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Volumn 11, Issue 2, 2006, Pages 135-147

Stress-induced phosphorylation of caveolin-1 and p38, and down-regulation of EGFr and ERK by the dietary lectin jacalin in two human carcinoma cell lines

Author keywords

[No Author keywords available]

Indexed keywords

CAVEOLIN 1; CHAPERONE; EPIDERMAL GROWTH FACTOR RECEPTOR; HEAT SHOCK PROTEIN 70; JACALIN; LECTIN; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; PEANUT AGGLUTININ; PROTEIN OXYGEN REGULATED PROTEIN 150; RECOMBINANT PROTEIN; STRESS ACTIVATED PROTEIN KINASE; UNCLASSIFIED DRUG;

EID: 33745460904     PISSN: 13558145     EISSN: 14661268     Source Type: Journal    
DOI: 10.1379/CSC-160R.1     Document Type: Conference Paper
Times cited : (23)

References (32)
  • 1
    • 0014212846 scopus 로고
    • Physical and chemical characterization of concanavalin A, the hemagglutinin from jack bean (Canavalia ensiformis)
    • Agrawal BB, Goldstein IJ. 1967. Physical and chemical characterization of concanavalin A, the hemagglutinin from jack bean (Canavalia ensiformis). Biochim Biophys Acta 133: 376-379.
    • (1967) Biochim Biophys Acta , vol.133 , pp. 376-379
    • Agrawal, B.B.1    Goldstein, I.J.2
  • 2
    • 0036353370 scopus 로고    scopus 로고
    • Agaricus bisporus (edible mushroom lectin) inhibits ocular fibroblast proliferation and collagen lattice contraction
    • Batterbury M, Tebbs CA, Rhodes JM, Grierson I. 2002. Agaricus bisporus (edible mushroom lectin) inhibits ocular fibroblast proliferation and collagen lattice contraction. Exp Eye Res 74: 361-370.
    • (2002) Exp Eye Res , vol.74 , pp. 361-370
    • Batterbury, M.1    Tebbs, C.A.2    Rhodes, J.M.3    Grierson, I.4
  • 4
    • 0017841656 scopus 로고
    • Identification of the dietary lectin, wheat germ agglutinin, in human intestinal contents
    • Brady PG, Vannier AM, Banwell JG. 1978. Identification of the dietary lectin, wheat germ agglutinin, in human intestinal contents. Gastroenterology 75: 236-239.
    • (1978) Gastroenterology , vol.75 , pp. 236-239
    • Brady, P.G.1    Vannier, A.M.2    Banwell, J.G.3
  • 5
    • 0346445420 scopus 로고    scopus 로고
    • Oolemmal proteomics - Identification of highly abundant heat shock proteins and molecular chaperones in the mature mouse egg and their localization on the plasma membrane
    • Calvert ME, Digilio LC, Herr JC, Coonrod SA. 2003. Oolemmal proteomics - identification of highly abundant heat shock proteins and molecular chaperones in the mature mouse egg and their localization on the plasma membrane. Reprod Biol Endocrinol 1: 27.
    • (2003) Reprod Biol Endocrinol , vol.1 , pp. 27
    • Calvert, M.E.1    Digilio, L.C.2    Herr, J.C.3    Coonrod, S.A.4
  • 6
    • 0028895533 scopus 로고
    • Direct demonstration of increased expression of Thomsen-Friedenreich (TF) antigen in colonic adenocarcinoma and ulcerative colitis mucin and its concealment in normal mucin
    • Campbell BJ, Finnie IA, Hounsell EF, Rhodes JM. 1995. Direct demonstration of increased expression of Thomsen-Friedenreich (TF) antigen in colonic adenocarcinoma and ulcerative colitis mucin and its concealment in normal mucin. J Clin Invest 95: 571-576.
    • (1995) J Clin Invest , vol.95 , pp. 571-576
    • Campbell, B.J.1    Finnie, I.A.2    Hounsell, E.F.3    Rhodes, J.M.4
  • 7
    • 0008249194 scopus 로고
    • Structural analysis of the carbohydrate chain isolated from Jacalin lectin
    • Capon C, Piller F, Wieruszeki JM, Leroy Y, Fournet B. 1990. Structural analysis of the carbohydrate chain isolated from Jacalin lectin. Carbohydr Res 199: 121-127.
    • (1990) Carbohydr Res , vol.199 , pp. 121-127
    • Capon, C.1    Piller, F.2    Wieruszeki, J.M.3    Leroy, Y.4    Fournet, B.5
