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Volumn 3, Issue 5, 2004, Pages 466-477

Transforming growth factor-β1 specificically induce proteins involved in the myofibroblast contractile apparatus

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ALPHA ACTIN; CALGIZZARIN; COFILIN; CYTOSKELETON PROTEIN; METHIONINE; PROFILIN; SULFUR 35; TRANSFORMING GROWTH FACTOR BETA1; UNCLASSIFIED DRUG;

EID: 2642524382     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M300108-MCP200     Document Type: Review
Times cited : (105)

References (72)
  • 1
    • 0024505353 scopus 로고
    • Subepithelial fibrosis in the bronchi of asthmatics
    • Roche, W. R., Beasley, R., Williams, J. H., and Holgate, S. T. (1989) Subepithelial fibrosis in the bronchi of asthmatics. Lancet 1, 520-524
    • (1989) Lancet , vol.1 , pp. 520-524
    • Roche, W.R.1    Beasley, R.2    Williams, J.H.3    Holgate, S.T.4
  • 3
    • 0015225464 scopus 로고
    • Presence of modified fibroblasts in granulation tissue and their possible role in wound contraction
    • Gabbiani, G., Ryan, G. B., and Majne, G. (1971) Presence of modified fibroblasts in granulation tissue and their possible role in wound contraction. Experientia 27, 549-550
    • (1971) Experientia , vol.27 , pp. 549-550
    • Gabbiani, G.1    Ryan, G.B.2    Majne, G.3
  • 4
    • 0027437297 scopus 로고
    • Mast cell and myofibroblast in wound healing
    • Hebda, P. A., Collins, M. A., and Tharp, M. D. (1993) Mast cell and myofibroblast in wound healing. Dermatol. Clin. 11, 685-696
    • (1993) Dermatol. Clin. , vol.11 , pp. 685-696
    • Hebda, P.A.1    Collins, M.A.2    Tharp, M.D.3
  • 5
    • 0023232209 scopus 로고
    • Morphologic and biochemical evidence for a contractile cell network within the rat intestinal mucosa
    • Joyce, N. C., Haire, M. F., and Palade, G. E. (1987) Morphologic and biochemical evidence for a contractile cell network within the rat intestinal mucosa. Gastroenterology 92, 68-81
    • (1987) Gastroenterology , vol.92 , pp. 68-81
    • Joyce, N.C.1    Haire, M.F.2    Palade, G.E.3
  • 6
    • 0033178473 scopus 로고    scopus 로고
    • Mechanisms of myofibroblast activity and phenotypic modulation
    • Serini, G., and Gabbiani, G. (1999) Mechanisms of myofibroblast activity and phenotypic modulation. Exp. Cell Res. 250, 273-283
    • (1999) Exp. Cell Res. , vol.250 , pp. 273-283
    • Serini, G.1    Gabbiani, G.2
  • 8
    • 0026842641 scopus 로고
    • Capillary growth: A two-cell system
    • D'Amore, P. A. (1992) Capillary growth: A two-cell system. Semin. Cancer Biol. 3, 49-56
    • (1992) Semin. Cancer Biol. , vol.3 , pp. 49-56
    • D'Amore, P.A.1
  • 9
    • 0026775988 scopus 로고
    • An in vitro model for cell-cell interactions
    • Saunders, K. B., and D'Amore, P. A. (1992) An in vitro model for cell-cell interactions. In Vitro Cell. Dev. Biol. 28A, 521-528
    • (1992) In Vitro Cell. Dev. Biol. , vol.28 A , pp. 521-528
    • Saunders, K.B.1    D'Amore, P.A.2
  • 10
    • 0028067243 scopus 로고
    • Paracrine interactions between fibroblasts and endothelial cells in a serum-free coculture model. Modulation of angiogenesis and collagen gel contraction
