메뉴 건너뛰기




Volumn 45, Issue 2, 2000, Pages 493-502

Galectin 1 is involved in vascular smooth muscle cell proliferation

Author keywords

Extracellular matrix; Smooth muscle

Indexed keywords

GALECTIN;

EID: 0033959858     PISSN: 00086363     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0008-6363(99)00276-X     Document Type: Article
Times cited : (95)

References (44)
  • 1
    • 0030028147 scopus 로고    scopus 로고
    • Molecular therapies for vascular diseases
    • Gibbons G.H., Dzau V.J. Molecular therapies for vascular diseases. Science. 272:1996;689-693.
    • (1996) Science , vol.272 , pp. 689-693
    • Gibbons, G.H.1    Dzau, V.J.2
  • 2
    • 0031456015 scopus 로고    scopus 로고
    • Smooth muscle migration in atherosclerosis and restenosis
    • Schwartz S.M. Smooth muscle migration in atherosclerosis and restenosis. J Clin Invest. 100S:1997;87S-89S.
    • (1997) J Clin Invest , vol.100
    • Schwartz, S.M.1
  • 3
    • 0031456944 scopus 로고    scopus 로고
    • The extracellular matrix as a cell cycle control element in atherosclerosis and restenosis
    • Assoian R.K., Marcantonio E.E. The extracellular matrix as a cell cycle control element in atherosclerosis and restenosis. J Clin Invest. 100:(11S):1997;15S-18S.
    • (1997) J Clin Invest , vol.100 , Issue.11 S
    • Assoian, R.K.1    Marcantonio, E.E.2
  • 4
    • 0030777243 scopus 로고    scopus 로고
    • Integrin signalling: Specificity and control of cell survival and cycle progression
    • Giancotti F.G. Integrin signalling: specificity and control of cell survival and cycle progression. Cur Opinion Cell Biol. 9:1997;691-700.
    • (1997) Cur Opinion Cell Biol , vol.9 , pp. 691-700
    • Giancotti, F.G.1
  • 5
    • 0030584077 scopus 로고    scopus 로고
    • The adaptor protein She couples a class of integrins to the control of cell cycle progression
    • Wary K.K., Mainiero F., Isakoff S.J., Marcantonio E.E., Giancotti F.G. The adaptor protein She couples a class of integrins to the control of cell cycle progression. Cell. 87:1996;733-743.
    • (1996) Cell , vol.87 , pp. 733-743
    • Wary, K.K.1    Mainiero, F.2    Isakoff, S.J.3    Marcantonio, E.E.4    Giancotti, F.G.5
  • 6
    • 85101730464 scopus 로고    scopus 로고
    • A requirment for caveolin-1 and associated kinase Fyn in integrin signalling and anchorage-dependent cell growth
    • Wary K.K., Mariotii A., Zurzolo C., Giancotti F.G. A requirment for caveolin-1 and associated kinase Fyn in integrin signalling and anchorage-dependent cell growth. Cell. 94:1998;6250-6254.
    • (1998) Cell , vol.94 , pp. 6250-6254
    • Wary, K.K.1    Mariotii, A.2    Zurzolo, C.3    Giancotti, F.G.4
  • 7
    • 0029876639 scopus 로고    scopus 로고
    • Adhesion-dependent cell cycle progression linked to the expression of cyclin D1, activation of cyclin E-cdk2, and phosphorylation of the retinoblastoma protein
    • Zhu X., Ohtsubo M., Bohmer R.M., Roberts J.M., Assoian R.K. Adhesion-dependent cell cycle progression linked to the expression of cyclin D1, activation of cyclin E-cdk2, and phosphorylation of the retinoblastoma protein. J Cell Biol. 133:1996;391-403.
    • (1996) J Cell Biol , vol.133 , pp. 391-403
    • Zhu, X.1    Ohtsubo, M.2    Bohmer, R.M.3    Roberts, J.M.4    Assoian, R.K.5
  • 9
    • 0030027049 scopus 로고    scopus 로고
    • Dependence of cyclin E-cdk2 kinase activity on cell anchorage
    • Fang F., Orend G., Watanabe N., Hunter T., Ruoslahti E. Dependence of cyclin E-cdk2 kinase activity on cell anchorage. Science. 271:1996;499-502.
    • (1996) Science , vol.271 , pp. 499-502
    • Fang, F.1    Orend, G.2    Watanabe, N.3    Hunter, T.4    Ruoslahti, E.5
  • 10
    • 0029347102 scopus 로고
    • Diversity of function is inherent in matricellular proteins: An appraisal of thrombospondin 1