  • 8
    • 1642536402 scopus 로고    scopus 로고
    • The cell surface-localized heat shock protein 70 epitope TKD induces migration and cytolytic activity selectively in human NK cells
    • Gastpar R, Gross C, Rossbacher L, Ellwart J, Riegger J, Multhoff G. 2004. The cell surface-localized heat shock protein 70 epitope TKD induces migration and cytolytic activity selectively in human NK cells. J Immunol 172: 972-980.
    • (2004) J Immunol , vol.172 , pp. 972-980
    • Gastpar, R.1    Gross, C.2    Rossbacher, L.3    Ellwart, J.4    Riegger, J.5    Multhoff, G.6
  • 9
    • 0008836984 scopus 로고    scopus 로고
    • Vicia faba agglutinin, the lectin present in broad beans, stimulates differentiation of undifferentiated colon cancer cells
    • Jordinson M, El Hariry I, Calnan D, Calam J, Pignatelli M. 1999. Vicia faba agglutinin, the lectin present in broad beans, stimulates differentiation of undifferentiated colon cancer cells. Gut 44: 709-714.
    • (1999) Gut , vol.44 , pp. 709-714
    • Jordinson, M.1    El Hariry, I.2    Calnan, D.3    Calam, J.4    Pignatelli, M.5
  • 10
    • 0032520680 scopus 로고    scopus 로고
    • Jacalin: A jackfruit (Artocarpus heterophyllus) seed-derived lectin of versatile applications in immunobiological research
    • Kabir S. 1998. Jacalin: a jackfruit (Artocarpus heterophyllus) seed-derived lectin of versatile applications in immunobiological research. J Immunol Methods 212: 193-211.
    • (1998) J Immunol Methods , vol.212 , pp. 193-211
    • Kabir, S.1
  • 12
    • 0029970952 scopus 로고    scopus 로고
    • The lectin jacalin triggers CD4-mediated lymphocyte signaling by binding CD4 through a protein-protein interaction
    • Lafont V, Dornand J, Covassin L, Liautard JP, Favero J. 1996. The lectin jacalin triggers CD4-mediated lymphocyte signaling by binding CD4 through a protein-protein interaction. J Leukoc Biol 59: 691-696.
    • (1996) J Leukoc Biol , vol.59 , pp. 691-696
    • Lafont, V.1    Dornand, J.2    Covassin, L.3    Liautard, J.P.4    Favero, J.5
  • 14
    • 0031972947 scopus 로고    scopus 로고
    • Peanut ingestion increases rectal proliferation in individuals with mucosal expression of peanut lectin receptor
    • Ryder SD, Jacyna MR, Levi AJ, Rizzi PM, Rhodes JM. 1998. Peanut ingestion increases rectal proliferation in individuals with mucosal expression of peanut lectin receptor. Gastroenterology 114: 44-49.
    • (1998) Gastroenterology , vol.114 , pp. 44-49
    • Ryder, S.D.1    Jacyna, M.R.2    Levi, A.J.3    Rizzi, P.M.4    Rhodes, J.M.5
  • 15
    • 0028137720 scopus 로고
    • Peanut lectin stimulates proliferation in colonic explants from patients with inflammatory bowel disease and colon polyps
    • Ryder SD, Parker N, Ecclestone D, Haqqani MT, Rhodes JM. 1994a. Peanut lectin stimulates proliferation in colonic explants from patients with inflammatory bowel disease and colon polyps. Gastroenterology 106: 117-124.
    • (1994) Gastroenterology , vol.106 , pp. 117-124
    • Ryder, S.D.1    Parker, N.2    Ecclestone, D.3    Haqqani, M.T.4    Rhodes, J.M.5
  • 16
    • 0026756145 scopus 로고
    • Peanut lectin: A mitogen for normal human colonic epithelium and human HT29 colorectal cancer cells
    • Ryder SD, Smith JA, Rhodes JM. 1992. Peanut lectin: a mitogen for normal human colonic epithelium and human HT29 colorectal cancer cells. J Natl Cancer Inst 84: 1410-1416.
    • (1992) J Natl Cancer Inst , vol.84 , pp. 1410-1416
    • Ryder, S.D.1    Smith, J.A.2    Rhodes, J.M.3
  • 17
    • 0028156009 scopus 로고
    • Proliferative responses of HT29 and Caco2 human colorectal cancer cells to a panel of lectins
    • Ryder SD, Smith JA, Rhodes EG, Parker N, Rhodes JM. 1994b. Proliferative responses of HT29 and Caco2 human colorectal cancer cells to a panel of lectins. Gastroenterology 106: 85-93.
