메뉴 건너뛰기




Volumn 184, Issue 2, 2000, Pages 171-182

The mitogenic activity of fibroblast growth correlates with its internalization and limited processing

Author keywords

[No Author keywords available]

Indexed keywords

FIBROBLAST GROWTH FACTOR 1;

EID: 0033935549     PISSN: 00219541     EISSN: None     Source Type: Journal    
DOI: 10.1002/1097-4652(200008)184:2<171::AID-JCP4>3.0.CO;2-J     Document Type: Article
Times cited : (17)

References (71)
  • 2
    • 0032952058 scopus 로고    scopus 로고
    • Nuclear activities of basic fibroblast growth factor: Potentiation of low-serum growth mediated by natural or chimeric nuclear localization signals
    • Arese M, Chen Y, Florkiewicz RZ, Gualandris A, Shen B, Rifkin DB. 1999. Nuclear activities of basic fibroblast growth factor: potentiation of low-serum growth mediated by natural or chimeric nuclear localization signals. Mol Biol Cell 10:1429-1444.
    • (1999) Mol Biol Cell , vol.10 , pp. 1429-1444
    • Arese, M.1    Chen, Y.2    Florkiewicz, R.Z.3    Gualandris, A.4    Shen, B.5    Rifkin, D.B.6
  • 3
    • 0028998783 scopus 로고
    • Proteolysis of glucagon within hepatic endosomes by membrane-associated cathepsins B and D
    • Authier F, Mort JS, Bell AW, Posner BI, Bergeron JJM. 1995. Proteolysis of glucagon within hepatic endosomes by membrane-associated cathepsins B and D. J Biol Chem 270:15798-15807.
    • (1995) J Biol Chem , vol.270 , pp. 15798-15807
    • Authier, F.1    Mort, J.S.2    Bell, A.W.3    Posner, B.I.4    Bergeron, J.J.M.5
  • 6
    • 0023894936 scopus 로고
    • Chloroquine and monensin inhibit induction of DNA synthesis in rat smooth muscle cells stimulated with platelet-derived growth factor
    • Bottger BA, Sjolund M, Thyberg J. 1988. Chloroquine and monensin inhibit induction of DNA synthesis in rat smooth muscle cells stimulated with platelet-derived growth factor. Cell Tissue Res 252: 275-285.
    • (1988) Cell Tissue Res , vol.252 , pp. 275-285
    • Bottger, B.A.1    Sjolund, M.2    Thyberg, J.3
  • 7
    • 0028589222 scopus 로고
    • Activation of cDNA transcription by FGF-2: Key role in protein kinase CKII
    • Bouche G, Baldin V, Belenguer P, Prats H, Amalric F. 1994. Activation of cDNA transcription by FGF-2: key role in protein kinase CKII. Cell Mol Biol Res 40:547-554.
    • (1994) Cell Mol Biol Res , vol.40 , pp. 547-554
    • Bouche, G.1    Baldin, V.2    Belenguer, P.3    Prats, H.4    Amalric, F.5
  • 8
    • 0025175587 scopus 로고
    • Possible dissociation of the heparin-binding and mitogenic activities of heparin-binding (acidic fibroblast) growth factor-1 from its receptor-binding activities by site-directed mutagenesis of a single lysine residue
    • Burgess WH, Shaheen AM, Ravera M, Jaye M, Donohue PJ, Winkles JA. 1990. Possible dissociation of the heparin-binding and mitogenic activities of heparin-binding (acidic fibroblast) growth factor-1 from its receptor-binding activities by site-directed mutagenesis of a single lysine residue. J Cell Biol 111:2129-2138.
    • (1990) J Cell Biol , vol.111 , pp. 2129-2138
    • Burgess, W.H.1    Shaheen, A.M.2    Ravera, M.3    Jaye, M.4    Donohue, P.J.5    Winkles, J.A.6
  • 9
    • 0026022241 scopus 로고
    • Structure-function studies of heparin-binding (acidic fibroblast) growth factor-1 using site directed mutagenesis
    • Burgess WH, Shaheen AM, Hampton B, Donohue PJ, Winkles JA. 1991. Structure-function studies of heparin-binding (acidic fibroblast) growth factor-1 using site directed mutagenesis. J Cell Biochem 45:131-138.
