartolini, P. (2002) Reversed-phase high-performance liquid chromatography method for the determination of prolactin in bacterial extracts and in its purified form. J. Chromatogr., A 955, 229-236.
    • (2002) J. Chromatogr., A , vol.955 , pp. 229-236
    • Soares, C.R.1    Camargo, I.M.2    Morganti, L.3    Gimbo, E.4    Oliveira, J.E.5    Legoux, R.6    Ferrara, P.7    Bartolini, P.8
  • 22
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network
    • Andrade, M. A., Chacon, P., Merelo, J. J., and Moran, F. (1993) Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network. Protein Eng. 6, 383-390.
    • (1993) Protein Eng , vol.6 , pp. 383-390
    • Andrade, M.A.1    Chacon, P.2    Merelo, J.J.3    Moran, F.4
  • 25
    • 0032963955 scopus 로고    scopus 로고
    • Heparin-binding property of human prolactin: A novel aspect of prolactin biology
    • Khurana, S., Kuns, R., and Ben-Jonathan, N. (1999) Heparin-binding property of human prolactin: A novel aspect of prolactin biology. Endocrinology 140, 1026-1029.
    • (1999) Endocrinology , vol.140 , pp. 1026-1029
    • Khurana, S.1    Kuns, R.2    Ben-Jonathan, N.3
  • 26
    • 34250860714 scopus 로고    scopus 로고
    • Enzymes catalyzing protein folding and their cellular functions
    • Nagradova, N. (2007) Enzymes catalyzing protein folding and their cellular functions. Curr. Protein Pept. Sci. 8, 273-282.
    • (2007) Curr. Protein Pept. Sci , vol.8 , pp. 273-282
    • Nagradova, N.1
  • 27
    • 0029828233 scopus 로고    scopus 로고
    • Strategies for achieving high-level expression of genes in Escherichia coli
    • Makrides, S. C. (1996) Strategies for achieving high-level expression of genes in Escherichia coli. Microbiol. Rev. 60, 512-538.
    • (1996) Microbiol. Rev , vol.60 , pp. 512-538
    • Makrides, S.C.1
  • 28
    • 0348195963 scopus 로고    scopus 로고
    • Construction of high-density display of CD147 ectodomain on VCSM13 phage via gpVIII: Effects of temperature, IPTG, and helper phage infection period
    • Intasai, N., Arooncharus, P., Kasinrerk, W., and Tayapiwatana, C. (2003) Construction of high-density display of CD147 ectodomain on VCSM13 phage via gpVIII: Effects of temperature, IPTG, and helper phage infection period. Protein Expression Purif. 32, 323-331.
    • (2003) Protein Expression Purif , vol.32 , pp. 323-331
    • Intasai, N.1    Arooncharus, P.2    Kasinrerk, W.3    Tayapiwatana, C.4
  • 29
    • 0033598777 scopus 로고    scopus 로고
    • Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm
    • Bessette, P. H., Aslund, F., Beckwith, J., and Georgiou, G. (1999) Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm. Proc. Natl. Acad. Sci. U.S.A. 96, 13703-13708.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 13703-13708
    • Bessette, P.H.1    Aslund, F.2    Beckwith, J.3    Georgiou, G.4
  • 30
    • 36048993741 scopus 로고    scopus 로고
    • Distinct human prolactin (hPRL) and growth hormone (hGH) behavior under bacteriophage lambda PL promoter control: Temperature plays a major role in protein yields
    • Soares, C. R., Ueda, E. K., Oliveira, T. L., Gomide, F. I., Heller, S. R., and Bartolini, P. (2008) Distinct human prolactin (hPRL) and growth hormone (hGH) behavior under bacteriophage lambda PL promoter control: Temperature plays a major role in protein yields. J. Biotechnol. 133, 27-35.
    • (2008) J. Biotechnol , vol.133 , pp. 27-35
    • Soares, C.R.1    Ueda, E.K.2    Oliveira, T.L.3    Gomide, F.I.4    Heller, S.R.5    Bartolini, P.6
  • 31
    • 5044239177 scopus 로고    scopus 로고
    • Cathepsin D processes human prolactin into multiple 16K-like N-terminal fragments: Study of their antiangiogenic properties and physiological relevance
    • Piwnica, D., Touraine, P., Struman, I., Tabruyn, S., Bolbach, G., Clapp, C., Martial, J. A., Kelly, P. A., and Goffin, V. (2004) Cathepsin D processes human prolactin into multiple 16K-like N-terminal fragments: Study of their antiangiogenic properties and physiological relevance. Mol. Endocrinol. 18, 2522-2542.