    • (1994) Gastroenterology , vol.106 , pp. 85-93
    • Ryder, S.D.1    Smith, J.A.2    Rhodes, E.G.3    Parker, N.4    Rhodes, J.M.5
  • 18
    • 9344237665 scopus 로고    scopus 로고
    • Studies on recombinant single chain Jacalin lectin reveal reduced affinity for saccharides despite normal folding like native Jacalin
    • Sahasrabuddhe AA, Gaikwad SM, Krishnasastry MV, Khan MI. 2004. Studies on recombinant single chain Jacalin lectin reveal reduced affinity for saccharides despite normal folding like native Jacalin. Protein Sci 13: 3264-3273.
    • (2004) Protein Sci , vol.13 , pp. 3264-3273
    • Sahasrabuddhe, A.A.1    Gaikwad, S.M.2    Krishnasastry, M.V.3    Khan, M.I.4
  • 19
    • 0025203339 scopus 로고
    • Stimulation of vascular cell proliferation by beta-galactoside specific lectins
    • Sanford GL, Harris-Hooker S. 1990. Stimulation of vascular cell proliferation by beta-galactoside specific lectins. FASEB J 4: 2912-2918.
    • (1990) FASEB J , vol.4 , pp. 2912-2918
    • Sanford, G.L.1    Harris-Hooker, S.2
  • 20
    • 0023002029 scopus 로고
    • Analysis of saccharide binding to Artocarpus integrifolia lectin reveals specific recognition of T-antigen (beta-D-Gal(1-3)D-GalNAc)
    • Sastry MV, Banarjee P, Patanjali SR, Swamy MJ, Swarnalatha GV, Surolia A. 1986. Analysis of saccharide binding to Artocarpus integrifolia lectin reveals specific recognition of T-antigen (beta-D-Gal(1-3)D-GalNAc). J Biol Chem 261: 11726-11733.
    • (1986) J Biol Chem , vol.261 , pp. 11726-11733
    • Sastry, M.V.1    Banarjee, P.2    Patanjali, S.R.3    Swamy, M.J.4    Swarnalatha, G.V.5    Surolia, A.6
  • 21
    • 0022789423 scopus 로고
    • Intrinsic fluorescence studies on saccharide binding to Artocarpus integrifolia lectin
    • Sastry MV, Surolia A. 1986. Intrinsic fluorescence studies on saccharide binding to Artocarpus integrifolia lectin. Biosci Rep 6: 853-860.
    • (1986) Biosci Rep , vol.6 , pp. 853-860
    • Sastry, M.V.1    Surolia, A.2
  • 22
    • 0037470247 scopus 로고    scopus 로고
    • Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function
    • Shin BK, Wang H, Yim AM, et al. 2003. Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function. J Biol Chem 278: 7607-7616.
    • (2003) J Biol Chem , vol.278 , pp. 7607-7616
    • Shin, B.K.1    Wang, H.2    Yim, A.M.3
  • 23
    • 0021920805 scopus 로고
    • Biosynthesis of the epidermal growth factor receptor in cultured human cells
    • Stoscheck CM, Soderquist AM, Carpenter G. 1985. Biosynthesis of the epidermal growth factor receptor in cultured human cells. Endocrinology 116: 528-535.
    • (1985) Endocrinology , vol.116 , pp. 528-535
    • Stoscheck, C.M.1    Soderquist, A.M.2    Carpenter, G.3
  • 25
    • 0037472639 scopus 로고    scopus 로고
    • Modulation of EGF receptor autophosphorylation by alpha-hemolysin of Staphylococcus aureus via protein tyrosine phosphatase
    • Vandana S, Navneet S, Surinder K, Krishnasastry MV. 2003. Modulation of EGF receptor autophosphorylation by alpha-hemolysin of Staphylococcus aureus via protein tyrosine phosphatase. FEBS Lett 535: 71-76.
    • (2003) FEBS Lett , vol.535 , pp. 71-76
    • Vandana, S.1    Navneet, S.2    Surinder, K.3    Krishnasastry, M.V.4
  • 26
    • 0035896560 scopus 로고    scopus 로고
    • Cellular stress induces the tyrosine phosphorylation of caveolin-1 (Tyr(14)) via activation of p38 mitogen-activated protein kinase and c-Src kinase. Evidence for caveolae, the actin cytoskeleton, and focal adhesions as mechanical sensors of osmotic stress
