메뉴 건너뛰기




Volumn 28, Issue 2, 2003, Pages 252-258

Expression and purification of the angiogenesis inhibitor 16-kDa prolactin fragment from insect cells

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI; INSECTA;

EID: 0038057564     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1046-5928(02)00639-3     Document Type: Article
Times cited : (33)

References (22)
  • 1
    • 0030451788 scopus 로고    scopus 로고
    • Extrapituitary prolactin: Distribution, regulation, function and clinical aspects
    • N. Ben-Jonathan, J.L. Mershon, D.L. Allen, R.W. Steinmetz, Extrapituitary prolactin: distribution, regulation, function and clinical aspects, Endocr. Rev. 17 (1996) 639-669.
    • (1996) Endocr. Rev. , vol.17 , pp. 639-669
    • Ben-Jonathan, N.1    Mershon, J.L.2    Allen, D.L.3    Steinmetz, R.W.4
  • 2
    • 0032460226 scopus 로고    scopus 로고
    • Prolactin and its receptor: Actions, signal transduction pathways and phenotypes observed in PRL receptor knockout mice
    • C. Bole-Feysot, V. Goffin, M. Edery, N. Binart, P.A. Kelly, Prolactin and its receptor: actions, signal transduction pathways and phenotypes observed in PRL receptor knockout mice, Endocr. Rev. 19 (1998) 225-268.
    • (1998) Endocr. Rev. , vol.19 , pp. 225-268
    • Bole-Feysot, C.1    Goffin, V.2    Edery, M.3    Binart, N.4    Kelly, P.A.5
  • 3
    • 0029035666 scopus 로고
    • Structural variants of prolactin: Occurrence and physiological significance
    • Y.N. Sinha, Structural variants of prolactin: occurrence and physiological significance, Endocr. Rev. 16 (1995) 354-369.
    • (1995) Endocr. Rev. , vol.16 , pp. 354-369
    • Sinha, Y.N.1
  • 4
    • 0027220451 scopus 로고
    • Mass spectrometric analysis of the fragments produced by cleavage and reduction of rat prolactin: Evidence that the cleaving enzyme is cathepsin D
    • R.A. Baldocchi, L. Tan, D.S. King, C.S. Nicoll, Mass spectrometric analysis of the fragments produced by cleavage and reduction of rat prolactin: evidence that the cleaving enzyme is cathepsin D, Endocrinology 133 (1993) 935-938.
    • (1993) Endocrinology , vol.133 , pp. 935-938
    • Baldocchi, R.A.1    Tan, L.2    King, D.S.3    Nicoll, C.S.4
  • 5
    • 0027236943 scopus 로고
    • The 16-kilodalton N-terminal fragment of human prolactin is a potent inhibitor of angiogenesis
    • C. Clapp, J.A. Martial, R.C. Guzman, F. Rentier-Delrue, R.I. Weiner, The 16-kilodalton N-terminal fragment of human prolactin is a potent inhibitor of angiogenesis, Endocrinology 133 (1993) 1292-1299.
    • (1993) Endocrinology , vol.133 , pp. 1292-1299
    • Clapp, C.1    Martial, J.A.2    Guzman, R.C.3    Rentier-Delrue, F.4    Weiner, R.I.5
  • 6
    • 0025949596 scopus 로고
    • The 16K fragment of prolactin specifically inhibits basal or fibroblast growth factor stimulated growth of capillary endothelial cells
    • N. Ferrara, C. Clapp, R. Weiner, The 16K fragment of prolactin specifically inhibits basal or fibroblast growth factor stimulated growth of capillary endothelial cells, Endocrinology 129 (1991) 896-900.
    • (1991) Endocrinology , vol.129 , pp. 896-900
    • Ferrara, N.1    Clapp, C.2    Weiner, R.3
  • 7
    • 0033573994 scopus 로고    scopus 로고
    • Opposing actions of intact and N-terminal fragments of the human prolactin/growth hormone family members on angiogenesis: An efficient mechanism for the regulation of angiogenesis
    • I. Struman, F. Bentzien, H. Lee, V. Mainfroid, G. D'Angelo, V. Goffin, R.I. Weiner, J.A. Martial, Opposing actions of intact and N-terminal fragments of the human prolactin/growth hormone family members on angiogenesis: An efficient mechanism for the regulation of angiogenesis, Proc. Natl. Acad. Sci. USA 96 (1999) 1246-1251.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1246-1251
    • Struman, I.1    Bentzien, F.2    Lee, H.3    Mainfroid, V.4    D'Angelo, G.5    Goffin, V.6    Weiner, R.I.7    Martial, J.A.8
  • 9
    • 0020564153 scopus 로고
    • Proteolytic fragmentation of rat prolactin by the rat ventral prostate gland
    • M.M. Compton, R.J. Witorsch, Proteolytic fragmentation of rat prolactin by the rat ventral prostate gland, Prostate 4 (1983) 231-246.
    • (1983) Prostate , vol.4 , pp. 231-246
    • Compton, M.M.1    Witorsch, R.J.2
  • 10
    • 0021200477 scopus 로고
    • Proteolytic degradation and modification of rat prolactin by subcellular fractions of the rat ventral prostate gland
    • M.M. Compton, R.J. Witorsch, Proteolytic degradation and modification of rat prolactin by subcellular fractions of the rat ventral prostate gland, Endocrinology 115 (1984) 476-484.
    • (1984) Endocrinology , vol.115 , pp. 476-484
