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Volumn 134, Issue 5, 2004, Pages 1157-1161

Dietary Soy Sphingolipids Suppress Tumorigenesis and Gene Expression in 1,2-Dimethylhydrazine-Treated CF1 Mice and ApcMin/+ Mice

Author keywords

Colon cancer; Gene expression; Mouse models; Soy; Sphingolipids

Indexed keywords

1,2 DIMETHYLHYDRAZINE; GLUCOSYLCERAMIDE; HYPOXIA INDUCIBLE FACTOR 1ALPHA; MESSENGER RNA; PALMITIC ACID; SPHINGOLIPID; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR 4; UNCLASSIFIED DRUG;

EID: 2442571212     PISSN: 00223166     EISSN: None     Source Type: Journal    
DOI: 10.1093/jn/134.5.1157     Document Type: Conference Paper
Times cited : (125)

References (51)
  • 2
    • 0014422454 scopus 로고
    • Metabolism of sphingomyelin in the intestinal tract of the rat
    • Nilsson, Å. (1968) Metabolism of sphingomyelin in the intestinal tract of the rat. Biochim. Biophys. Acta 164: 575-584.
    • (1968) Biochim. Biophys. Acta , vol.164 , pp. 575-584
    • Nilsson, Å.1
  • 3
    • 0014694801 scopus 로고
    • Metabolism of cerebrosides in the intestinal tract of the rat
    • Nilsson, Å. (1969) Metabolism of cerebrosides in the intestinal tract of the rat. Biochim. Biophys. Acta 187: 113-121.
    • (1969) Biochim. Biophys. Acta , vol.187 , pp. 113-121
    • Nilsson, Å.1
  • 4
    • 0028235958 scopus 로고
    • Uptake and metabolism of sphingolipids in isolated intestinal loops of mice
    • Schmelz, E. M., Crall, K. J., Larocque, R., Dillehay, D. L. & Merrill, A. H., Jr. (1994) Uptake and metabolism of sphingolipids in isolated intestinal loops of mice. J. Nutr. 124: 702-712.
    • (1994) J. Nutr. , vol.124 , pp. 702-712
    • Schmelz, E.M.1    Crall, K.J.2    Larocque, R.3    Dillehay, D.L.4    Merrill Jr., A.H.5
  • 5
    • 0042419991 scopus 로고    scopus 로고
    • Digestion of maize sphingolipids in rats and uptake of sphingadienine by Caco-2 cells
    • Sugawara, T., Kinoshita, M., Ohnishi, M., Nagata, J. & Saito, M. (2003) Digestion of maize sphingolipids in rats and uptake of sphingadienine by Caco-2 cells. J. Nutr. 133: 2777-2782.
    • (2003) J. Nutr. , vol.133 , pp. 2777-2782
    • Sugawara, T.1    Kinoshita, M.2    Ohnishi, M.3    Nagata, J.4    Saito, M.5
  • 7
    • 0002043424 scopus 로고    scopus 로고
    • Sphingolipids: Mechanism-based inhibitors of carcinogenesis produces by animals, plants and other organisms
    • (Wildman, R.E.C.). CRC Press, Boca Raton, FL
    • Merrill, A. H., Jr. & Schmelz, E. M. (2000) Sphingolipids: mechanism-based inhibitors of carcinogenesis produces by animals, plants and other organisms. In: Handbook of Nutraceutical and Functional Foods (Wildman, R.E.C.), pp. 377-391. CRC Press, Boca Raton, FL.
    • (2000) Handbook of Nutraceutical and Functional Foods , pp. 377-391
    • Merrill Jr., A.H.1    Schmelz, E.M.2
  • 8
    • 0037203316 scopus 로고    scopus 로고
    • Sphingosine in apoptosis signaling
    • Cuvillier, O. (2002) Sphingosine in apoptosis signaling. Biochim. Biophys. Acta 1585: 153-162.
