메뉴 건너뛰기




Volumn 69, Issue 12, 2005, Pages 1723-1732

Real-time measurement in living cells of insulin-like growth factor activity using bioluminescence resonance energy transfer

Author keywords

Bioluminescence resonance energy transfer; Insulin; Insulin like growth factor; Insulin like growth factor binding proteins; Receptor

Indexed keywords

ENHANCED YELLOW FLUORESCENT PROTEIN; FLUOROPHOSPHATE; INSULIN RECEPTOR; LUCIFERASE; PROTEINASE; SOMATOMEDIN; SOMATOMEDIN BINDING PROTEIN; SOMATOMEDIN RECEPTOR; UNCLASSIFIED DRUG; YELLOW FLUORESCENT PROTEIN;

EID: 20344390240     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2005.04.005     Document Type: Article
Times cited : (10)

References (35)
  • 1
    • 0028958031 scopus 로고
    • Insulin-like growth factors and their binding proteins: Biological actions
    • J.I. Jones, and D.R. Clemmons Insulin-like growth factors and their binding proteins: biological actions Endocrnol Rev 16 1 1995 3 34
    • (1995) Endocrnol Rev , vol.16 , Issue.1 , pp. 3-34
    • Jones, J.I.1    Clemmons, D.R.2
  • 2
    • 0035742583 scopus 로고    scopus 로고
    • Insulin and insulin-like growth factor I receptors: Similarities and differences in signal transduction
    • J. Dupont, and D. LeRoith Insulin and insulin-like growth factor I receptors: similarities and differences in signal transduction Horm Res 55 Suppl. 2 2001 22 26
    • (2001) Horm Res , vol.55 , Issue.SUPPL. 2 , pp. 22-26
    • Dupont, J.1    Leroith, D.2
  • 3
    • 0036905115 scopus 로고    scopus 로고
    • Cellular actions of the insulin-like growth factor binding proteins
    • S.M. Firth, and R.C. Baxter Cellular actions of the insulin-like growth factor binding proteins Endocr Rev 23 6 2002 824 854
    • (2002) Endocr Rev , vol.23 , Issue.6 , pp. 824-854
    • Firth, S.M.1    Baxter, R.C.2
  • 4
    • 0347087571 scopus 로고    scopus 로고
    • Deregulation of the IGF axis in cancer: Epidemiological evidence and potential therapeutic interventions
    • L. Jerome, L. Shiry, and B. Leyland-Jones Deregulation of the IGF axis in cancer: epidemiological evidence and potential therapeutic interventions Endocr Relat Cancer 10 4 2003 561 578
    • (2003) Endocr Relat Cancer , vol.10 , Issue.4 , pp. 561-578
    • Jerome, L.1    Shiry, L.2    Leyland-Jones, B.3
  • 5
    • 0038398622 scopus 로고    scopus 로고
    • The insulin-like growth factor system and cancer
    • D. LeRoith, and C.T. Roberts Jr. The insulin-like growth factor system and cancer Cancer Lett 195 2 2003 127 137
    • (2003) Cancer Lett , vol.195 , Issue.2 , pp. 127-137
    • Leroith, D.1    Roberts Jr., C.T.2
  • 7
    • 0036782071 scopus 로고    scopus 로고
    • Structural biology of insulin and IGF1 receptors: Implications for drug design
    • P. De Meyts, and J. Whittaker Structural biology of insulin and IGF1 receptors: implications for drug design Nat Rev Drug Discov 1 10 2002 769 783
    • (2002) Nat Rev Drug Discov , vol.1 , Issue.10 , pp. 769-783
    • De Meyts, P.1    Whittaker, J.2
  • 8
    • 0242624594 scopus 로고    scopus 로고
    • Growth factor receptors as therapeutic targets: Strategies to inhibit the insulin-like growth factor I receptor
    • E. Surmacz Growth factor receptors as therapeutic targets: strategies to inhibit the insulin-like growth factor I receptor Oncogene 22 42 2003 6589 6597
    • (2003) Oncogene , vol.22 , Issue.42 , pp. 6589-6597