    • Compton, M.M.1    Witorsch, R.J.2
  • 11
    • 0023568445 scopus 로고
    • Analysis of the proteolytic cleavage of prolactin by the mammary gland and liver of the rat. Characterization of the cleaved and 16k forms
    • C. Clapp, Analysis of the proteolytic cleavage of prolactin by the mammary gland and liver of the rat. Characterization of the cleaved and 16k forms, Endocrinology 121 (1987) 2055-2064.
    • (1987) Endocrinology , vol.121 , pp. 2055-2064
    • Clapp, C.1
  • 13
    • 0022634695 scopus 로고
    • Proteolytic modification of rat prolactin by subcellular fractions of the lactating rat mammary gland
    • V.L. Wong, M.M. Compton, R.J. Witorsch, Proteolytic modification of rat prolactin by subcellular fractions of the lactating rat mammary gland, Biochim. Biophys. Acta 881 (1986) 167-174.
    • (1986) Biochim. Biophys. Acta , vol.881 , pp. 167-174
    • Wong, V.L.1    Compton, M.M.2    Witorsch, R.J.3
  • 14
    • 0023652134 scopus 로고
    • Biological, immunological and biochemical characterization of cleaved prolactin generated by lactating mammary gland
    • R.S. Vick, V.L. Wong, R.J. Witorsch, Biological, immunological and biochemical characterization of cleaved prolactin generated by lactating mammary gland, Biochim. Biophys. Acta 931 (1987) 196-204.
    • (1987) Biochim. Biophys. Acta , vol.931 , pp. 196-204
    • Vick, R.S.1    Wong, V.L.2    Witorsch, R.J.3
  • 15
    • 0026566153 scopus 로고
    • A specific, high affinity, saturable binding site for the 16-kilodalton fragment of prolactin on capillary endothelial cells
    • C. Clapp, R.I. Weiner, A specific, high affinity, saturable binding site for the 16-kilodalton fragment of prolactin on capillary endothelial cells, Endocrinology 130 (1992) 1380-1386.
    • (1992) Endocrinology , vol.130 , pp. 1380-1386
    • Clapp, C.1    Weiner, R.I.2
  • 16
    • 0029071065 scopus 로고
    • Activation of mitogen-activated protein kinases by vascular endothelial growth factor and basic fibroblast growth factor in capillary endothelial cells is inhibited by the antiangiogenic factor 16-kDa N-terminal fragment of prolactin
    • G.D. D'Angelo, I. Struman, J. Martial, R.I. Weiner, Activation of mitogen-activated protein kinases by vascular endothelial growth factor and basic fibroblast growth factor in capillary endothelial cells is inhibited by the antiangiogenic factor 16-kDa N-terminal fragment of prolactin, Proc. Natl. Acad. Sci. USA 92 (1995) 6374-6378.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6374-6378
    • D'Angelo, G.D.1    Struman, I.2    Martial, J.3    Weiner, R.I.4
  • 17
    • 0031730107 scopus 로고    scopus 로고
    • Inhibition of urokinase activity by the antiangiogenic factor 16k prolactin: Activation of plasminogen activator inhibitor I expression
    • H. Lee, I. Struman, C. Clapp, J. Martial, R.I. Weiner, Inhibition of urokinase activity by the antiangiogenic factor 16k prolactin: activation of plasminogen activator inhibitor I expression, Endocrinology 139 (1998) 3696-3703.
    • (1998) Endocrinology , vol.139 , pp. 3696-3703
    • Lee, H.1    Struman, I.2    Clapp, C.3    Martial, J.4    Weiner, R.I.5
  • 18
    • 0033768751 scopus 로고    scopus 로고
    • The antiangiogenic factor 16K PRL induces programmed cell death in endothelial cells by caspase activation
    • J.-F. Martini, C. Piot, L.M. Humeau, I. Struman, J.A. Martial, R.I. Weiner, The antiangiogenic factor 16K PRL induces programmed cell death in endothelial cells by caspase activation, Mol. Endocrinol. 14 (2000) 1536-1549.
    • (2000) Mol. Endocrinol. , vol.14 , pp. 1536-1549
    • Martini, J.-F.1    Piot, C.2    Humeau, L.M.3    Struman, I.4    Martial, J.A.5    Weiner, R.I.6
  • 19
    • 0029035666 scopus 로고
    • Structural variants of prolactin: Occurrence and physiological significance
    • Y.N. Sinha, Structural variants of prolactin: occurrence and physiological significance, Endocr. Rev. 16 (1995) 354-369.
    • (1995) Endocr. Rev. , vol.16 , pp. 354-369
    • Sinha, Y.N.1
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227 (1970) 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0036305590 scopus 로고    scopus 로고
    • TIRAP mediates endotoxin-induced NF-kappaB activation and apoptosis in endothelial cells
    • D.D. Bannerman, R.D. Erwert, R.K. Winn, J.M. Harlan, TIRAP mediates endotoxin-induced NF-kappaB activation and apoptosis in endothelial cells, Biochem. Biophys. Res. Commun. 295 (2002) 157-162.
    • (2002) Biochem. Biophys. Res. Commun. , vol.295 , pp. 157-162
    • Bannerman, D.D.1    Erwert, R.D.2    Winn, R.K.3    Harlan, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.