    • (1991) J Cell Biochem , vol.45 , pp. 131-138
    • Burgess, W.H.1    Shaheen, A.M.2    Hampton, B.3    Donohue, P.J.4    Winkles, J.A.5
  • 10
    • 0028088551 scopus 로고
    • Structure-function studies of FGF-1: Dissociation and partial reconstitution of certain of its biological activities
    • Burgess WH, Friesel R, Winkles J. 1994. Structure-function studies of FGF-1: dissociation and partial reconstitution of certain of its biological activities. Mol Reprod Dev 39:56-61.
    • (1994) Mol Reprod Dev , vol.39 , pp. 56-61
    • Burgess, W.H.1    Friesel, R.2    Winkles, J.3
  • 11
    • 0002525015 scopus 로고    scopus 로고
    • The fibroblast growth factor family: Multifunctional regulators of cell proliferation
    • Pustazi L, Lewis CE, Yap E. editors. Oxford: Oxford University Press
    • Burgess WH, Winkles JA. 1996. The fibroblast growth factor family: multifunctional regulators of cell proliferation. In: Pustazi L, Lewis CE, Yap E. editors. Cell proliferation in cancer: regulatory mechanisms of neoplastic cell growth. Oxford: Oxford University Press. p 154-217.
    • (1996) Cell Proliferation in Cancer: Regulatory Mechanisms of Neoplastic Cell Growth , pp. 154-217
    • Burgess, W.H.1    Winkles, J.A.2
  • 12
    • 0022614962 scopus 로고
    • Determination of the number of endothelial cells in culture using an acid phosphatase assay
    • Connolly DT, Knight MB, Harakas NK, Wittwer AJ, Feder J. 1986. Determination of the number of endothelial cells in culture using an acid phosphatase assay. Anal Biochem 152:136-140.
    • (1986) Anal Biochem , vol.152 , pp. 136-140
    • Connolly, D.T.1    Knight, M.B.2    Harakas, N.K.3    Wittwer, A.J.4    Feder, J.5
  • 14
    • 0024382416 scopus 로고
    • Cleavage of parathyroid hormone in macrophage endosomes illustrates a novel pathway for intracellular processing of proteins
    • Diment S, Martin KJ, Stahl PD. 1989. Cleavage of parathyroid hormone in macrophage endosomes illustrates a novel pathway for intracellular processing of proteins. J Biol Chem 264:13403-13406.
    • (1989) J Biol Chem , vol.264 , pp. 13403-13406
    • Diment, S.1    Martin, K.J.2    Stahl, P.D.3
  • 15
    • 0019287379 scopus 로고
    • The entry of diphtheria toxin into the mammalian cell cytoplasm: Evidence for lysosomal involvement
    • Draper RK, Simon MI. 1980. The entry of diphtheria toxin into the mammalian cell cytoplasm: evidence for lysosomal involvement. J Cell Biol 87:849-854.
    • (1980) J Cell Biol , vol.87 , pp. 849-854
    • Draper, R.K.1    Simon, M.I.2
  • 16
    • 0030028359 scopus 로고    scopus 로고
    • Nuclear localization of a complex of fibroblast growth factor (FGF)-1 and an NH2-terminal fragment of FGF receptor isoforms R4 and R1α in human liver cells
    • Feng S, Xu J, Wang F, Kan M, McKeehan WL. 1996. Nuclear localization of a complex of fibroblast growth factor (FGF)-1 and an NH2-terminal fragment of FGF receptor isoforms R4 and R1α in human liver cells. Biochim Biophys Acta 1310:67-73.
    • (1996) Biochim Biophys Acta , vol.1310 , pp. 67-73
    • Feng, S.1    Xu, J.2    Wang, F.3    Kan, M.4    McKeehan, W.L.5
  • 17
    • 0022977112 scopus 로고
    • The characterization of the receptor for endothelial cell growth factor by covalent ligand attachment
    • Friesel R, Burgess WH, Mehlman T, Maciag T. 1986. The characterization of the receptor for endothelial cell growth factor by covalent ligand attachment. J Biol Chem 261:7581-7584.
    • (1986) J Biol Chem , vol.261 , pp. 7581-7584
    • Friesel, R.1    Burgess, W.H.2    Mehlman, T.3    Maciag, T.4
  • 18
    • 0023877257 scopus 로고
    • Internalization and degradation of heparin binding growth factor-1 by endothelial cells
    • Friesel R, Maciag T. 1988. Internalization and degradation of heparin binding growth factor-1 by endothelial cells. Biochem Biophys Res Commun 151:957-964.