    • (2002) Biochim. Biophys. Acta , vol.1585 , pp. 153-162
    • Cuvillier, O.1
  • 9
    • 0037203342 scopus 로고    scopus 로고
    • Ceramide in apoptosis: An overview and current perspectives
    • Pettus, B. J., Chalfant, C. E. & Hannun, Y. A. (2000) Ceramide in apoptosis: an overview and current perspectives. Biochim. Biophys. Acta 1585: 114-125.
    • (2000) Biochim. Biophys. Acta , vol.1585 , pp. 114-125
    • Pettus, B.J.1    Chalfant, C.E.2    Hannun, Y.A.3
  • 10
    • 0022974603 scopus 로고
    • Sphingosine inhibition of protein kinase C activity and of phorbol dibutyrate binding in vitro and in human platelets
    • Hannun, Y. A., Loomis, C. R., Merrill, A. H., Jr. & Bell, R. M. (1986) Sphingosine inhibition of protein kinase C activity and of phorbol dibutyrate binding in vitro and in human platelets. J. Biol. Chem. 261: 12604-12609.
    • (1986) J. Biol. Chem. , vol.261 , pp. 12604-12609
    • Hannun, Y.A.1    Loomis, C.R.2    Merrill Jr., A.H.3    Bell, R.M.4
  • 11
    • 15844387528 scopus 로고    scopus 로고
    • Ceramidese inactivates cellular protein kinase Cα
    • Lee, J. Y., Hannun, Y. A. & Obeid, L. M. (1996) Ceramidese inactivates cellular protein kinase Cα. J. Biol. Chem. 21: 13169-13174.
    • (1996) J. Biol. Chem. , vol.21 , pp. 13169-13174
    • Lee, J.Y.1    Hannun, Y.A.2    Obeid, L.M.3
  • 12
    • 0036479251 scopus 로고    scopus 로고
    • Ceramide-induced inhibition of Akt is mediated through protein kinese Cξ: Implications for growth arrest
    • Bourbon, N. A., Sandrasegarane, L. & Kester, M. (2002) Ceramide-induced inhibition of Akt is mediated through protein kinese Cξ: implications for growth arrest. J. Biol. Chem. 277: 3286-3292.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3286-3292
    • Bourbon, N.A.1    Sandrasegarane, L.2    Kester, M.3
  • 13
    • 0033617315 scopus 로고    scopus 로고
    • A novel pathway for tumor necrosis factor-α and ceramide signaling involving sequential activation of tyrosine kinase, p21(ras), and phosphatidylinositol 3 kinase
    • Hanna, A. N., Chan, E.Y.W., Xu, J., Stone, J. C. & Brindley, D. N. (1999) A novel pathway for tumor necrosis factor-α and ceramide signaling involving sequential activation of tyrosine kinase, p21(ras), and phosphatidylinositol 3 kinase. J. Biol. Chem. 274: 12722-12729.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12722-12729
    • Hanna, A.N.1    Chan, E.Y.W.2    Xu, J.3    Stone, J.C.4    Brindley, D.N.5
  • 14
    • 0037070603 scopus 로고    scopus 로고
    • Involvement of phosphatidylinositol 3-kinase in nuclear translocation of protein kinase C zeta induced by C2-ceramide in rat hepatocytes
    • Calcerrada, M. C., Miguel, B. G., Martin, L., Catalan, R. E. & Martinez, A. M. (2002) Involvement of phosphatidylinositol 3-kinase in nuclear translocation of protein kinase C zeta induced by C2-ceramide in rat hepatocytes. FEBS Lett. 514: 361-365.