    • Villaschi, S., and Nicosia, R. F. (1994) Paracrine interactions between fibroblasts and endothelial cells in a serum-free coculture model. Modulation of angiogenesis and collagen gel contraction. Lab. Invest. 71, 291-299
    • (1994) Lab. Invest. , vol.71 , pp. 291-299
    • Villaschi, S.1    Nicosia, R.F.2
  • 12
    • 0032559341 scopus 로고    scopus 로고
    • A structural scaffolding of intermediate filaments in health and disease
    • Fuchs, E., and Cleveland, D. W. (1998) A structural scaffolding of intermediate filaments in health and disease. Science 279, 514-519
    • (1998) Science , vol.279 , pp. 514-519
    • Fuchs, E.1    Cleveland, D.W.2
  • 13
    • 0023128995 scopus 로고
    • Intermediate filaments of myofibroblasts. Immunochemical and immunocytochemical analyses
    • Iwasaki, H., Isayama, T., Ichiki, T., and Kikuchi, M. (1987) Intermediate filaments of myofibroblasts. Immunochemical and immunocytochemical analyses. Pathol. Res. Practice 182, 248-254
    • (1987) Pathol. Res. Practice , vol.182 , pp. 248-254
    • Iwasaki, H.1    Isayama, T.2    Ichiki, T.3    Kikuchi, M.4
  • 14
    • 0028122690 scopus 로고
    • Heterogeneity of myofibroblast phenotypic features: An example of fibroblastic cell plasticity
    • Schmitt-Graff, A., Desmouliere, A., and Gabbiani, G. (1994) Heterogeneity of myofibroblast phenotypic features: An example of fibroblastic cell plasticity. Virchows Arch. 425, 3-24
    • (1994) Virchows Arch. , vol.425 , pp. 3-24
    • Schmitt-Graff, A.1    Desmouliere, A.2    Gabbiani, G.3
  • 15
    • 0028182776 scopus 로고
    • Identification and classification of interstitial cells in the canine proximal colon by ultrastructure and immunocytochemistry
    • Torihashi, S., Gerthoffer, W. T., Kobayashi, S., and Sanders, K. M. (1994) Identification and classification of interstitial cells in the canine proximal colon by ultrastructure and immunocytochemistry. Histochemistry 101, 169-183
    • (1994) Histochemistry , vol.101 , pp. 169-183
    • Torihashi, S.1    Gerthoffer, W.T.2    Kobayashi, S.3    Sanders, K.M.4
  • 16
    • 0027333421 scopus 로고
    • Molecular aspects of mesenchymal-epithelial interactions
    • Birchmeier, C., and Birchmeier, W. (1993) Molecular aspects of mesenchymal-epithelial interactions. Annu. Rev. Cell Biol. 9, 511-540
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 511-540
    • Birchmeier, C.1    Birchmeier, W.2
  • 19
    • 0028109801 scopus 로고
    • Transforming growth factor β in tissue fibrosis
    • Border, W. A., and Noble, N. A. (1994) Transforming growth factor β in tissue fibrosis. N. Engl. J. Med. 331, 1286-1292
    • (1994) N. Engl. J. Med. , vol.331 , pp. 1286-1292
    • Border, W.A.1    Noble, N.A.2
  • 20
    • 0030970555 scopus 로고    scopus 로고
    • Closing in on the signals of hepatic fibrosis
    • Friedman, S. L. (1997) Closing in on the signals of hepatic fibrosis. Gastroenterology 112, 1406-1409
    • (1997) Gastroenterology , vol.112 , pp. 1406-1409
    • Friedman, S.L.1
  • 21
    • 0029997830 scopus 로고    scopus 로고
    • Transdifferentiation of hepatic stellate cells (Ito cells) to myofibroblasts: A key event in hepatic fibrogenesis
    • Gressner, A. M. (1996) Transdifferentiation of hepatic stellate cells (Ito cells) to myofibroblasts: A key event in hepatic fibrogenesis. Kidney Int. 54, (suppl.) S39-45
    • (1996) Kidney Int. , vol.54 , Issue.SUPPL.