    • (1988) Biochem Biophys Res Commun , vol.151 , pp. 957-964
    • Friesel, R.1    Maciag, T.2
  • 19
    • 0029862822 scopus 로고    scopus 로고
    • Basic fibroblast growth factor (FGF-2) is addressed to caveolae after binding to the plasma membrane of BHK cells
    • Gleizes P-E, Noaillac-Depeyre J, Dupont M-A, Gas N. 1996. Basic fibroblast growth factor (FGF-2) is addressed to caveolae after binding to the plasma membrane of BHK cells. Eur J Cell Biol 71:144-153.
    • (1996) Eur J Cell Biol , vol.71 , pp. 144-153
    • Gleizes, P.-E.1    Noaillac-Depeyre, J.2    Dupont, M.-A.3    Gas, N.4
  • 20
    • 0019307389 scopus 로고
    • Chloroquine inhibits lysosomal enzyme pinocytosis and enhances lysosomal enzyme secretion by impairing receptor recycling
    • Gonzalez-Noriega A, Grubb JH, Talkad V, Sly WAS. 1980. Chloroquine inhibits lysosomal enzyme pinocytosis and enhances lysosomal enzyme secretion by impairing receptor recycling. J Cell Biol 85:839-852.
    • (1980) J Cell Biol , vol.85 , pp. 839-852
    • Gonzalez-Noriega, A.1    Grubb, J.H.2    Talkad, V.3    Sly, W.A.S.4
  • 21
    • 0030227202 scopus 로고    scopus 로고
    • Molecular mechanisms of angiogenesis: Experimental models define cellular trafficking of FGF-1
    • Hicks KK, Shin JT, Opalenik SR, Thompson JA. 1996. Molecular mechanisms of angiogenesis: experimental models define cellular trafficking of FGF-1. Puerto Rico Health Sci J 15:179-186.
    • (1996) Puerto Rico Health Sci J , vol.15 , pp. 179-186
    • Hicks, K.K.1    Shin, J.T.2    Opalenik, S.R.3    Thompson, J.A.4
  • 22
    • 0028135716 scopus 로고
    • Cell cycle-dependent nuclear localization of exogenously added fibroblast growth factor-1 in BALB/c 3T3 and human vascular endothelial cells
    • Imamura T, Oka S, Tanahashi T, Okita Y. 1994. Cell cycle-dependent nuclear localization of exogenously added fibroblast growth factor-1 in BALB/c 3T3 and human vascular endothelial cells. Exp Cell Res 215:363-372.
    • (1994) Exp Cell Res , vol.215 , pp. 363-372
    • Imamura, T.1    Oka, S.2    Tanahashi, T.3    Okita, Y.4
  • 23
    • 0028071526 scopus 로고
    • Nuclear signaling pathways for polypeptide ligands and their membrane receptors
    • Jans D. 1994. Nuclear signaling pathways for polypeptide ligands and their membrane receptors. FASEB J 8:841-847.
    • (1994) FASEB J , vol.8 , pp. 841-847
    • Jans, D.1
  • 24
    • 0032078165 scopus 로고    scopus 로고
    • Nuclear targeting by growth factors, cytokines, and their receptors: A role in signaling?
    • Jans DA, Hassan G. 1998. Nuclear targeting by growth factors, cytokines, and their receptors: a role in signaling? Bioessays 20:400-411.
    • (1998) Bioessays , vol.20 , pp. 400-411
    • Jans, D.A.1    Hassan, G.2
  • 25
    • 0026649742 scopus 로고
    • Fibroblast growth factor receptor tyrosine kinase: Molecular analysis and signal transduction
    • Jaye M, Schlessinger J, Dionne CA. 1992. Fibroblast growth factor receptor tyrosine kinase: molecular analysis and signal transduction. Biochim Biophys Acta 1135:185-199.
    • (1992) Biochim Biophys Acta , vol.1135 , pp. 185-199
    • Jaye, M.1    Schlessinger, J.2    Dionne, C.A.3
  • 26
    • 0029036707 scopus 로고
    • Nucleolar association of fibroblast growth factor 3 via specific sequence motifs has inhibitory effects on cell growth
    • Kiefer P, Dickson C. 1995. Nucleolar association of fibroblast growth factor 3 via specific sequence motifs has inhibitory effects on cell growth. Mol Cell Biol 15:4364-4374.