    • Bornstein P. Diversity of function is inherent in matricellular proteins: an appraisal of thrombospondin 1. J Cell Biol. 130:1995;503-506.
    • (1995) J Cell Biol , vol.130 , pp. 503-506
    • Bornstein, P.1
  • 11
    • 0033009167 scopus 로고    scopus 로고
    • Galectin-1 modulates attachment, spreading and migration of cultured vascular smooth muscle cells via interactions with cellular receptors and components of extracellular matrix
    • Moiseeva E.P., Spring E.L., Baron J.H., de Bono D.P. Galectin-1 modulates attachment, spreading and migration of cultured vascular smooth muscle cells via interactions with cellular receptors and components of extracellular matrix. J Vasc Res. 36:1999;47-58.
    • (1999) J Vasc Res , vol.36 , pp. 47-58
    • Moiseeva, E.P.1    Spring, E.L.2    Baron, J.H.3    De Bono, D.P.4
  • 13
    • 0023355008 scopus 로고
    • Distribution of an endogenous β-galactoside-specific lectin during foetal and neonatal rabbit development
    • Catt J.W., Harrison F.L., Carleton J.S. Distribution of an endogenous β-galactoside-specific lectin during foetal and neonatal rabbit development. J Cell Sci. 87:1990;623-633.
    • (1990) J Cell Sci , vol.87 , pp. 623-633
    • Catt, J.W.1    Harrison, F.L.2    Carleton, J.S.3
  • 14
    • 0025068901 scopus 로고
    • Immunochemical localisation of 14 kDa beta-galactoside-binding lectin in various organs of rat
    • Wasano K., Hirakawa Y., Yamamoto T. Immunochemical localisation of 14 kDa beta-galactoside-binding lectin in various organs of rat. Cell Tissue Res. 1:1990;43-49.
    • (1990) Cell Tissue Res , vol.1 , pp. 43-49
    • Wasano, K.1    Hirakawa, Y.2    Yamamoto, T.3
  • 15
    • 0026079139 scopus 로고
    • Identification of an autocrine negative growth factor: Mouse β-galactoside-binding protein is a cytostatic factor and cell growth regulator
    • Wells V., Mallucci L. Identification of an autocrine negative growth factor: mouse β-galactoside-binding protein is a cytostatic factor and cell growth regulator. Cell. 64:1991;91-97.
    • (1991) Cell , vol.64 , pp. 91-97
    • Wells, V.1    Mallucci, L.2
  • 16
    • 0026001374 scopus 로고
    • Overexpression of a β-galactoside-binding protein causes transformation of BALB3T3 fibroblast cells
    • Yamaoka K., Ohno S., Kawasaki H., Suzuki K. Overexpression of a β-galactoside-binding protein causes transformation of BALB3T3 fibroblast cells. Bioch Bioph Res Com. 179:1991;272-279.
    • (1991) Bioch Bioph Res Com , vol.179 , pp. 272-279
    • Yamaoka, K.1    Ohno, S.2    Kawasaki, H.3    Suzuki, K.4
  • 17
    • 0029954457 scopus 로고    scopus 로고
    • Structural and functional characterisation of a novel tumour-derived rat galectin-1 having transforming growth factor (TGF) activity
    • Yamaoka K., Ingendoh A., Tsubuki S., Nagai Y., Sanai Y. Structural and functional characterisation of a novel tumour-derived rat galectin-1 having transforming growth factor (TGF) activity. J Biochem. 119:1996;878-886.
    • (1996) J Biochem , vol.119 , pp. 878-886
    • Yamaoka, K.1    Ingendoh, A.2    Tsubuki, S.3    Nagai, Y.4    Sanai, Y.5
  • 18
    • 0030582135 scopus 로고    scopus 로고
    • Biphasic modulation of cell growth by recombinant human galectin-1
    • Adams L., Scott G.K., Weinberg C.S. Biphasic modulation of cell growth by recombinant human galectin-1. Bioch Bioph Acta. 1312:1996;137-144.
    • (1996) Bioch Bioph Acta , vol.1312 , pp. 137-144
    • Adams, L.1    Scott, G.K.2    Weinberg, C.S.3
  • 21
    • 0026499690 scopus 로고
    • Development and characterisation of a cloned rat pulmonary arterial smooth muscle cell line that maintains differentiated properties through multiple subcultures
    • Rothman A., Kulik T.J., Taubman M.B., Berk B.C., Smith C.W.J., Nadal-Ginard B. Development and characterisation of a cloned rat pulmonary arterial smooth muscle cell line that maintains differentiated properties through multiple subcultures. Circulation. 86:1992;1977-1986.