    • (2002) FEBS Lett. , vol.514 , pp. 361-365
    • Calcerrada, M.C.1    Miguel, B.G.2    Martin, L.3    Catalan, R.E.4    Martinez, A.M.5
  • 15
  • 16
    • 0037066727 scopus 로고    scopus 로고
    • De novo ceramide regulates the alternative splicing of caspase 9 and Bcl-x in A549 lung adenocarcinoma cells. Dependence on protein phosphatase-1
    • Chalfant, C. E., Rathman, K., Pinkerman, R. L., Wood, R. E., Obeid, L. M., Ogretmen, B. & Hannun, Y. A. (2002) De novo ceramide regulates the alternative splicing of caspase 9 and Bcl-x in A549 lung adenocarcinoma cells. Dependence on protein phosphatase-1. J. Biol. Chem. 277: 12587-12595.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12587-12595
    • Chalfant, C.E.1    Rathman, K.2    Pinkerman, R.L.3    Wood, R.E.4    Obeid, L.M.5    Ogretmen, B.6    Hannun, Y.A.7
  • 17
    • 0034672232 scopus 로고    scopus 로고
    • Regulation of cyclin-dependent kinase activity by ceramide
    • Lee, J. Y., Bielawska, A. E. & Obeid, L. M. (2000) Regulation of cyclin-dependent kinase activity by ceramide. Exp. Cell Res. 261: 303-311.
    • (2000) Exp. Cell Res. , vol.261 , pp. 303-311
    • Lee, J.Y.1    Bielawska, A.E.2    Obeid, L.M.3
  • 19
    • 0028304788 scopus 로고
    • Dietary sphingomyelin inhibits 1,2-dimethylhydrazine-induced colon cancer in CF1 mice
    • Dillehay, D. L., Webb, S. K., Schmelz, E. M. & Merrill A. H., Jr. (1994) Dietary sphingomyelin inhibits 1,2-dimethylhydrazine-induced colon cancer in CF1 mice. J. Nutr. 124: 615-620.
    • (1994) J. Nutr. , vol.124 , pp. 615-620
    • Dillehay, D.L.1    Webb, S.K.2    Schmelz, E.M.3    Merrill Jr., A.H.4
  • 20
    • 0029953485 scopus 로고    scopus 로고
    • Sphingomyelin consumption suppresses aberrant colonic crypt foci and increases the proportion of adenomas versus adenocarcinomas in CF1 mice treated with 1,2-dimethylhydrazine: Implications for dietary sphingolipids and colon carcinogenesis
    • Schmelz, E. M., Dillehay, D. L., Webb, S. K., Reiter, A., Adams, J. & Merrill, A. H., Jr. (1996) Sphingomyelin consumption suppresses aberrant colonic crypt foci and increases the proportion of adenomas versus adenocarcinomas in CF1 mice treated with 1,2-dimethylhydrazine: implications for dietary sphingolipids and colon carcinogenesis. Cancer Res. 56: 4935-4941.
    • (1996) Cancer Res. , vol.56 , pp. 4935-4941
    • Schmelz, E.M.1    Dillehay, D.L.2    Webb, S.K.3    Reiter, A.4    Adams, J.5    Merrill Jr., A.H.6
  • 21
    • 0033998537 scopus 로고    scopus 로고
    • Colonic cell proliferation and aberrant crypt formation are inhibited by dairy glycosphingolipids in 1,2-dimethylhydrazine-treated CF1 mice
    • Schmelz, E. M., Sullards, M. C., Dillehay, D. L. & Merrill, A. H., Jr. (2000) Colonic cell proliferation and aberrant crypt formation are inhibited by dairy glycosphingolipids in 1,2-dimethylhydrazine-treated CF1 mice. J. Nutr. 130: 522-527.
    • (2000) J. Nutr. , vol.130 , pp. 522-527
    • Schmelz, E.M.1    Sullards, M.C.2    Dillehay, D.L.3    Merrill Jr., A.H.4
  • 22
    • 0030818728 scopus 로고    scopus 로고
    • Suppression of aberrant colonic crypt foci by synthetic sphingomyelins with saturated or unsaturated sphingoid base backbone
    • Schmelz, E. M., Bushnev, A. S., Dillehay, D. L., Liotta, D. C. & Merrill, A. H., Jr. (1997) Suppression of aberrant colonic crypt foci by synthetic sphingomyelins with saturated or unsaturated sphingoid base backbone. Nutr. Cancer 28: 81-85.