    • (1995) Mol Cell Biol , vol.15 , pp. 4364-4374
    • Kiefer, P.1    Dickson, C.2
  • 27
    • 0019504320 scopus 로고
    • Lysosomotrophic amines inhibit mitogenesis induced by growth factors
    • King AC, Hernaez-Davis L, Cuatrecasas P. 1981. Lysosomotrophic amines inhibit mitogenesis induced by growth factors. Proc Nat Acad Sci USA 78:717-721.
    • (1981) Proc Nat Acad Sci USA , vol.78 , pp. 717-721
    • King, A.C.1    Hernaez-Davis, L.2    Cuatrecasas, P.3
  • 28
    • 0021702553 scopus 로고
    • 125I-epidermal growth factor, causes intracellular accumulation of receptors and blocks the mitogenic response
    • 125I-epidermal growth factor, causes intracellular accumulation of receptors and blocks the mitogenic response. Biochem Biophys Res Commun 124:585-591.
    • (1984) Biochem Biophys Res Commun , vol.124 , pp. 585-591
    • King, A.C.1
  • 29
    • 2642677628 scopus 로고    scopus 로고
    • Inability of the acidic fibroblast growth factor mutant K132E to stimulate DNA synthesis after translocation inot cells
    • Klingenberg O, Wiedlocha A, Rapak A, Munoz R, Falnes PO, Olsnes S. 1998. Inability of the acidic fibroblast growth factor mutant K132E to stimulate DNA synthesis after translocation inot cells. J Biol Chem 273:11164-11172.
    • (1998) J Biol Chem , vol.273 , pp. 11164-11172
    • Klingenberg, O.1    Wiedlocha, A.2    Rapak, A.3    Munoz, R.4    Falnes, P.O.5    Olsnes, S.6
  • 30
    • 0041153989 scopus 로고    scopus 로고
    • Effects of mutations of a phosphorylation site in an exposed loop in acidic fibroblast growth factor
    • Klingenberg O, Wiedlocha A, Olsnes S. 1999. Effects of mutations of a phosphorylation site in an exposed loop in acidic fibroblast growth factor. J Biol Chem 274:18081-18086.
    • (1999) J Biol Chem , vol.274 , pp. 18081-18086
    • Klingenberg, O.1    Wiedlocha, A.2    Olsnes, S.3
  • 31
    • 0032533863 scopus 로고    scopus 로고
    • Cloning an intracellular protein that binds selectively to mitogenic acidic fibroblast growth factor
    • Kolpakova E, Wiedlocha A, Stenmark H, Klingenberg O, Falnes PO, Olsnes S. 1998. Cloning an intracellular protein that binds selectively to mitogenic acidic fibroblast growth factor. Biochem J 336:213-222.
    • (1998) Biochem J , vol.336 , pp. 213-222
    • Kolpakova, E.1    Wiedlocha, A.2    Stenmark, H.3    Klingenberg, O.4    Falnes, P.O.5    Olsnes, S.6
  • 32
    • 0026322122 scopus 로고
    • The role of receptor-ligand endocytosis and degradation in interleukin-2 signaling and T-lymphocyte proliferation
    • Legrue SJ, Sheu T-L, Chernajovsky Y. 1991. The role of receptor-ligand endocytosis and degradation in interleukin-2 signaling and T-lymphocyte proliferation. Lymphokine Cytokine Res 10:431-436.
    • (1991) Lymphokine Cytokine Res , vol.10 , pp. 431-436
    • Legrue, S.J.1    Sheu, T.-L.2    Chernajovsky, Y.3
  • 33
    • 0029954235 scopus 로고    scopus 로고
    • Nuclear translocation of fibroblast growth factor (FGF) receptors in response to FGF-2
    • Maher P. 1996. Nuclear translocation of fibroblast growth factor (FGF) receptors in response to FGF-2. J Cell Biol 134:529-536.
    • (1996) J Cell Biol , vol.134 , pp. 529-536
    • Maher, P.1
  • 35
    • 0027368966 scopus 로고
    • aFGF binding to low and high affinity receptors induces both aFGF and aFGF receptors dimerization
    • Mascarelli F, Fuhrmann G, Courtois Y. 1993. aFGF binding to low and high affinity receptors induces both aFGF and aFGF receptors dimerization. Growth Factors 8:211-233.