    • (1992) Circulation , vol.86 , pp. 1977-1986
    • Rothman, A.1    Kulik, T.J.2    Taubman, M.B.3    Berk, B.C.4    Smith, C.W.J.5    Nadal-Ginard, B.6
  • 22
    • 0030863829 scopus 로고    scopus 로고
    • Characterisation of the promoter which regulates expression of a phosphoglucomutase-related protein, a component of the dystrophin/utrophin cytoskeleton, predominantly expressed in smooth muscle
    • Moiseeva E.P., Critchley D.R. Characterisation of the promoter which regulates expression of a phosphoglucomutase-related protein, a component of the dystrophin/utrophin cytoskeleton, predominantly expressed in smooth muscle. Eur J Biochem. 248:1997;634-643.
    • (1997) Eur J Biochem , vol.248 , pp. 634-643
    • Moiseeva, E.P.1    Critchley, D.R.2
  • 25
    • 0001929753 scopus 로고
    • The catabolism of extracellular matrix components
    • M.A. Haralson, & J.R. Hassell. New York, USA: Oxford University Press
    • Fisher S.J., Werb Z. The catabolism of extracellular matrix components. Haralson M.A., Hassell J.R. Extracellular matrix. A practical approach. 1995;261-287 Oxford University Press, New York, USA.
    • (1995) Extracellular Matrix. A Practical Approach , pp. 261-287
    • Fisher, S.J.1    Werb, Z.2
  • 26
    • 0032479459 scopus 로고    scopus 로고
    • Galectin-3 gene (LGALS3) expression in experimental atherosclerosis and cultured smooth muscle cells
    • Arar C., Gaudin J.-C., Capron L., Legrand A. Galectin-3 gene (LGALS3) expression in experimental atherosclerosis and cultured smooth muscle cells. FEBS Lett. 430:1998;307-311.
    • (1998) FEBS Lett , vol.430 , pp. 307-311
    • Arar, C.1    Gaudin, J.-C.2    Capron, L.3    Legrand, A.4
  • 28
    • 0029982650 scopus 로고    scopus 로고
    • Cell-specific transcriptional regulation and reactivation of galectin-1 gene expression are controlled by DNA methylation of the promoter region
    • Benvenuto G., Caprentieri M.L., Salvatore P., Cindolo L., Bruni C.B., Chiariotti L. Cell-specific transcriptional regulation and reactivation of galectin-1 gene expression are controlled by DNA methylation of the promoter region. Mol Cell Biol. 16:1996;2736-2743.
    • (1996) Mol Cell Biol , vol.16 , pp. 2736-2743
    • Benvenuto, G.1    Caprentieri, M.L.2    Salvatore, P.3    Cindolo, L.4    Bruni, C.B.5    Chiariotti, L.6
  • 29
    • 0031500199 scopus 로고    scopus 로고
    • Galectin-1: Secretion and modulation of cell interactions with laminin
    • Cooper D.N.W. Galectin-1: secretion and modulation of cell interactions with laminin. Trends Glycoscience Glycotechnology. 9:1997;57-67.
    • (1997) Trends Glycoscience Glycotechnology , vol.9 , pp. 57-67
    • Cooper, D.N.W.1
  • 30
    • 0025372418 scopus 로고
    • The S-type lectin from calf heart tissue binds selectively to the carbohydrate chains of laminin
    • Zhou Q., Cummings R.D. The S-type lectin from calf heart tissue binds selectively to the carbohydrate chains of laminin. Archives Biochem Biophys. 281:1990;27-35.
    • (1990) Archives Biochem Biophys , vol.281 , pp. 27-35
    • Zhou, Q.1    Cummings, R.D.2
  • 32
    • 0028053242 scopus 로고
    • Selective modulation of the interaction of integrin with fibronectin and laminin by L14 lectin during muscle differentiation
    • Gu M., Wang W., Song W.K., Cooper D.N.W., Kaufman S.J. Selective modulation of the interaction of integrin with fibronectin and laminin by L14 lectin during muscle differentiation. J Cell Sci. 107:1994;175-181.
    • (1994) J Cell Sci , vol.107 , pp. 175-181
    • Gu, M.1    Wang, W.2    Song, W.K.3    Cooper, D.N.W.4    Kaufman, S.J.5
  • 33
    • 0025569426 scopus 로고
    • Lamp-1 in CHO cells is a primary carrier of poly-N-acetyllactosamine chains and is bound preferentially by a mammalian S-type lectin