    • Gressner, A.M.1
  • 22
    • 0028147777 scopus 로고
    • Fibrogenic cytokines and connective tissue production
    • Kovacs, E. J., and DiPietro, L. A. (1994) Fibrogenic cytokines and connective tissue production. FASEB J. 8, 854-861
    • (1994) FASEB J. , vol.8 , pp. 854-861
    • Kovacs, E.J.1    DiPietro, L.A.2
  • 24
    • 0028278029 scopus 로고
    • Myofibroblasts and their role in lung collagen gene expression during pulmonary fibrosis. A combined immunohistochemical and in situ hybridization study
    • Zhang, K., Rekhter, M. D., Gordon, D., and Phan, S. H. (1994) Myofibroblasts and their role in lung collagen gene expression during pulmonary fibrosis. A combined immunohistochemical and in situ hybridization study. Am. J. Pathol. 145, 114-125
    • (1994) Am. J. Pathol. , vol.145 , pp. 114-125
    • Zhang, K.1    Rekhter, M.D.2    Gordon, D.3    Phan, S.H.4
  • 25
    • 0027212686 scopus 로고
    • Transforming growth factor-β1 induces α-smooth muscle actin expression in granulation tissue myofibroblasts and in quiescent and growing cultured fibroblasts
    • Desmouliere, A., Geinoz, A., Gabbiani, F., and Gabbiani, G. (1993) Transforming growth factor-β1 induces α-smooth muscle actin expression in granulation tissue myofibroblasts and in quiescent and growing cultured fibroblasts. J. Cell Biol. 122, 103-111
    • (1993) J. Cell Biol. , vol.122 , pp. 103-111
    • Desmouliere, A.1    Geinoz, A.2    Gabbiani, F.3    Gabbiani, G.4
  • 26
    • 0027161705 scopus 로고
    • Induction of alpha-smooth muscle actin by transforming growth factor-β1 in quiescent human breast gland fibroblasts. Implications for myofibroblast generation in breast neoplasia
    • Ronnov-Jessen, L., and Petersen, O. W. (1993) Induction of alpha-smooth muscle actin by transforming growth factor-β1 in quiescent human breast gland fibroblasts. Implications for myofibroblast generation in breast neoplasia. Lab. invest. 68, 696-707
    • (1993) Lab. Invest. , vol.68 , pp. 696-707
    • Ronnov-Jessen, L.1    Petersen, O.W.2
  • 27
    • 0026445528 scopus 로고
    • Transforming growth factor-β: Recent progress and new challenges
    • Sporn, M. B., and Roberts, A. B. (1992) Transforming growth factor-β: Recent progress and new challenges. J. Cell Biol. 119, 1017-1021
    • (1992) J. Cell Biol. , vol.119 , pp. 1017-1021
    • Sporn, M.B.1    Roberts, A.B.2
  • 28
    • 0031454239 scopus 로고    scopus 로고
    • Hepatic fibrosis, glomerulosclerosis, and a lipodystrophy-like syndrome in PEPCK-TGF-β1 transgenic mice
    • Clouthier, D. E., Comerford, S. A., and Hammer, R. E. (1997) Hepatic fibrosis, glomerulosclerosis, and a lipodystrophy-like syndrome in PEPCK-TGF-β1 transgenic mice. J. Clin. Invest. 100, 2697-2713
    • (1997) J. Clin. Invest. , vol.100 , pp. 2697-2713
    • Clouthier, D.E.1    Comerford, S.A.2    Hammer, R.E.3
  • 29
    • 0030890765 scopus 로고    scopus 로고
    • A transforming growth factor β (TGFβ) control element drives TGFβ-induced stimulation of smooth muscle a-actin gene expression in concert with two CArG elements
    • Hautmann, M. B., Madsen, C. S., and Owens, G. K. (1997) A transforming growth factor β (TGFβ) control element drives TGFβ-induced stimulation of smooth muscle a-actin gene expression in concert with two CArG elements. J. Biol. Chem. 272, 10948-10956
    • (1997) J. Biol. Chem. , vol.272 , pp. 10948-10956
    • Hautmann, M.B.1    Madsen, C.S.2    Owens, G.K.3
  • 31
    • 0031011375 scopus 로고    scopus 로고
    • Myofibroblast phenotypes expression in experimental renal scarring
    • Muchaneta-Kubara, E. C., and el Nahas, A. M. (1997) Myofibroblast phenotypes expression in experimental renal scarring. Nephrol. Dialysis Transplant. 12, 904-915
    • (1997) Nephrol. Dialysis Transplant. , vol.12 , pp. 904-915
    • Muchaneta-Kubara, E.C.1    el Nahas, A.M.2
  • 32
