메뉴 건너뛰기




Volumn 10, Issue 3, 2000, Pages 149-158

Expression of galectin-3 in cells exposed to stress - Roles of Jun and NF-κB

Author keywords

Galectin 3; Jun; Nf b; Stress; UV

Indexed keywords

ALKYLATING AGENT; DIFFERENTIATION ANTIGEN; GALECTIN 3; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; PROTEIN C JUN; TRYPSIN;

EID: 0033655187     PISSN: 10158987     EISSN: None     Source Type: Journal    
DOI: 10.1159/000016345     Document Type: Article
Times cited : (66)

References (37)
  • 1
    • 0020058758 scopus 로고
    • Mac-2, a novel 32,000 Mr mouse macrophage subpopulationspecific antigen defined by monoclonal antibodies
    • Ho MK, Springer TA: Mac-2, a novel 32,000 Mr mouse macrophage subpopulationspecific antigen defined by monoclonal antibodies. J Immunol 1982;128:1221-8.
    • (1982) J Immunol , vol.128 , pp. 1221-1228
    • Springer Ta, H.M.K.1
  • 2
    • 0023406938 scopus 로고
    • SchindlerM, Wang JL Endogenous lectins from cultured cells nuclear localization of carbohydrate-binding protein 35 in proliferating 3T3 fibroblasts
    • Moutsatsos IK, Wade M.SchindlerM, Wang JL: Endogenous lectins from cultured cells: nuclear localization of carbohydrate-binding protein 35 in proliferating 3T3 fibroblasts. Proc Natl Acad Sci USA 1987;84:6452-6.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 6452-6456
    • Wade M, M.I.K.1
  • 3
    • 0032967450 scopus 로고    scopus 로고
    • GaIectin-3 and polarized growth within collagen gels of wild-type and ricin-résistant MDCK renal epithelial cells
    • Bao Q, Hughes RC: GaIectin-3 and polarized growth within collagen gels of wild-type and ricin-résistant MDCK renal epithelial cells. Glycobiology 1999;9:489-95.
    • (1999) Glycobiology , vol.9 , pp. 489-495
    • Hughes Rc, B.Q.1
  • 4
    • 0029102299 scopus 로고
    • Functional evidence that cell surface galectin-3 mediates homotypic cell adhesion
    • Inohara H, Raz A: Functional evidence that cell surface galectin-3 mediates homotypic cell adhesion. Cancer Res 1995;55:3267-71.
    • (1995) Cancer Res , vol.55 , pp. 3267-3271
    • Raz A, I.H.1
  • 5
    • 0022624749 scopus 로고
    • Differential expression of endogenous lectins on the surface of nontumorigenic, rumorigenic, and metastatic cells
    • Raz A, Meromsky L, Lotan R: Differential expression of endogenous lectins on the surface of nontumorigenic, rumorigenic, and metastatic cells. Cancer Res 1986;46:366772.
    • (1986) Cancer Res , vol.46 , pp. 366772
    • Raz, A.1    Meromsky, L.2    Lotan, R.3
  • 7
    • 0023952291 scopus 로고
    • Carbohydrate binding protein 35. Complementary DNA sequence reveals homology with proteins of the heterogeneous nuclear RNP
    • Jia S, Wang JL: Carbohydrate binding protein 35. Complementary DNA sequence reveals homology with proteins of the heterogeneous nuclear RNP. J Biol Chem 1988;263:6009-11.
    • (1988) J Biol Chem , vol.263 , pp. 6009-6011
    • Wang Jl, J.S.1
  • 8
    • 0006522290 scopus 로고    scopus 로고
    • Galectins - A new family of lectins
    • Laue G, Flöge! M: Galectins - a new family of lectins. Croat Chem Acta 1996;69:33952.
    • (1996) Croat Chem Acta , vol.69 , pp. 33952
    • Flöge M, L.G.1
  • 9
    • 0027225381 scopus 로고
    • Secretion of the baby hamster kidney 30-kDa galactosebinding lectin from polarized and nonpolarized cells a pathway independent of the endoplasmic reticuIum-Golgi complex
    • Sato S, Burdett I, Hughes RC: Secretion of the baby hamster kidney 30-kDa galactosebinding lectin from polarized and nonpolarized cells: a pathway independent of the endoplasmic reticuIum-Golgi complex. Exp Cell Res 1993;207:8-18.
    • (1993) Exp Cell Res , vol.207 , pp. 8-18
    • Sato, S.1    Burdett, I.2    Hughes, R.C.3
  • 10
    • 0033199579 scopus 로고    scopus 로고
    • Determinants in the N-terminal domains of galectin-3 for secretion by a novel pathway circumventing the endoplasmic reticulum-GoIgi complex
    • Menon RP, Hughes RC: Determinants in the N-terminal domains of galectin-3 for secretion by a novel pathway circumventing the endoplasmic reticulum-GoIgi complex. Eur J Biochem 1999;264:569-76.
    • (1999) Eur J Biochem , vol.264 , pp. 569-576
    • Hughes Rc, M.R.P.1
  • 12
    • 0026523484 scopus 로고
    • Nuclear and cytoplasmic localization of a lectin-ribonucleoprotein complex