    • Do K.Y., Smith D.F., Cummings R.D. Lamp-1 in CHO cells is a primary carrier of poly-N-acetyllactosamine chains and is bound preferentially by a mammalian S-type lectin. Bioch Bioph Res Comm. 173:1990;1123-1128.
    • (1990) Bioch Bioph Res Comm , vol.173 , pp. 1123-1128
    • Do, K.Y.1    Smith, D.F.2    Cummings, R.D.3
  • 34
    • 0027158151 scopus 로고
    • Galaptin-mediated attachment of human ovarian carcinoma A121 cells and detection of the cellular galaptin-binding glycoproteins
    • Skrincosky D.M., Allen H.J., Bernacki R.J. Galaptin-mediated attachment of human ovarian carcinoma A121 cells and detection of the cellular galaptin-binding glycoproteins. Cancer Res. 53:1993;2667-2675.
    • (1993) Cancer Res , vol.53 , pp. 2667-2675
    • Skrincosky, D.M.1    Allen, H.J.2    Bernacki, R.J.3
  • 35
    • 0027945617 scopus 로고
    • Concomitant increases in galectin-1 and its glycoconjugate ligands in cultured human colon-carcinoma cells by sodium-butyrate
    • Ohannesian D.W., Lotan D., Lotan R. Concomitant increases in galectin-1 and its glycoconjugate ligands in cultured human colon-carcinoma cells by sodium-butyrate. Cancer Res. 54:1994;5992-6000.
    • (1994) Cancer Res , vol.54 , pp. 5992-6000
    • Ohannesian, D.W.1    Lotan, D.2    Lotan, R.3
  • 36
    • 0032577178 scopus 로고    scopus 로고
    • Regulation of cellular adhesion to extracellular matrix proteins by galectin 3
    • Ochieng J., Leite-Browning M.L., Warfield P. Regulation of cellular adhesion to extracellular matrix proteins by galectin 3. Bioch Biophys Res Comm. 246:1998;788-791.
    • (1998) Bioch Biophys Res Comm , vol.246 , pp. 788-791
    • Ochieng, J.1    Leite-Browning, M.L.2    Warfield, P.3
  • 37
    • 0031482246 scopus 로고    scopus 로고
    • Galectin-1: Oligomeric structure and interactions with polylactosamine
    • Cho M., Cummings R.D. Galectin-1: oligomeric structure and interactions with polylactosamine. Trends Glycoscience Glycotechnology. 9:1997;47-56.
    • (1997) Trends Glycoscience Glycotechnology , vol.9 , pp. 47-56
    • Cho, M.1    Cummings, R.D.2
  • 39
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in E. coli as fusions with glutathione S-transferase
    • Smith D.B., Johnson K.S. Single-step purification of polypeptides expressed in E. coli as fusions with glutathione S-transferase. Gene. 67:1988;31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 40
    • 0028593398 scopus 로고
    • 3-Dimensional structure of Schistosoma-japonicum glutathione-S-transferase fused with a 6-amino acid conserved neutralizing epitope of gp41 from HIV
    • Lim K., Ho J.X., Keeling K., Gilliland G.L., Ji X.H., Ruker F., Carter D.C. 3-Dimensional structure of Schistosoma-japonicum glutathione-S-transferase fused with a 6-amino acid conserved neutralizing epitope of gp41 from HIV. Protein Sci. 3:1994;2233-2244.
    • (1994) Protein Sci , vol.3 , pp. 2233-2244
    • Lim, K.1    Ho, J.X.2    Keeling, K.3    Gilliland, G.L.4    Ji, X.H.5    Ruker, F.6    Carter, D.C.7
  • 43
    • 0022001366 scopus 로고
    • Light microscopic immunolocation of thrombospondin in human tissues
    • Wight T.N., Raugi G.J., Mumby S.M., Borstein P. Light microscopic immunolocation of thrombospondin in human tissues. J Histochem Cytochem. 33:1985;295-302.
    • (1985) J Histochem Cytochem , vol.33 , pp. 295-302
    • Wight, T.N.1    Raugi, G.J.2    Mumby, S.M.3    Borstein, P.4
  • 44
    • 0031713365 scopus 로고    scopus 로고
    • Fibronectin: Structure, assembly and cardiovascular implications
    • Magnusson M.K., Mosher D.F. Fibronectin: structure, assembly and cardiovascular implications. Arterioscler Throm Vasc Biol. 18:1998;1363-1370.
    • (1998) Arterioscler Throm Vasc Biol , vol.18 , pp. 1363-1370
    • Magnusson, M.K.1    Mosher, D.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.