    • (1993) Growth Factors , vol.8 , pp. 211-233
    • Mascarelli, F.1    Fuhrmann, G.2    Courtois, Y.3
  • 36
    • 0020628344 scopus 로고
    • The role of intermediate vesicles in the adsorptive endocvtosis and transport of ligand to lysosomes by human fibroblasts
    • Merion M, Sly WS. 1983. The role of intermediate vesicles in the adsorptive endocvtosis and transport of ligand to lysosomes by human fibroblasts. J Cell Biol 96:644-650.
    • (1983) J Cell Biol , vol.96 , pp. 644-650
    • Merion, M.1    Sly, W.S.2
  • 37
    • 0023189534 scopus 로고
    • The interleukin-1 receptor. Dynamics of interleukin 1 binding and internalization in T cells and fibroblasts
    • Mizel SB, Kilian PL, Lewis JC, Paganelli KA, Chizzonite RA. 1987. The interleukin-1 receptor. Dynamics of interleukin 1 binding and internalization in T cells and fibroblasts. J Immunonol 138:2906-2912.
    • (1987) J Immunonol , vol.138 , pp. 2906-2912
    • Mizel, S.B.1    Kilian, P.L.2    Lewis, J.C.3    Paganelli, K.A.4    Chizzonite, R.A.5
  • 39
    • 0030027488 scopus 로고    scopus 로고
    • Identification of six novel autophosphorylation sites on fibroblast growth factor receptor-1 and elucidation of their importance in receptor activation and signal transduction
    • Mohammadi M, Dikic I, Sorokin A, Burgess WH, Jaye M, Schlessinger J. 1996a. Identification of six novel autophosphorylation sites on fibroblast growth factor receptor-1 and elucidation of their importance in receptor activation and signal transduction. Mol Cell Biol 16:977-989.
    • (1996) Mol Cell Biol , vol.16 , pp. 977-989
    • Mohammadi, M.1    Dikic, I.2    Sorokin, A.3    Burgess, W.H.4    Jaye, M.5    Schlessinger, J.6
  • 40
    • 0030598848 scopus 로고    scopus 로고
    • Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism
    • Mohammadi M, Schlessinger J, Hubbard SR. 1996b. Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism. Cell 86:577-587.
    • (1996) Cell , vol.86 , pp. 577-587
    • Mohammadi, M.1    Schlessinger, J.2    Hubbard, S.R.3
  • 41
    • 0023771001 scopus 로고
    • Metabolism of receptor-bound and matrix-bound basic fibroblast growth factor by bovine capillary endothelial cells
    • Moscatelli D. 1988. Metabolism of receptor-bound and matrix-bound basic fibroblast growth factor by bovine capillary endothelial cells. J Cell Biol 107:753-759.
    • (1988) J Cell Biol , vol.107 , pp. 753-759
    • Moscatelli, D.1
  • 42
    • 0024424391 scopus 로고
    • Transformation of NIH 3T3 cells with basic fibroblast growth factor or the hst/K-fgf oncogene causes downregulation of the fibroblast growth factor receptor: Reversal of morphological transformation and restoration of receptor number by suramin
    • Moscatelli D, Quarto N. 1989. Transformation of NIH 3T3 cells with basic fibroblast growth factor or the hst/K-fgf oncogene causes downregulation of the fibroblast growth factor receptor: reversal of morphological transformation and restoration of receptor number by suramin. J Cell Biol 109:2519-2527.
    • (1989) J Cell Biol , vol.109 , pp. 2519-2527
    • Moscatelli, D.1    Quarto, N.2
  • 43
    • 0030870932 scopus 로고    scopus 로고
    • Effect of mutation of cytoplasmic receptor domain and of genistein on transport of acidic fibroblast growth factor into cells
    • Munoz R, Klingenberg O, Wiedlocha A, Rapak A, Falnes PO, Olsnes S. 1997. Effect of mutation of cytoplasmic receptor domain and of genistein on transport of acidic fibroblast growth factor into cells. Oncogene 15:525-536.
    • (1997) Oncogene , vol.15 , pp. 525-536
    • Munoz, R.1    Klingenberg, O.2    Wiedlocha, A.3    Rapak, A.4    Falnes, P.O.5    Olsnes, S.6
  • 44
    • 2642714342 scopus 로고
    • Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents
    • Ohkuma S, Poole B. 1978. Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents. Proc Nat Acad Sci USA 75:3327-3331.