    • Wang JL, Werner EA, Laing JG, Patterson RJ: Nuclear and cytoplasmic localization of a lectin-ribonucleoprotein complex. Biochem Soc Trans 1992;20:269-74.
    • (1992) Biochem Soc Trans , vol.20 , pp. 269-274
    • Wang, J.L.1    Werner, E.A.2    Laing, J.G.3    Patterson, R.J.4
  • 13
    • 0031819671 scopus 로고    scopus 로고
    • The human LGALS3 (galectin-3) gene determination of the gene structure and functional characterization of the promoter
    • Kadrofske MM, Openo KP, Wang JL: The human LGALS3 (galectin-3) gene: determination of the gene structure and functional characterization of the promoter. Arch Biochem Biophys 1998;349:7-20.
    • (1998) Arch Biochem Biophys , vol.349 , pp. 7-20
    • Kadrofske, M.M.1    Kp, O.2    Wang, J.L.3
  • 14
    • 0033057848 scopus 로고    scopus 로고
    • Heat-shock proteins, molecular chaperones, and the stress response evolutionary and ecological physiology
    • Feder ME, Hofmann GE: Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology. Int J Cancer 1999;61:243-82.
    • (1999) Int J Cancer , vol.61 , pp. 243-282
    • Hofmann Ge, F.M.E.1
  • 16
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interactions with heat shock protein and immunophilin chaperones
    • Pratt WB, Toft DO: Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocrin Rev 1997;18:306-60.
    • (1997) Endocrin Rev , vol.18 , pp. 306-360
    • Toft Do, P.W.B.1
  • 17
    • 0032533212 scopus 로고    scopus 로고
    • Dexamethasone protection of rat intestinal epithelial cells against oxidant injury is mediated by induction of heat shock protein 72
    • Urayama S, Musch MW, Retsky J, Madonna MB, Straus D, Chang EB: Dexamethasone protection of rat intestinal epithelial cells against oxidant injury is mediated by induction of heat shock protein 72. J Clin Invest 1998;102:1860-5.
    • (1998) J Clin Invest , vol.102 , pp. 1860-1865
    • Urayama, S.1    Musch, M.W.2    Retsky, J.3    Madonna, M.B.4    Straus, D.5    Chang, E.B.6
  • 18
    • 0029864979 scopus 로고    scopus 로고
    • Tissue-specific regulation of sialyltransferase activities in the rat by corticosteroids in vivo
    • Coughlan CM, Seckl JR, Fox DJ, Unsworth R, Breen KC: Tissue-specific regulation of sialyltransferase activities in the rat by corticosteroids in vivo. Glycobiology 1996;6:15-22.
    • (1996) Glycobiology , vol.6 , pp. 15-22
    • Coughlan, C.M.1    Seckl, J.R.2    Fox, D.J.3    Unsworth, R.4    Breen, K.C.5
  • 19
    • 0033324859 scopus 로고    scopus 로고
    • Glycosylation of glycoprotein GP62 in the stress response
    • Dumias J, Laue G, Flögel M: Glycosylation of glycoprotein GP62 in the stress response. Glycoconjugate J 1999; 16:685-9.
    • (1999) Glycoconjugate J , vol.16 , pp. 685-689
    • Dumias, J.1    Laue, G.2    Flögel, M.3
  • 21
    • 33744872171 scopus 로고    scopus 로고
    • Glycobiology of stress
    • (Fink, G, eds) San Diego Academic Press
    • Laue G, Flögel M: Glycobiology of stress. In Encyclopedia of stress. (Fink, G, eds) San Diego: Academic Press, 2000, pp 27682.
    • (2000) In Encyclopedia of Stress. , pp. 27682
    • Flögel M, L.G.1
  • 22
    • 0029858078 scopus 로고    scopus 로고
    • GrimbergenJ.BosmaPJ, Rahmsdorf HJ, Kooistra T Role of c-Jun and proximal phorbol 12-myristate-13-acetate-(PMA)responsive elements in the regulation of basai and PMA-stimulated plasminogen-activator inhibitor-1 gene expression in HepG2
    • Arts J.GrimbergenJ.BosmaPJ, Rahmsdorf HJ, Kooistra T: Role of c-Jun and proximal phorbol 12-myristate-13-acetate-(PMA)responsive elements in the regulation of basai and PMA-stimulated plasminogen-activator inhibitor-1 gene expression in HepG2. Eur J Biochem 1996;241:393-402.
    • (1996) Eur J Biochem , vol.241 , pp. 393-402
    • Arts, J.1
  • 23
    • 0031010398 scopus 로고    scopus 로고
    • Covalent modification of the active site threonine of proteasomal beta subunits and thé Escherichia coli homolog HslV by a new class of inhibitors
    • Bogyo M, McMaster JS, Gaczynska M, Tortorella D, Goldberg AL, Ploegh H: Covalent modification of the active site threonine of proteasomal beta subunits and thé Escherichia coli homolog HslV by a new class of inhibitors. Proc Natl Acad Sci USA 1997;94:6629-34.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6629-6634