    • Surmacz, E.1
  • 9
    • 3042775027 scopus 로고    scopus 로고
    • The insulin like growth factor-1 receptor (IGF-1R) as a drug target: Novel approaches to cancer therapy
    • C. Bahr, and B. Groner The insulin like growth factor-1 receptor (IGF-1R) as a drug target: novel approaches to cancer therapy Growth Horm IGF Res 14 4 2004 287 295
    • (2004) Growth Horm IGF Res , vol.14 , Issue.4 , pp. 287-295
    • Bahr, C.1    Groner, B.2
  • 10
    • 12144290914 scopus 로고    scopus 로고
    • Inhibition of the insulin-like growth factor receptor-1 tyrosine kinase activity as a therapeutic strategy for multiple myeloma, other hematologic malignancies, and solid tumors
    • C.S. Mitsiades, N.S. Mitsiades, C.J. McMullan, V. Poulaki, R. Shringarpure, and M. Akiyama Inhibition of the insulin-like growth factor receptor-1 tyrosine kinase activity as a therapeutic strategy for multiple myeloma, other hematologic malignancies, and solid tumors Cancer Cell 5 3 2004 221 230
    • (2004) Cancer Cell , vol.5 , Issue.3 , pp. 221-230
    • Mitsiades, C.S.1    Mitsiades, N.S.2    McMullan, C.J.3    Poulaki, V.4    Shringarpure, R.5    Akiyama, M.6
  • 11
    • 0032932822 scopus 로고    scopus 로고
    • Insulin receptor isoform A, a newly recognized, high-affinity insulin-like growth factor II receptor in fetal and cancer cells
    • F. Frasca, G. Pandini, P. Scalia, L. Sciacca, R. Mineo, and A. Costantino Insulin receptor isoform A, a newly recognized, high-affinity insulin-like growth factor II receptor in fetal and cancer cells Mol Cell Biol 19 5 1999 3278 3288
    • (1999) Mol Cell Biol , vol.19 , Issue.5 , pp. 3278-3288
    • Frasca, F.1    Pandini, G.2    Scalia, P.3    Sciacca, L.4    Mineo, R.5    Costantino, A.6
  • 13
    • 0036550234 scopus 로고    scopus 로고
    • Signalling through IGF-I and insulin receptors: Where is the specificity?
    • J.J. Kim, and D. Accili Signalling through IGF-I and insulin receptors: where is the specificity? Growth Horm IGF Res 12 2 2002 84 90
    • (2002) Growth Horm IGF Res , vol.12 , Issue.2 , pp. 84-90
    • Kim, J.J.1    Accili, D.2
  • 14
    • 0036121371 scopus 로고    scopus 로고
    • Regulation of insulin-like growth factor type I (IGF-I) receptor kinase activity by protein tyrosine phosphatase 1B (PTP-1B) and enhanced IGF-I-mediated suppression of apoptosis and motility in PTP-1B-deficient fibroblasts
    • D.A. Buckley, A. Cheng, P.A. Kiely, M.L. Tremblay, and R. O'Connor Regulation of insulin-like growth factor type I (IGF-I) receptor kinase activity by protein tyrosine phosphatase 1B (PTP-1B) and enhanced IGF-I-mediated suppression of apoptosis and motility in PTP-1B-deficient fibroblasts Mol Cell Biol 22 7 2002 1998 2010
    • (2002) Mol Cell Biol , vol.22 , Issue.7 , pp. 1998-2010
    • Buckley, D.A.1    Cheng, A.2    Kiely, P.A.3    Tremblay, M.L.4    O'Connor, R.5
  • 15
    • 1842424803 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase-1B dephosphorylation of the insulin receptor occurs in a perinuclear endosome compartment in human embryonic kidney 293 cells
    • Y. Romsicki, M. Reece, J.Y. Gauthier, E. Asante-Appiah, and B.P. Kennedy Protein tyrosine phosphatase-1B dephosphorylation of the insulin receptor occurs in a perinuclear endosome compartment in human embryonic kidney 293 cells J Biol Chem 279 13 2004 12868 12875
    • (2004) J Biol Chem , vol.279 , Issue.13 , pp. 12868-12875