    • 0029836030 scopus 로고    scopus 로고
    • Transforming growth factor-β1 expression and myofibroblast formation during arterial repair
    • Shi, Y., O'Brien, J. E., Jr., Fard, A., and Zalewski, A. (1996) Transforming growth factor-β1 expression and myofibroblast formation during arterial repair. Artetioscler. Thromb. Vasc. Biol. 16, 1298-1305
    • (1996) Artetioscler. Thromb. Vasc. Biol. , vol.16 , pp. 1298-1305
    • Shi, Y.1    O'Brien Jr., J.E.2    Fard, A.3    Zalewski, A.4
  • 33
    • 0029936704 scopus 로고    scopus 로고
    • Transforming growth factor-β1 induces α-smooth muscle-actin expression in cultured human and monkey trabecular meshwork
    • Tamm, E. R., Siegner, A., Baur, A., and Lutjen-Drecoll E. (1996) Transforming growth factor-β1 induces α-smooth muscle-actin expression in cultured human and monkey trabecular meshwork. Exp. Eye Res. 62, 389-397
    • (1996) Exp. Eye Res. , vol.62 , pp. 389-397
    • Tamm, E.R.1    Siegner, A.2    Baur, A.3    Lutjen-Drecoll, E.4
  • 34
    • 0026778310 scopus 로고
    • Transforming growth factor-β in disease: The dark side of tissue repair
    • Border, W. A., and Ruoslahti, E. (1992) Transforming growth factor-β in disease: The dark side of tissue repair. J. Clin. Invest. 90, 1-7
    • (1992) J. Clin. Invest. , vol.90 , pp. 1-7
    • Border, W.A.1    Ruoslahti, E.2
  • 35
    • 0030934532 scopus 로고    scopus 로고
    • Wound healing - Aiming for perfect skin regeneration
    • Martin, P. (1997) Wound healing - Aiming for perfect skin regeneration. Science 276, 75-81
    • (1997) Science , vol.276 , pp. 75-81
    • Martin, P.1
  • 36
    • 0036197606 scopus 로고    scopus 로고
    • Transforming growth factor-β-induced mobilization of actin cytoskeleton requires signaling by small GTPases Cdc42 and RhoA
    • Edlund, S., Landstrom, M., Heldin, C. H., and Aspenstrom, P. (2002) Transforming growth factor-β-induced mobilization of actin cytoskeleton requires signaling by small GTPases Cdc42 and RhoA. Mol. Biol. Cell 13, 902-914
    • (2002) Mol. Biol. Cell , vol.13 , pp. 902-914
    • Edlund, S.1    Landstrom, M.2    Heldin, C.H.3    Aspenstrom, P.4
  • 37
    • 0035185853 scopus 로고    scopus 로고
    • Transforming growth factor-β1 mediates epitheliall to mesenchymal transdifferentiation through a RhoA-dependent mechanism
    • Bhowmick, N. A., Ghiassi, M., Bakin, A., Aakre, M., Lundquist, C. A., Engel, M. E., Arteaga, C. L., and Moses, H. L. (2001) Transforming growth factor-β1 mediates epitheliall to mesenchymal transdifferentiation through a RhoA-dependent mechanism. Mol. Biol. Cell 12, 27-36
    • (2001) Mol. Biol. Cell , vol.12 , pp. 27-36
    • Bhowmick, N.A.1    Ghiassi, M.2    Bakin, A.3    Aakre, M.4    Lundquist, C.A.5    Engel, M.E.6    Arteaga, C.L.7    Moses, H.L.8
  • 38
    • 0032004524 scopus 로고    scopus 로고
    • Rat fibroblasts cultured from various organs exhibit differences in α-smooth muscle actin expression, cytoskeletal pattern, and adhesive structure organization
    • Dugina, V., Alexandrova, A., Chaponnier, C., Vasiliev, J., and Gabbiani, G. (1998) Rat fibroblasts cultured from various organs exhibit differences in α-smooth muscle actin expression, cytoskeletal pattern, and adhesive structure organization. Exp. Cell Res. 238, 481-490
    • (1998) Exp. Cell Res. , vol.238 , pp. 481-490
    • Dugina, V.1    Alexandrova, A.2    Chaponnier, C.3    Vasiliev, J.4    Gabbiani, G.5
  • 39
    • 66249143091 scopus 로고    scopus 로고
    • A proteomic approach to mimic fibrosis disease evolvement by an in vitro cell line
    • Malmstrom, J., Westergren-Thorsson, G., and Marko-Varga, G. (2001) A proteomic approach to mimic fibrosis disease evolvement by an in vitro cell line. Electrophoresis 22, 1776-1784
    • (2001) Electrophoresis , vol.22 , pp. 1776-1784
    • Malmstrom, J.1    Westergren-Thorsson, G.2    Marko-Varga, G.3