    • Volonte D, Galbiati F, Pestell RG, Lisanti MP. 2001. Cellular stress induces the tyrosine phosphorylation of caveolin-1 (Tyr(14)) via activation of p38 mitogen-activated protein kinase and c-Src kinase. Evidence for caveolae, the actin cytoskeleton, and focal adhesions as mechanical sensors of osmotic stress. J Biol Chem 276: 8094-8103.
    • (2001) J Biol Chem , vol.276 , pp. 8094-8103
    • Volonte, D.1    Galbiati, F.2    Pestell, R.G.3    Lisanti, M.P.4
  • 27
    • 0023759583 scopus 로고
    • Increased expression of Thomsen-Friedenreich antigens during tumor progression in breast cancer patients
    • Wolf MF, Ludwig A, Fritz P, Schumacher K. 1988. Increased expression of Thomsen-Friedenreich antigens during tumor progression in breast cancer patients. Tumour Biol 9: 190-194.
    • (1988) Tumour Biol , vol.9 , pp. 190-194
    • Wolf, M.F.1    Ludwig, A.2    Fritz, P.3    Schumacher, K.4
  • 28
    • 0027483961 scopus 로고
    • Reversible inhibition of proliferation of epithelial cell lines by Agaricus bisporus (edible mushroom) lectin
    • Yu L, Fernig DG, Smith JA, Milton JD, Rhodes JM. 1993. Reversible inhibition of proliferation of epithelial cell lines by Agaricus bisporus (edible mushroom) lectin. Cancer Res 53: 4627-4632.
    • (1993) Cancer Res , vol.53 , pp. 4627-4632
    • Yu, L.1    Fernig, D.G.2    Smith, J.A.3    Milton, J.D.4    Rhodes, J.M.5
  • 29
    • 0037025319 scopus 로고    scopus 로고
    • An N-terminal truncated form of Orp150 is a cytoplasmic ligand for the anti-proliferative mushroom Agaricus bisporus lectin and is required for nuclear localization sequence-dependent nuclear protein import
    • Yu LG, Andrews N, Weldon M, et al. 2002. An N-terminal truncated form of Orp150 is a cytoplasmic ligand for the anti-proliferative mushroom Agaricus bisporus lectin and is required for nuclear localization sequence-dependent nuclear protein import. J Biol Chem 277: 24538-24545.
    • (2002) J Biol Chem , vol.277 , pp. 24538-24545
    • Yu, L.G.1    Andrews, N.2    Weldon, M.3
  • 30
    • 0033582532 scopus 로고    scopus 로고
    • Edible mushroom (Agaricus bisporus) lectin, which reversibly inhibits epithelial cell proliferation, blocks nuclear localization sequence-dependent nuclear protein import
    • Yu LG, Fernig DG, White MR, et al. 1999. Edible mushroom (Agaricus bisporus) lectin, which reversibly inhibits epithelial cell proliferation, blocks nuclear localization sequence-dependent nuclear protein import. J Biol Chem 274: 4890-4899.
    • (1999) J Biol Chem , vol.274 , pp. 4890-4899
    • Yu, L.G.1    Fernig, D.G.2    White, M.R.3
  • 31
    • 0035152508 scopus 로고    scopus 로고
    • Opposite effects on human colon cancer cell proliferation of two dietary Thomsen-Friedenreich antigen-binding lectins
    • Yu LG, Milton JD, Fernig DG, Rhodes JM. 2001. Opposite effects on human colon cancer cell proliferation of two dietary Thomsen-Friedenreich antigen-binding lectins. J Cell Physiol 186: 282-287.
    • (2001) J Cell Physiol , vol.186 , pp. 282-287
    • Yu, L.G.1    Milton, J.D.2    Fernig, D.G.3    Rhodes, J.M.4
  • 32
    • 4744352601 scopus 로고    scopus 로고
    • Protein phosphatase 2A, a negative regulator of the ERK signaling pathway, is activated by tyrosine phosphorylation of putative HLA class II-associated protein I (PHAPI)/pp32 in response to the antiproliferative lectin, jacalin
    • Yu LG, Packman LC, Weldon M, Hamlett J, Rhodes JM. 2004. Protein phosphatase 2A, a negative regulator of the ERK signaling pathway, is activated by tyrosine phosphorylation of putative HLA class II-associated protein I (PHAPI)/pp32 in response to the antiproliferative lectin, jacalin. J Biol Chem 279: 41377-41383.
    • (2004) J Biol Chem , vol.279 , pp. 41377-41383
    • Yu, L.G.1    Packman, L.C.2    Weldon, M.3    Hamlett, J.4    Rhodes, J.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.