    • (1997) Nutr. Cancer , vol.28 , pp. 81-85
    • Schmelz, E.M.1    Bushnev, A.S.2    Dillehay, D.L.3    Liotta, D.C.4    Merrill Jr., A.H.5
  • 24
    • 0035884179 scopus 로고    scopus 로고
    • Modulation of intracellular beta-catenin localization and intestinal tumorigenesis in vivo and in vitro by sphingolipids
    • Schmelz, E. M., Roberts, P. C., Kustin, E. M., Lemonnier, L. A., Sullards, M. C., Dillehay, D. L. & Merrill, A. H., Jr. (2001) Modulation of intracellular beta-catenin localization and intestinal tumorigenesis in vivo and in vitro by sphingolipids. Cancer Res. 61: 6723-6729.
    • (2001) Cancer Res. , vol.61 , pp. 6723-6729
    • Schmelz, E.M.1    Roberts, P.C.2    Kustin, E.M.3    Lemonnier, L.A.4    Sullards, M.C.5    Dillehay, D.L.6    Merrill Jr., A.H.7
  • 25
    • 0031557898 scopus 로고    scopus 로고
    • The adenomatous polyposis coli (APC) tumor suppressor
    • Polakis, P. (1997) The adenomatous polyposis coli (APC) tumor suppressor. Biochim. Biophys. Acta 1332: F127-F147.
    • (1997) Biochim. Biophys. Acta , vol.1332
    • Polakis, P.1
  • 26
    • 0034101550 scopus 로고    scopus 로고
    • Structure determination of soybean and wheat glucosylceramides by tandem mass spectroscopy
    • Sullards, M. C., Lynch, D. V., Merrill, A. H. & Adams, J. (2000) Structure determination of soybean and wheat glucosylceramides by tandem mass spectroscopy. J. Mass Spectrom. 35: 347-353.
    • (2000) J. Mass Spectrom. , vol.35 , pp. 347-353
    • Sullards, M.C.1    Lynch, D.V.2    Merrill, A.H.3    Adams, J.4
  • 28
    • 0017375321 scopus 로고
    • Report of the American Institute of Nutrition ad hoc committee on standards for nutritional studies
    • American Institute of Nutrition (1977) Report of the American Institute of Nutrition ad hoc committee on standards for nutritional studies. J. Nutr. 107: 1340-1348.
    • (1977) J. Nutr. , vol.107 , pp. 1340-1348
  • 29
    • 0033571163 scopus 로고    scopus 로고
    • Ceramide β-D-glucuronide: Synthesis, digestion and suppression of early biomarkers of colon carcinogenesis
    • Schmelz, E. M., Bushnev, A. S., Dillehay, D. L., Sullards, M. C., Liotta, D. C. & Merrill, A. H., Jr. (1999) Ceramide β-D-glucuronide: synthesis, digestion and suppression of early biomarkers of colon carcinogenesis. Cancer Res. 59: 5768-5772.
    • (1999) Cancer Res. , vol.59 , pp. 5768-5772
    • Schmelz, E.M.1    Bushnev, A.S.2    Dillehay, D.L.3    Sullards, M.C.4    Liotta, D.C.5    Merrill Jr., A.H.6
  • 31
    • 0025019387 scopus 로고
    • Characteristics of the growth inhibition and cytotoxicity of long-chain (sphingoid) bases for Chinese hamster ovary cells: Evidence for an involvement of protein kinase C
    • Stevens, V. L., Nimkar, S., Jamison, W. C., Liotta, D. C. & Merrill, A. H., Jr. (1990) Characteristics of the growth inhibition and cytotoxicity of long-chain (sphingoid) bases for Chinese hamster ovary cells: evidence for an involvement of protein kinase C. Biochim. Biophys. Acta 1051: 37-45.
    • (1990) Biochim. Biophys. Acta , vol.1051 , pp. 37-45
    • Stevens, V.L.1    Nimkar, S.2    Jamison, W.C.3    Liotta, D.C.4    Merrill Jr., A.H.5
  • 32
    • 0036122349 scopus 로고    scopus 로고
    • Lithium blocks the PKB and GSK3 dephosphorolation induced by ceramide through protein phosphatase-2A
    • Mora, A., Sabjo, G., Risco, A. M., Cuenda, A., Alonso, J. C., Soler, G. & Centeno, F. (2002) Lithium blocks the PKB and GSK3 dephosphorolation induced by ceramide through protein phosphatase-2A. Cell. Signal. 14: 557-562.