  • 40
    • 0024455978 scopus 로고
    • Revelation of specificity of 64K autoantibodies in IDDM serums by high-resolution 2-D gel electrophoresis. Unambiguous identification of 64K target antigen
    • Baekkeskov, S., Warnock, G., Christie, M., Rajotte, R. V., Larsen, P. M., and Fey, S. (1989) Revelation of specificity of 64K autoantibodies in IDDM serums by high-resolution 2-D gel electrophoresis. Unambiguous identification of 64K target antigen. Diabetes 38, 1133-1141
    • (1989) Diabetes , vol.38 , pp. 1133-1141
    • Baekkeskov, S.1    Warnock, G.2    Christie, M.3    Rajotte, R.V.4    Larsen, P.M.5    Fey, S.6
  • 41
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O., and Mann, M. (1996) Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68, 850-858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 42
    • 0033057707 scopus 로고    scopus 로고
    • Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry
    • Gobom, J., Nordhoff, E., Mirgorodskaya, E., Ekman, R., and Roepstorff, P. (1999) Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry. J. Mass Spectrom. 34,105-116
    • (1999) J. Mass Spectrom. , vol.34 , pp. 105-116
    • Gobom, J.1    Nordhoff, E.2    Mirgorodskaya, E.3    Ekman, R.4    Roepstorff, P.5
  • 43
    • 0025078258 scopus 로고
    • Stimulation of Mn-superoxide dismutase expression by tumor necrosis factor-α: Quantitative determination of Mn-SOD protein levels in TNF-resistant and sensitive cells by ELISA
    • Kawaguchi, T., Takeyasu, A., Matsunobu, K., Uda, T., Ishizawa, M., Suzuki, K., Nishiura, T., Ishikawa, M., and Taniguchi, N. (1990) Stimulation of Mn-superoxide dismutase expression by tumor necrosis factor-α: Quantitative determination of Mn-SOD protein levels in TNF-resistant and sensitive cells by ELISA. Biochem. Biophys. Res. Commun. 171, 1378-1386
    • (1990) Biochem. Biophys. Res. Commun. , vol.171 , pp. 1378-1386
    • Kawaguchi, T.1    Takeyasu, A.2    Matsunobu, K.3    Uda, T.4    Ishizawa, M.5    Suzuki, K.6    Nishiura, T.7    Ishikawa, M.8    Taniguchi, N.9
  • 44
    • 0345624495 scopus 로고    scopus 로고
    • Two-dimensional gel analysis of human endometrial proteins: Characterization of proteins with increased expression in hyperplasia and adenocarcinoma
    • Byrjalsen, I., Mose Larsen, P., Fey, S. J., Nilas, L., Larsen, M. R., and Christiansen, C. (1999) Two-dimensional gel analysis of human endometrial proteins: Characterization of proteins with increased expression in hyperplasia and adenocarcinoma. Mol. Hum. Reprod. 5, 748-756
    • (1999) Mol. Hum. Reprod. , vol.5 , pp. 748-756
    • Byrjalsen, I.1    Mose Larsen, P.2    Fey, S.J.3    Nilas, L.4    Larsen, M.R.5    Christiansen, C.6
  • 45
    • 0035252854 scopus 로고    scopus 로고
    • 2D or not 2D. Two-dimensional gel electrophoresis
    • Fey, S. J., and Larsen, P. M. (2001) 2D or not 2D. Two-dimensional gel electrophoresis. Curr. Opin. Chem. Biol. 5, 26-33
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 26-33
    • Fey, S.J.1    Larsen, P.M.2
  • 46
    • 0029828593 scopus 로고    scopus 로고
    • Assessment of homogeneity in polypeptide expression in breast carcinomas shows widely variable expression in highly malignant tumors
    • Franzen, B., Auer, G., Alaiya, A. A., Eriksson, E., Uryu, K., Hirano, T., Okuzawa, K., Kato, H., and Linder, S. (1996) Assessment of homogeneity in polypeptide expression in breast carcinomas shows widely variable expression in highly malignant tumors. Int. J. Cancer 69, 408-414
    • (1996) Int. J. Cancer , vol.69 , pp. 408-414
    • Franzen, B.1    Auer, G.2    Alaiya, A.A.3    Eriksson, E.4    Uryu, K.5    Hirano, T.6    Okuzawa, K.7    Kato, H.8    Linder, S.9
  • 47
    • 0030022205 scopus 로고    scopus 로고
    • Lung fibroblast α-smooth muscle actin expression and contractile phenotype in bleomycin-induced pulmonary fibrosis