    • (2004) Mol. Endocrinol , vol.18 , pp. 2522-2542
    • Piwnica, D.1    Touraine, P.2    Struman, I.3    Tabruyn, S.4    Bolbach, G.5    Clapp, C.6    Martial, J.A.7    Kelly, P.A.8    Goffin, V.9
  • 32
    • 38549103628 scopus 로고    scopus 로고
    • Protein quality control in the early secretory pathway
    • Anelli, T., and Sitia, R. (2008) Protein quality control in the early secretory pathway. EMBO J. 27, 315-327.
    • (2008) EMBO J , vol.27 , pp. 315-327
    • Anelli, T.1    Sitia, R.2
  • 33
    • 0024419338 scopus 로고
    • Biosynthesis of the secreted 24 kd isoforms of prolactin
    • Greenan, J. R., Balden, E., Ho, T. W. C., and Walker, A. M. (1989) Biosynthesis of the secreted 24 kd isoforms of prolactin. Endocrinology 125, 2041-2048.
    • (1989) Endocrinology , vol.125 , pp. 2041-2048
    • Greenan, J.R.1    Balden, E.2    Ho, T.W.C.3    Walker, A.M.4
  • 34
    • 0033601846 scopus 로고    scopus 로고
    • Prolactin kinase activity in bovine anterior pituitary sub-cellular fractions
    • Wicks, J. R., and Brooks, C. L. (1999) Prolactin kinase activity in bovine anterior pituitary sub-cellular fractions. Mol. Cell. Endocrinol. 147, 125-132.
    • (1999) Mol. Cell. Endocrinol , vol.147 , pp. 125-132
    • Wicks, J.R.1    Brooks, C.L.2
  • 35
    • 33344469275 scopus 로고    scopus 로고
    • Two wrongs can make a right: Dimers of prolactin and growth hormone receptor antagonists behave as agonists
    • Langenheim, J. F., Tan, D., Walker, A. M., and Chen, W. (2006) Two wrongs can make a right: Dimers of prolactin and growth hormone receptor antagonists behave as agonists. Mol. Endocrinol. 20, 661-674.
    • (2006) Mol. Endocrinol , vol.20 , pp. 661-674
    • Langenheim, J.F.1    Tan, D.2    Walker, A.M.3    Chen, W.4
  • 41
    • 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
  • 43
    • 0027995384 scopus 로고
    • Classification of acid denaturation of proteins: Intermediates and unfolded states
    • Fink,A. L., Calciano, L. J., Goto, Y., Kurotsu, T., and Palleros, D. R. (1994) Classification of acid denaturation of proteins: Intermediates and unfolded states. Biochemistry 33, 12504-12511.
    • (1994) Biochemistry , vol.33 , pp. 12504-12511
    • Fink, A.L.1    Calciano, L.J.2    Goto, Y.3    Kurotsu, T.4    Palleros, D.R.5
  • 44
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • Jennings, P. A., and Wright, P. E. (1993) Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science 262, 892-896.
    • (1993) Science , vol.262 , pp. 892-896
    • Jennings, P.A.1    Wright, P.E.2
  • 45
    • 0033871781 scopus 로고    scopus 로고
    • Protein folding intermediates and pathways studied by hydrogen exchange
    • Englander, S. W. (2000) Protein folding intermediates and pathways studied by hydrogen exchange. Annu. Rev. Biophys. Biomol. Struct. 29, 213-238.
    • (2000) Annu. Rev. Biophys. Biomol. Struct , vol.29 , pp. 213-238
    • Englander, S.W.1
  • 46
    • 33344472286 scopus 로고    scopus 로고
    • Antiangiogenesis in cancer therapy: Endostatin and its mechanisms of action
    • Folkman, J. (2006) Antiangiogenesis in cancer therapy: Endostatin and its mechanisms of action. Exp. Cell Res. 312, 594-607.
    • (2006) Exp. Cell Res , vol.312 , pp. 594-607
    • Folkman, J.1
  • 47
    • 0029131388 scopus 로고
    • Enhanced activity of the bacteriophage lambda PL promoter at low temperature
    • Giladi, H., Goldenberg, D., Koby, S., and Oppenheim, A. B. (1995) Enhanced activity of the bacteriophage lambda PL promoter at low temperature. FEMS Microbiol. Rev. 17, 135-140.
    • (1995) FEMS Microbiol. Rev , vol.17 , pp. 135-140
    • Giladi, H.1    Goldenberg, D.2    Koby, S.3    Oppenheim, A.B.4
  • 48
    • 0024506674 scopus 로고
    • Bioactive recombinant methionyl bovine prolactin: Structure-function studies using site-specific mutagenesis
    • Luck,D. N., Gout, P. W., Beer, C. T., and Smith, M. (1989) Bioactive recombinant methionyl bovine prolactin: Structure-function studies using site-specific mutagenesis. Mol. Endocrinol. 3, 822-831.
    • (1989) Mol. Endocrinol , vol.3 , pp. 822-831
    • Luck, D.N.1    Gout, P.W.2    Beer, C.T.3    Smith, M.4


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