    • Bogyo, M.1    McMaster, J.S.2    Gaczynska, M.3    Tortorella, D.4    Goldberg, A.L.5    Ploegh, H.6
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemnili UK: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970;227:680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemnili, U.K.1
  • 26
    • 0031906550 scopus 로고    scopus 로고
    • Signal transduction through NF-kappa B
    • May MJ, Ghosh S: Signal transduction through NF-kappa B. Immunol Today 1998;19:80-8.
    • (1998) Immunol Today , vol.19 , pp. 80-88
    • Ghosh S, M.M.J.1
  • 27
    • 0032573165 scopus 로고    scopus 로고
    • Ionizing radiation and short wavelength UV activate NF-kappaB through two distinct mechanisms
    • Li N, Karin M: Ionizing radiation and short wavelength UV activate NF-kappaB through two distinct mechanisms. Proc Natl Acad Sci USA 1998;95:13012-7.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 13012-13017
    • Karin M, L.N.1
  • 28
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • Apweiler R, Hermjakob H, Sharon N: On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochem Biophys Acta 1999:1473:4-8.
    • (1999) Biochem Biophys Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 29
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides all of the theories are correct
    • Varki A: Biological roles of oligosaccharides: all of the theories are correct. Glycobiology 1993;3:97-130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 30
    • 0029166638 scopus 로고
    • Glycobiology of the cell surface the emergence of sugars as an important feature of the cell periphery
    • Cook GM: Glycobiology of the cell surface: the emergence of sugars as an important feature of the cell periphery. Glycobiology 1995;5:449-58.
    • (1995) Glycobiology , vol.5 , pp. 449-458
    • Cook, G.M.1
  • 31
    • 0008449836 scopus 로고    scopus 로고
    • Glycosylation in stress and disease
    • Laue G, Flögel M: Glycosylation in stress and disease. Period Biol 1996;98:279-87.
    • (1996) Period Biol , vol.98 , pp. 279-287
    • Flögel M, L.G.1
  • 32
    • 0032168441 scopus 로고    scopus 로고
    • Evolving views of protein glycosylation
    • Drickamer K, Taylor ME: Evolving views of protein glycosylation. Trends Biochem Sci 1998;23:321-4.
    • (1998) Trends Biochem Sci , vol.23 , pp. 321-324
    • Taylor Me, D.K.1
  • 33
    • 0029934119 scopus 로고    scopus 로고
    • Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes
    • Hebert DN, Foellmer B, Helenius A: Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes. EMBO Journal 1996;15:29618.
    • (1996) EMBO Journal , vol.15 , pp. 29618
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 34
    • 0029001510 scopus 로고
    • Selectin-carbohydrate interactions and the initiation of the inflammatory response
    • Lasky LA: Selectin-carbohydrate interactions and the initiation of the inflammatory response. Annu Rev Biochem 1995;64:113-39.
    • (1995) Annu Rev Biochem , vol.64 , pp. 113-139
    • Lasky, L.A.1
  • 35
    • 0024496396 scopus 로고
    • Trypsinization and the radiosensitivity of mitotic and log phase Chinese hamster V79 cells exposed to 250 kVp X-rays
    • Reddy NM, Stevenson AF, Lange CS: Trypsinization and the radiosensitivity of mitotic and log phase Chinese hamster V79 cells exposed to 250 kVp X-rays. Int J Rad Biol 1989;55:105-17.
    • (1989) Int J Rad Biol , vol.55 , pp. 105-117
    • Reddy, N.M.1    Stevenson, A.F.2    Lange, C.S.3
  • 36
    • 0016771354 scopus 로고
    • Effect of cell trypsinization on nuclear proteins of WI38 fibroblasts in culture
    • Maizel A, Nicolini C, Baserga R: Effect of cell trypsinization on nuclear proteins of WI38 fibroblasts in culture. J Cell Physiol 1975:86:71-82.
    • (1975) J Cell Physiol , vol.86 , pp. 71-82
    • Maizel, A.1    Nicolini, C.2    Baserga, R.3
  • 37
    • 0018424099 scopus 로고
    • Changes in cellular heat and/or radiation sensitivity observed at various times after trypsinization and plating
    • Raaphorst OP, Sapareto SA, Freeman ML, Dewey WC: Changes in cellular heat and/or radiation sensitivity observed at various times after trypsinization and plating. Int J Rad Biol 1979;35:193-7.
    • (1979) Int J Rad Biol , vol.35 , pp. 193-197
    • Raaphorst, O.P.1    Sapareto, S.A.2    Freeman, M.L.3    Dewey, W.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.