    • Zhang, H. Y., Gharaee Kermani, M., Zhang, K., Karmiol, S., and Phan, S. H. (1996) Lung fibroblast α-smooth muscle actin expression and contractile phenotype in bleomycin-induced pulmonary fibrosis. Am. J. Pathol. 148, 527-537
    • (1996) Am. J. Pathol. , vol.148 , pp. 527-537
    • Zhang, H.Y.1    Gharaee Kermani, M.2    Zhang, K.3    Karmiol, S.4    Phan, S.H.5
  • 48
    • 0036500132 scopus 로고    scopus 로고
    • Functional proteomics of transforming growth factor-β1-stimulated Mv1Lu epithelial cells: Rad51 as a target of TGFβ1-dependent regulation of DNA repair
    • Kanamoto, T., Heilman, U., Heldin, C. H., and Souchelnytskyi, S. (2002) Functional proteomics of transforming growth factor-β1-stimulated Mv1Lu epithelial cells: Rad51 as a target of TGFβ1-dependent regulation of DNA repair. EMBO J. 21, 1219-1230
    • (2002) EMBO J. , vol.21 , pp. 1219-1230
    • Kanamoto, T.1    Heilman, U.2    Heldin, C.H.3    Souchelnytskyi, S.4
  • 49
    • 0025808612 scopus 로고
    • Regulation of the expression of a secreted acidic protein rich in cysteine (SPARC) in human fibroblasts by transforming growth factor β. Comparison of transcriptional and post-transcriptional control with fibronectin and type I collagen
    • Wrana, J. L., Overall, C. M., Sodek, J. (1991) Regulation of the expression of a secreted acidic protein rich in cysteine (SPARC) in human fibroblasts by transforming growth factor β. Comparison of transcriptional and post-transcriptional control with fibronectin and type I collagen. Eur. J. Biochem. 197, 519-528
    • (1991) Eur. J. Biochem. , vol.197 , pp. 519-528
    • Wrana, J.L.1    Overall, C.M.2    Sodek, J.3
  • 50
    • 0026783009 scopus 로고
    • cDNA cloning and sequence analysis of beta ig-h3, a novel gene induced in a human adenocarcinoma cell line after treatment with transforming growth factor-β
    • Skonier, J., Neubauer, M., Madisen, L., Bennett, K., Plowman, G. D., and Purchio, A. F. (1992) cDNA cloning and sequence analysis of beta ig-h3, a novel gene induced in a human adenocarcinoma cell line after treatment with transforming growth factor-β. DNA Cell Biol. 11, 511-522
    • (1992) DNA Cell Biol. , vol.11 , pp. 511-522
    • Skonier, J.1    Neubauer, M.2    Madisen, L.3    Bennett, K.4    Plowman, G.D.5    Purchio, A.F.6
  • 51
    • 0037070101 scopus 로고    scopus 로고
    • Upregulation by retinoic acid of transforming growth factor-β-stimulated heat shock protein 27 induction in osteoblasts: Involvement of mitogen-activated protein kinases
    • Hatakeyama, D., Kozawa, O., Niwa, M., Matsuno, H., Ito, H., Kato, K., Tatematsu, N., Shibata, T., and Uematsu, T. (2002) Upregulation by retinoic acid of transforming growth factor-β-stimulated heat shock protein 27 induction in osteoblasts: Involvement of mitogen-activated protein kinases. Biochim. Biophys. Acta 1589, 15-30
    • (2002) Biochim. Biophys. Acta , vol.1589 , pp. 15-30
    • Hatakeyama, D.1    Kozawa, O.2    Niwa, M.3    Matsuno, H.4    Ito, H.5    Kato, K.6    Tatematsu, N.7    Shibata, T.8    Uematsu, T.9
  • 52
    • 0032847679 scopus 로고    scopus 로고
    • Similarities and differences in smooth muscle α-actin induction by TGF-β in smooth muscle versus non-smooth muscle cells
    • Hautmann, M. B., Adam, P. J., and Owens, G. K. (1999) Similarities and differences in smooth muscle α-actin induction by TGF-β in smooth muscle versus non-smooth muscle cells. Arterioscler. Thromb. Vasc. Biol. 19, 2049-2058
    • (1999) Arterioscler. Thromb. Vasc. Biol. , vol.19 , pp. 2049-2058
    • Hautmann, M.B.1    Adam, P.J.2    Owens, G.K.3
  • 54
    • 0033198879 scopus 로고    scopus 로고
    • Putting a new twist on actin: ADF/cofilins modulate actin dynamics
    • Bamburg, J. R., McGough, A., and Ono, S. (1999) Putting a new twist on actin: ADF/cofilins modulate actin dynamics. Trends Cell Biol. 9, 364-370