    • Romsicki, Y.1    Reece, M.2    Gauthier, J.Y.3    Asante-Appiah, E.4    Kennedy, B.P.5
  • 16
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • S.N. Ho, H.D. Hunt, R.M. Horton, J.K. Pullen, and L.R. Pease Site-directed mutagenesis by overlap extension using the polymerase chain reaction Gene 77 1 1989 51 59
    • (1989) Gene , vol.77 , Issue.1 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 17
    • 0023084783 scopus 로고
    • Analysis of mutation in human cells by using an Epstein-Barr virus shuttle system
    • R.B. DuBridge, P. Tang, H.C. Hsia, P.M. Leong, J.H. Miller, and M.P. Calos Analysis of mutation in human cells by using an Epstein-Barr virus shuttle system Mol Cell Biol 7 1 1987 379 387
    • (1987) Mol Cell Biol , vol.7 , Issue.1 , pp. 379-387
    • Dubridge, R.B.1    Tang, P.2    Hsia, H.C.3    Leong, P.M.4    Miller, J.H.5    Calos, M.P.6
  • 18
    • 0027236954 scopus 로고
    • Production of high-titer helper-free retroviruses by transient transfection
    • W.S. Pear, G.P. Nolan, M.L. Scott, and D. Baltimore Production of high-titer helper-free retroviruses by transient transfection Proc Natl Acad Sci USA 90 18 1993 8392 8396
    • (1993) Proc Natl Acad Sci USA , vol.90 , Issue.18 , pp. 8392-8396
    • Pear, W.S.1    Nolan, G.P.2    Scott, M.L.3    Baltimore, D.4
  • 19
    • 0034724192 scopus 로고    scopus 로고
    • Detection of beta 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET)
    • S. Angers, A. Salahpour, E. Joly, S. Hilairet, D. Chelsky, and M. Dennis Detection of beta 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET) Proc Natl Acad Sci USA 97 7 2000 3684 3689
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.7 , pp. 3684-3689
    • Angers, S.1    Salahpour, A.2    Joly, E.3    Hilairet, S.4    Chelsky, D.5    Dennis, M.6
  • 20
    • 0035447508 scopus 로고    scopus 로고
    • Mutational analysis of the proteolytic domain of pregnancy-associated plasma protein-A (PAPP-A): Classification as a metzincin
    • H.B. Boldt, M.T. Overgaard, L.S. Laursen, K. Weyer, L. Sottrup-Jensen, and C. Oxvig Mutational analysis of the proteolytic domain of pregnancy-associated plasma protein-A (PAPP-A): classification as a metzincin Biochem J 358 Part 2 2001 359 367
    • (2001) Biochem J , vol.358 , Issue.PART 2 , pp. 359-367
    • Boldt, H.B.1    Overgaard, M.T.2    Laursen, L.S.3    Weyer, K.4    Sottrup-Jensen, L.5    Oxvig, C.6
  • 21
    • 0034613177 scopus 로고    scopus 로고
    • Expression of recombinant human pregnancy-associated plasma protein-A and identification of the proform of eosinophil major basic protein as its physiological inhibitor
    • M.T. Overgaard, J. Haaning, H.B. Boldt, I.M. Olsen, L.S. Laursen, and M. Christiansen Expression of recombinant human pregnancy-associated plasma protein-A and identification of the proform of eosinophil major basic protein as its physiological inhibitor J Biol Chem 275 40 2000 31128 31133
    • (2000) J Biol Chem , vol.275 , Issue.40 , pp. 31128-31133
    • Overgaard, M.T.1    Haaning, J.2    Boldt, H.B.3    Olsen, I.M.4    Laursen, L.S.5    Christiansen, M.6
  • 22
    • 0028032599 scopus 로고
    • Isolation and characterization of circulating complex between human pregnancy-associated plasma protein-A and proform of eosinophil major basic protein