    • (1978) Proc Nat Acad Sci USA , vol.75 , pp. 3327-3331
    • Ohkuma, S.1    Poole, B.2
  • 45
    • 0023949782 scopus 로고
    • Selective degradation of tumor necrosis factor in sensitive cells and production of membrane-active substance
    • Ohsawa F, Natori S. 1988. Selective degradation of tumor necrosis factor in sensitive cells and production of membrane-active substance. J Biochem 103:730-734.
    • (1988) J Biochem , vol.103 , pp. 730-734
    • Ohsawa, F.1    Natori, S.2
  • 46
    • 0031750101 scopus 로고    scopus 로고
    • Filipin-dependent inhibition of cholera toxin: Evidence for toxin internalization and activation through caveolae-like domains
    • Orlandi PA, Fishman PH. 1998. Filipin-dependent inhibition of cholera toxin: evidence for toxin internalization and activation through caveolae-like domains. J Cell Biol 141:905-915.
    • (1998) J Cell Biol , vol.141 , pp. 905-915
    • Orlandi, P.A.1    Fishman, P.H.2
  • 47
    • 0028081352 scopus 로고
    • Intact and functional fibroblast growth factor (FGF) receptor-1 trafficks near the nucleus in response to FGF-1
    • Prudovsky I, Savion N, Zhan X, Friesel R, Xu J, Hou J, McKeehan WL, Maciag T. 1994. Intact and functional fibroblast growth factor (FGF) receptor-1 trafficks near the nucleus in response to FGF-1. J Biol Chem 269:31720-31724.
    • (1994) J Biol Chem , vol.269 , pp. 31720-31724
    • Prudovsky, I.1    Savion, N.2    Zhan, X.3    Friesel, R.4    Xu, J.5    Hou, J.6    McKeehan, W.L.7    Maciag, T.8
  • 48
    • 15844396312 scopus 로고    scopus 로고
    • The nuclear trafficking of extracellular FGF-1 correlates with the perinuclear association of the FGFR-1α isoforms but not the FGFR-1β isoforms
    • Prudovsky I, Savion N, LaVallee TM, Maciag T. 1996. The nuclear trafficking of extracellular FGF-1 correlates with the perinuclear association of the FGFR-1α isoforms but not the FGFR-1β isoforms. J Biol Chem 271:14198-14205.
    • (1996) J Biol Chem , vol.271 , pp. 14198-14205
    • Prudovsky, I.1    Savion, N.2    LaVallee, T.M.3    Maciag, T.4
  • 49
    • 0026214066 scopus 로고
    • Selective expression of high molecular weight basic fibroblast growth factor confers a unique phenotype to NIH 3T3 cells
    • Quarto N, Talarico D, Florkiewicz R, Rifkin DB. 1991. Selective expression of high molecular weight basic fibroblast growth factor confers a unique phenotype to NIH 3T3 cells. Cell Regulation 2:699-708.
    • (1991) Cell Regulation , vol.2 , pp. 699-708
    • Quarto, N.1    Talarico, D.2    Florkiewicz, R.3    Rifkin, D.B.4
  • 50
    • 0023898022 scopus 로고
    • Binding, internalization, and intracellular localization of interleukin-1β in human diploid fibroblasts
    • Qwarnstrom EE, Page RC, Gillis S, Dower SK. 1988. Binding, internalization, and intracellular localization of interleukin-1β in human diploid fibroblasts. J Biol Chem 263:8261-8269.
    • (1988) J Biol Chem , vol.263 , pp. 8261-8269
    • Qwarnstrom, E.E.1    Page, R.C.2    Gillis, S.3    Dower, S.K.4
  • 51
    • 0027323554 scopus 로고
    • Heparan sulfate proteoglycan and FGF receptor target basic FGF to different intracellular destinations
    • Reiland J, Rapraeger AC. 1993. Heparan sulfate proteoglycan and FGF receptor target basic FGF to different intracellular destinations. J Cell Sci 105:1085-1093.
    • (1993) J Cell Sci , vol.105 , pp. 1085-1093
    • Reiland, J.1    Rapraeger, A.C.2
  • 54
    • 0027997787 scopus 로고
    • Filipin-sensitive caveolae-mediated transport in endothelium: Reduced transcytosis, scavenger endocytosis, and capillary permeability of select macromolecules
    • Schnitzer JE, Oh P, Pinney E, Allard J. 1994. Filipin-sensitive caveolae-mediated transport in endothelium: reduced transcytosis, scavenger endocytosis, and capillary permeability of select macromolecules. J Cell Biol 127:1217-1232.