    • (1999) Trends Cell Biol. , vol.9 , pp. 364-370
    • Bamburg, J.R.1    McGough, A.2    Ono, S.3
  • 55
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard, T. D., and Borisy, G. G. (2003) Cellular motility driven by assembly and disassembly of actin filaments. Cell 112, 453-465
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 56
    • 0034722329 scopus 로고    scopus 로고
    • Phosphorylation of ADF/cofilin abolishes EGF-induced actin nucleation at the leading edge and subsequent lamellipod extension
    • Zebda, N., Bernard, O., Bailly, M., Welti, S., Lawrence, D. S., and Condeelis, J. S. (2000) Phosphorylation of ADF/cofilin abolishes EGF-induced actin nucleation at the leading edge and subsequent lamellipod extension. J. Cell Biol. 151, 1119-1128
    • (2000) J. Cell Biol. , vol.151 , pp. 1119-1128
    • Zebda, N.1    Bernard, O.2    Bailly, M.3    Welti, S.4    Lawrence, D.S.5    Condeelis, J.S.6
  • 57
    • 0024468554 scopus 로고
    • A cofilin-like protein is involved in the regulation of actin assembly in developing skeletal muscle
    • Abe, H., Ohshima, S., and Obinata, T. (1989) A cofilin-like protein is involved in the regulation of actin assembly in developing skeletal muscle. J. Biochem. 106, 696-702
    • (1989) J. Biochem. , vol.106 , pp. 696-702
    • Abe, H.1    Ohshima, S.2    Obinata, T.3
  • 58
    • 0037039167 scopus 로고    scopus 로고
    • Cofilin produces newly polymerized actin filaments that are preferred for dendritic nucleation by the Arp2/3 complex
    • Ichetovkin, I., Grant, W., and Condeelis, J. (2002) Cofilin produces newly polymerized actin filaments that are preferred for dendritic nucleation by the Arp2/3 complex. Curr. Biol. 12, 79-84
    • (2002) Curr. Biol. , vol.12 , pp. 79-84
    • Ichetovkin, I.1    Grant, W.2    Condeelis, J.3
  • 59
    • 0035928737 scopus 로고    scopus 로고
    • Inhibition of the Arp2/3 complex-nucleated actin polymerization and branch formation by tropomyosin
    • Blanchoin, L., Pollard, T. D., and Hitchcock-DeGregori, S. E. (2001) Inhibition of the Arp2/3 complex-nucleated actin polymerization and branch formation by tropomyosin. Curr. Biol. 11, 1300-1304
    • (2001) Curr. Biol. , vol.11 , pp. 1300-1304
    • Blanchoin, L.1    Pollard, T.D.2    Hitchcock-DeGregori, S.E.3
  • 60
    • 0022410877 scopus 로고
    • An actin-depolymerizing protein (destrin) from porcine kidney. Its action on F-actin containing or lacking tropomyosin
    • Nishida, E., Muneyuki, E., Maekawa, S., Ohta, Y., and Sakai, H. (1985) An actin-depolymerizing protein (destrin) from porcine kidney. Its action on F-actin containing or lacking tropomyosin. Biochemistry 24, 6624-6630
    • (1985) Biochemistry , vol.24 , pp. 6624-6630
    • Nishida, E.1    Muneyuki, E.2    Maekawa, S.3    Ohta, Y.4    Sakai, H.5
  • 61
    • 0020025754 scopus 로고
    • Tropomyosin binding to F-actin protects the F-actin from disassembly by brain actin-depolymerizing factor (ADF)
    • Bernstein, B. W., and Bamburg, J. R. (1982) Tropomyosin binding to F-actin protects the F-actin from disassembly by brain actin-depolymerizing factor (ADF). Cell Motil. 2, 11-8
    • (1982) Cell Motil. , vol.2 , pp. 11-18
    • Bernstein, B.W.1    Bamburg, J.R.2
  • 62
    • 0037128928 scopus 로고    scopus 로고
    • Tropomyosin inhibits ADF/cofilin-dependent actin filament dynamics
    • Ono, S., and Ono, K. (2002) Tropomyosin inhibits ADF/cofilin-dependent actin filament dynamics. J. Cell Biol. 156, 1065-1076
    • (2002) J. Cell Biol. , vol.156 , pp. 1065-1076
    • Ono, S.1    Ono, K.2
  • 63
    • 0036912348 scopus 로고    scopus 로고
    • Spatial regulation of actin dynamics: A tropomyosin-free, actin-rich compartment at the leading edge