    • C. Oxvig, O. Sand, T. Kristensen, L. Kristensen, and L. Sottrup-Jensen Isolation and characterization of circulating complex between human pregnancy-associated plasma protein-A and proform of eosinophil major basic protein Biochim Biophys Acta 1201 3 1994 415 423
    • (1994) Biochim Biophys Acta , vol.1201 , Issue.3 , pp. 415-423
    • Oxvig, C.1    Sand, O.2    Kristensen, T.3    Kristensen, L.4    Sottrup-Jensen, L.5
  • 23
    • 0026470979 scopus 로고
    • The insulin receptor activation process involves localized conformational changes
    • V. Baron, P. Kaliman, N. Gautier, and E. Van Obberghen The insulin receptor activation process involves localized conformational changes J Biol Chem 267 32 1992 23290 23294
    • (1992) J Biol Chem , vol.267 , Issue.32 , pp. 23290-23294
    • Baron, V.1    Kaliman, P.2    Gautier, N.3    Van Obberghen, E.4
  • 24
    • 0033524455 scopus 로고    scopus 로고
    • A bioluminescence resonance energy transfer (BRET) system: Application to interacting circadian clock proteins
    • Y. Xu, D.W. Piston, and C.H. Johnson A bioluminescence resonance energy transfer (BRET) system: application to interacting circadian clock proteins Proc Natl Acad Sci USA 96 1 1999 151 156
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.1 , pp. 151-156
    • Xu, Y.1    Piston, D.W.2    Johnson, C.H.3
  • 25
    • 0038170289 scopus 로고    scopus 로고
    • Applications of novel resonance energy transfer techniques to study dynamic hormone receptor interactions in living cells
    • K.A. Eidne, K.M. Kroeger, and A.C. Hanyaloglu Applications of novel resonance energy transfer techniques to study dynamic hormone receptor interactions in living cells Trends Endocrinol Metab 13 10 2002 415 421
    • (2002) Trends Endocrinol Metab , vol.13 , Issue.10 , pp. 415-421
    • Eidne, K.A.1    Kroeger, K.M.2    Hanyaloglu, A.C.3
  • 26
    • 0035798712 scopus 로고    scopus 로고
    • Insulin receptor substrate-1 pleckstrin homology and phosphotyrosine- binding domains are both involved in plasma membrane targeting
    • A.R. Jacobs, D. LeRoith, and S.I. Taylor Insulin receptor substrate-1 pleckstrin homology and phosphotyrosine-binding domains are both involved in plasma membrane targeting J Biol Chem 276 44 2001 40795 40802
    • (2001) J Biol Chem , vol.276 , Issue.44 , pp. 40795-40802
    • Jacobs, A.R.1    Leroith, D.2    Taylor, S.I.3
  • 27
    • 0031055324 scopus 로고    scopus 로고
    • Development of "substrate-trapping" mutants to identify physiological substrates of protein tyrosine phosphatases
    • A.J. Flint, T. Tiganis, D. Barford, and N.K. Tonks Development of "substrate-trapping" mutants to identify physiological substrates of protein tyrosine phosphatases Proc Natl Acad Sci USA 94 5 1997 1680 1685
    • (1997) Proc Natl Acad Sci USA , vol.94 , Issue.5 , pp. 1680-1685
    • Flint, A.J.1    Tiganis, T.2    Barford, D.3    Tonks, N.K.4
  • 28
    • 0036500994 scopus 로고    scopus 로고
    • Imaging sites of receptor dephosphorylation by PTP1B on the surface of the endoplasmic reticulum
    • F.G. Haj, P.J. Verveer, A. Squire, B.G. Neel, and P.I. Bastiaens Imaging sites of receptor dephosphorylation by PTP1B on the surface of the endoplasmic reticulum Science 295 5560 2002 1708 1711
    • (2002) Science , vol.295 , Issue.5560 , pp. 1708-1711
    • Haj, F.G.1    Verveer, P.J.2    Squire, A.3    Neel, B.G.4    Bastiaens, P.I.5
  • 29
    • 0034801960 scopus 로고    scopus 로고