    • (1994) J Cell Biol , vol.127 , pp. 1217-1232
    • Schnitzer, J.E.1    Oh, P.2    Pinney, E.3    Allard, J.4
  • 56
    • 0026001765 scopus 로고
    • 16-Kilodalton heparin binding (fibroblast) growth factor type one appears in a stable 40-kilodalton complex after receptor-dependent internalization
    • Shi E, Kan M, Xu J, McKeehan WL. 1991. 16-Kilodalton heparin binding (fibroblast) growth factor type one appears in a stable 40-kilodalton complex after receptor-dependent internalization. J Biol Chem 266:5774-5779.
    • (1991) J Biol Chem , vol.266 , pp. 5774-5779
    • Shi, E.1    Kan, M.2    Xu, J.3    McKeehan, W.L.4
  • 57
    • 0030989326 scopus 로고    scopus 로고
    • Insulin internalization and other signaling pathways in the pleiotropic effects of insulin
    • Smith RM, Harada S, Jarett L. 1997. Insulin internalization and other signaling pathways in the pleiotropic effects of insulin. Int Rev Cytol 173:243-280.
    • (1997) Int Rev Cytol , vol.173 , pp. 243-280
    • Smith, R.M.1    Harada, S.2    Jarett, L.3
  • 58
    • 0029072576 scopus 로고
    • Cationic amphiphilic drugs inhibit the internalization of cholera toxin to the golgi apparatus and the subsequent elevation of cyclic AMP
    • Sofer A, Futerman AH. 1995. Cationic amphiphilic drugs inhibit the internalization of cholera toxin to the golgi apparatus and the subsequent elevation of cyclic AMP. J Biol Chem 270:12117-12122.
    • (1995) J Biol Chem , vol.270 , pp. 12117-12122
    • Sofer, A.1    Futerman, A.H.2
  • 60
    • 0028356454 scopus 로고
    • Internalization of fibroblast growth factor receptor is inhibited by a point mutation at tyrosine 766
    • Sorokin A, Mohammadi M, Huang J, Schlessinger J. 1994. Internalization of fibroblast growth factor receptor is inhibited by a point mutation at tyrosine 766. J Biol Chem 269:17056-17061.
    • (1994) J Biol Chem , vol.269 , pp. 17056-17061
    • Sorokin, A.1    Mohammadi, M.2    Huang, J.3    Schlessinger, J.4
  • 61
    • 0032558391 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans control intracellular processing of bFGF in vascular smooth muscle cells
    • Sperinde GV, Nugent MA. 1998. Heparan sulfate proteoglycans control intracellular processing of bFGF in vascular smooth muscle cells. Biochemistry 37:13153-13164.
    • (1998) Biochemistry , vol.37 , pp. 13153-13164
    • Sperinde, G.V.1    Nugent, M.A.2
  • 62
    • 0033082844 scopus 로고    scopus 로고
    • Basic fibroblast growth factor does not prevent heparan sulphate proteoglycan catabolism in intact cells, but it alters the distribution of the glycosaminoglycan degradation products
    • Tumova S, Hatch BA, Law DJ, Bame KJ. 1999. Basic fibroblast growth factor does not prevent heparan sulphate proteoglycan catabolism in intact cells, but it alters the distribution of the glycosaminoglycan degradation products. Biochem J 337:471-481.
    • (1999) Biochem J , vol.337 , pp. 471-481
    • Tumova, S.1    Hatch, B.A.2    Law, D.J.3    Bame, K.J.4
  • 63
    • 0027520440 scopus 로고
    • Mis-assembly of clathrin lattices on endosomes reveals a regulatory switch for coated pit formation
    • Wang L-H, Rothberg KG, Anderson RGW. 1993. Mis-assembly of clathrin lattices on endosomes reveals a regulatory switch for coated pit formation. J Cell Biol 123:1107-1117.
    • (1993) J Cell Biol , vol.123 , pp. 1107-1117
    • Wang, L.-H.1    Rothberg, K.G.2    Anderson, R.G.W.3
  • 64
    • 0030346223 scopus 로고    scopus 로고
    • Retrograde transport of acidic fibroblast growth factor as a part of the growth factor signaling
    • Wiedlocha A. 1996. Retrograde transport of acidic fibroblast growth factor as a part of the growth factor signaling. Arch Immunol Ther Exp 44:201-207.