    • DesMarais, V., Ichetovkin, I., Condeelis, J., and Hitchcock-DeGregori, S. E. (2002) Spatial regulation of actin dynamics: A tropomyosin-free, actin-rich compartment at the leading edge. J. Cell Sci. 115, 4649-4660
    • (2002) J. Cell Sci. , vol.115 , pp. 4649-4660
    • DesMarais, V.1    Ichetovkin, I.2    Condeelis, J.3    Hitchcock-DeGregori, S.E.4
  • 64
    • 0033895522 scopus 로고    scopus 로고
    • TGF-β superfamily members do not promote smooth muscle-specific alternative splicing, a late marker of vascular smooth muscle cell differentiation
    • King-Briggs, K. E., and Shanahan, C. M. (2000) TGF-β superfamily members do not promote smooth muscle-specific alternative splicing, a late marker of vascular smooth muscle cell differentiation. Differentiation 66, 43-48
    • (2000) Differentiation , vol.66 , pp. 43-48
    • King-Briggs, K.E.1    Shanahan, C.M.2
  • 65
    • 0032491393 scopus 로고    scopus 로고
    • HA1077, a protein kinase inhibitor, inhibits calponin phosphorylation on Ser175 in porcine coronary artery
    • Nagumo, H., Seto, M., Sakurada, K., Walsh, M. P., and Sasaki, Y. (1998) HA1077, a protein kinase inhibitor, inhibits calponin phosphorylation on Ser175 in porcine coronary artery. Eur. J. Pharmacol. 360, 257-264
    • (1998) Eur. J. Pharmacol. , vol.360 , pp. 257-264
    • Nagumo, H.1    Seto, M.2    Sakurada, K.3    Walsh, M.P.4    Sasaki, Y.5
  • 67
    • 0036605185 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation using mass spectrometry: Deciphering the phosphoproteome
    • Mann, M., Ong, S. E., Gronborg, M., Steen, H., Jensen, O. N., and Pandey, A. (2002) Analysis of protein phosphorylation using mass spectrometry: Deciphering the phosphoproteome. Trends Biotechnol. 20, 261-268
    • (2002) Trends Biotechnol. , vol.20 , pp. 261-268
    • Mann, M.1    Ong, S.E.2    Gronborg, M.3    Steen, H.4    Jensen, O.N.5    Pandey, A.6
  • 68
    • 0034634613 scopus 로고    scopus 로고
    • S100A6 and S100A11 are specific targets of the calcium- and zinc-binding S100B protein in vivo
    • Deloulme, J. C., Assard, N., Mbele, G. O., Mangin, C., Kuwano, R., and Baudier, J. (2000) S100A6 and S100A11 are specific targets of the calcium- and zinc-binding S100B protein in vivo. J. Biol. Chem. 275, 35302-35310
    • (2000) J. Biol. Chem. , vol.275 , pp. 35302-35310
    • Deloulme, J.C.1    Assard, N.2    Mbele, G.O.3    Mangin, C.4    Kuwano, R.5    Baudier, J.6
  • 69
    • 1242306225 scopus 로고    scopus 로고
    • Subcellular localization of S100A11 (S100C, calgizzarin) in developing and adult avian skeletal muscles
    • Arcuri, C., Giambanco, I., Bianchi, R., and Donato, R. (2002) Subcellular localization of S100A11 (S100C, calgizzarin) in developing and adult avian skeletal muscles. Biochim. Biophys. Acta 1600, 84-94
    • (2002) Biochim. Biophys. Acta , vol.1600 , pp. 84-94
    • Arcuri, C.1    Giambanco, I.2    Bianchi, R.3    Donato, R.4
  • 70
    • 0034909132 scopus 로고    scopus 로고
    • Up-regulation of S100C in normal human fibroblasts in the process of aging in vitro
    • Sakaguchi, M., Miyazaki, M., Kondo, T., and Namba, M. (2001) Up-regulation of S100C in normal human fibroblasts in the process of aging in vitro. Exp. Gerontol. 36, 1317-1325
    • (2001) Exp. Gerontol. , vol.36 , pp. 1317-1325
    • Sakaguchi, M.1    Miyazaki, M.2    Kondo, T.3    Namba, M.4
  • 72
    • 0035219384 scopus 로고    scopus 로고
    • Loss of nuclear localization of the S100C protein in immortalized human fibroblasts
    • Sakaguchi, M., Tsuji, T., Inoue, Y., Miyazaki, M., Namba, M., Yamada, H., and Tanaka, T. (2001) Loss of nuclear localization of the S100C protein in immortalized human fibroblasts. Radiat. Res. 155, 208-214
    • (2001) Radiat. Res. , vol.155 , pp. 208-214
    • Sakaguchi, M.1    Tsuji, T.2    Inoue, Y.3    Miyazaki, M.4    Namba, M.5    Yamada, H.6    Tanaka, T.7


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