    • Monitoring the activation state of the insulin receptor using bioluminescence resonance energy transfer
    • N. Boute, K. Pernet, and T. Issad Monitoring the activation state of the insulin receptor using bioluminescence resonance energy transfer Mol Pharmacol 60 4 2001 640 645
    • (2001) Mol Pharmacol , vol.60 , Issue.4 , pp. 640-645
    • Boute, N.1    Pernet, K.2    Issad, T.3
  • 30
    • 0037367940 scopus 로고    scopus 로고
    • Dynamics of the interaction between the insulin receptor and protein tyrosine-phosphatase 1B in living cells
    • N. Boute, S. Boubekeur, D. Lacasa, and T. Issad Dynamics of the interaction between the insulin receptor and protein tyrosine-phosphatase 1B in living cells EMBO Rep 4 3 2003 313 319
    • (2003) EMBO Rep , vol.4 , Issue.3 , pp. 313-319
    • Boute, N.1    Boubekeur, S.2    Lacasa, D.3    Issad, T.4
  • 31
    • 0032981399 scopus 로고    scopus 로고
    • The insulin-like growth factor (IGF)-dependent IGF binding protein-4 protease secreted by human fibroblasts is pregnancy-associated plasma protein-A
    • J.B. Lawrence, C. Oxvig, M.T. Overgaard, L. Sottrup-Jensen, G.J. Gleich, and L.G. Hays The insulin-like growth factor (IGF)-dependent IGF binding protein-4 protease secreted by human fibroblasts is pregnancy-associated plasma protein-A Proc Natl Acad Sci USA 96 6 1999 3149 3153
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.6 , pp. 3149-3153
    • Lawrence, J.B.1    Oxvig, C.2    Overgaard, M.T.3    Sottrup-Jensen, L.4    Gleich, G.J.5    Hays, L.G.6
  • 32
    • 0035943504 scopus 로고    scopus 로고
    • Pregnancy-associated plasma protein-A (PAPP-A) cleaves insulin-like growth factor binding protein (IGFBP)-5 independent of IGF: Implications for the mechanism of IGFBP-4 proteolysis by PAPP-A
    • L.S. Laursen, M.T. Overgaard, R. Soe, H.B. Boldt, L. Sottrup-Jensen, and L.C. Giudice Pregnancy-associated plasma protein-A (PAPP-A) cleaves insulin-like growth factor binding protein (IGFBP)-5 independent of IGF: implications for the mechanism of IGFBP-4 proteolysis by PAPP-A FEBS Lett 504 1-2 2001 36 40
    • (2001) FEBS Lett , vol.504 , Issue.1-2 , pp. 36-40
    • Laursen, L.S.1    Overgaard, M.T.2    Soe, R.3    Boldt, H.B.4    Sottrup-Jensen, L.5    Giudice, L.C.6
  • 33
    • 1642311220 scopus 로고    scopus 로고
    • Metalloproteinase pregnancy-associated plasma protein a is a critical growth regulatory factor during fetal development
    • C.A. Conover, L.K. Bale, M.T. Overgaard, E.W. Johnstone, U.H. Laursen, and E.M. Fuchtbauer Metalloproteinase pregnancy-associated plasma protein A is a critical growth regulatory factor during fetal development Development 131 5 2004 1187 1194
    • (2004) Development , vol.131 , Issue.5 , pp. 1187-1194
    • Conover, C.A.1    Bale, L.K.2    Overgaard, M.T.3    Johnstone, E.W.4    Laursen, U.H.5    Fuchtbauer, E.M.6
  • 35
    • 0037033109 scopus 로고    scopus 로고
    • Cell surface targeting of pregnancy-associated plasma protein a proteolytic activity
    • L.S. Laursen, M.T. Overgaard, K. Weyer, H.B. Boldt, P. Ebbesen, and M. Christiansen Cell surface targeting of pregnancy-associated plasma protein A proteolytic activity J Biol Chem 277 49 2002 47225 47234
    • (2002) J Biol Chem , vol.277 , Issue.49 , pp. 47225-47234
    • Laursen, L.S.1    Overgaard, M.T.2    Weyer, K.3    Boldt, H.B.4    Ebbesen, P.5    Christiansen, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.