    • (1996) Arch Immunol Ther Exp , vol.44 , pp. 201-207
    • Wiedlocha, A.1
  • 65
    • 0028328846 scopus 로고
    • Dual mode of signal transduction by externally added acidic fibroblast growth factor
    • Wiedlocha A, Falnes PO, Madshus IH, Sandvig K, Olsnes S. 1994. Dual mode of signal transduction by externally added acidic fibroblast growth factor. Cell 76:1039-1051.
    • (1994) Cell , vol.76 , pp. 1039-1051
    • Wiedlocha, A.1    Falnes, P.O.2    Madshus, I.H.3    Sandvig, K.4    Olsnes, S.5
  • 66
    • 0029557495 scopus 로고
    • Translocation to cytosol of exogenous, CAAX-tagged acidic fibroblast growth factor
    • Wiedlocha A, Falnes PO, Rapak A, Klingenberg O, Munoz R, Olsnes S. 1995. Translocation to cytosol of exogenous, CAAX-tagged acidic fibroblast growth factor. J Biol Chem 270:30680-30685.
    • (1995) J Biol Chem , vol.270 , pp. 30680-30685
    • Wiedlocha, A.1    Falnes, P.O.2    Rapak, A.3    Klingenberg, O.4    Munoz, R.5    Olsnes, S.6
  • 67
    • 0029655962 scopus 로고    scopus 로고
    • Stimulation of proliferation of a human osteosarcoma cell line by exogenous acidic fibroblast growth factor requires both activation of receptor tyrosine kinase and growth factor internalization
    • Wiedlocha A, Falnes PO, Rapak A, Munoz R, Klingenberg O, Olsnes S. 1996. Stimulation of proliferation of a human osteosarcoma cell line by exogenous acidic fibroblast growth factor requires both activation of receptor tyrosine kinase and growth factor internalization. Mol Cell Biol 16:270-280.
    • (1996) Mol Cell Biol , vol.16 , pp. 270-280
    • Wiedlocha, A.1    Falnes, P.O.2    Rapak, A.3    Munoz, R.4    Klingenberg, O.5    Olsnes, S.6
  • 68
    • 0031972479 scopus 로고    scopus 로고
    • Serum- and polypeptide growth factor-inducible gene expression in mouse fibroblasts
    • Moldave K, editor. San Diego, CA: Academic Press
    • Winkles JA. 1998. Serum- and polypeptide growth factor-inducible gene expression in mouse fibroblasts. In: Moldave K, editor. Progress in nucleic acid research and molecular biology, Vol 58. San Diego, CA: Academic Press. p 41-78.
    • (1998) Progress in Nucleic Acid Research and Molecular Biology , vol.58 , pp. 41-78
    • Winkles, J.A.1
  • 69
    • 0022186993 scopus 로고
    • Inhibition of intracellular degradation of proteoglycans by leupeptin in rat ovarian granulosa cells
    • Yanagishita M. 1985. Inhibition of intracellular degradation of proteoglycans by leupeptin in rat ovarian granulosa cells. J Biol Chem 260:11075-11082.
    • (1985) J Biol Chem , vol.260 , pp. 11075-11082
    • Yanagishita, M.1
  • 70
    • 0026469173 scopus 로고
    • Analysis of endogenous and exogenous nuclear translocation of fibroblast growth factor-1 in NIH 3T3 cells
    • Zhan X, Hu X, Friedman S, Maciag T. 1992. Analysis of endogenous and exogenous nuclear translocation of fibroblast growth factor-1 in NIH 3T3 cells. Biochem Biophys Res Commun 188:982-991.
    • (1992) Biochem Biophys Res Commun , vol.188 , pp. 982-991
    • Zhan, X.1    Hu, X.2    Friedman, S.3    Maciag, T.4
  • 71
    • 0027286319 scopus 로고
    • Long term growth factor exposure and differential tyrosine phosphorylation are required for DNA synthesis in BALB/c 3T3 cells
    • Zhan X, Hu X, Friesel R, Maciag T. 1993. Long term growth factor exposure and differential tyrosine phosphorylation are required for DNA synthesis in BALB/c 3T3 cells. J Biol Chem 268:9611-9620.
    • (1993) J Biol Chem , vol.268 , pp. 9611-9620
    • Zhan, X.1    Hu, X.2    Friesel, R.3    Maciag, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.