    • (2002) Cell. Signal. , vol.14 , pp. 557-562
    • Mora, A.1    Sabjo, G.2    Risco, A.M.3    Cuenda, A.4    Alonso, J.C.5    Soler, G.6    Centeno, F.7
  • 33
    • 0027076191 scopus 로고
    • Retinoblastoma protein dephosphorylation induced by D-erythro-sphingosine
    • Chao, R., Khan, W. & Hannun, Y. A. (1992) Retinoblastoma protein dephosphorylation induced by D-erythro-sphingosine. J. Biol. Chem. 267: 23459-23462.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23459-23462
    • Chao, R.1    Khan, W.2    Hannun, Y.A.3
  • 35
    • 0035980052 scopus 로고    scopus 로고
    • Molecular mechanisms of ceramide-mediated telomerase inhibition in the A549 human lung adenocarcinoma cell line
    • Ogretmen, B., Kraveka, J. M., Schady, D., Usta, J., Hannun, Y. A. & Obeid, L. M. (2001) Molecular mechanisms of ceramide-mediated telomerase inhibition in the A549 human lung adenocarcinoma cell line. J. Biol. Chem. 276: 32506-32514.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32506-32514
    • Ogretmen, B.1    Kraveka, J.M.2    Schady, D.3    Usta, J.4    Hannun, Y.A.5    Obeid, L.M.6
  • 36
    • 0033525685 scopus 로고    scopus 로고
    • Ceramide induces cytochrome c release from isolated mitochondria. Importance of mitochondrial redox state
    • Ghafourifar, P., Klein, S. D., Schucht, O., Schenk, U., Pruschy, M., Rocha, S. & Richter, C. (1999) Ceramide induces cytochrome c release from isolated mitochondria. Importance of mitochondrial redox state. J. Biol. Chem. 274: 6080-6084.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6080-6084
    • Ghafourifar, P.1    Klein, S.D.2    Schucht, O.3    Schenk, U.4    Pruschy, M.5    Rocha, S.6    Richter, C.7
  • 37
    • 0032549509 scopus 로고    scopus 로고
    • Inhibition of sphingo-lipid-induced apoptosis by caspase inhibitors indicates that sphingosine acts in an earlier part of the apoptotic pathway than ceramide
    • Sweeney, E., Inokuchi, J. & Igarashi, Y. (1998) Inhibition of sphingo-lipid-induced apoptosis by caspase inhibitors indicates that sphingosine acts in an earlier part of the apoptotic pathway than ceramide. FEBS Lett. 425: 61-65.
    • (1998) FEBS Lett. , vol.425 , pp. 61-65
    • Sweeney, E.1    Inokuchi, J.2    Igarashi, Y.3
  • 38
    • 15144359445 scopus 로고    scopus 로고
    • Ceramide formation leads to caspase-3 activation during hypoxic PC12 cells death. Inhibitory effects of Bcl-2 on ceramide formation and caspase-3 activation
    • Yoshimura, S., Banno, Y., Nakashima, S., Takenaka, K., Sakai, H., Nishimura, Y., Sakai, N., Shimizu, S., Eguchi, Y. et al. (1998) Ceramide formation leads to caspase-3 activation during hypoxic PC12 cells death. Inhibitory effects of Bcl-2 on ceramide formation and caspase-3 activation. J. Biol. Chem. 273: 6921-6927.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6921-6927
    • Yoshimura, S.1    Banno, Y.2    Nakashima, S.3    Takenaka, K.4    Sakai, H.5    Nishimura, Y.6    Sakai, N.7    Shimizu, S.8    Eguchi, Y.9
  • 39
    • 0033575320 scopus 로고    scopus 로고
    • Ceramide induces Bcl-2 dephosphorylation via a mechanism involving mitochondrial PP2A
    • Ruvolo, P. P., Deng, X., Ito, T., Carr, B. K. & May, W. S. (1999) Ceramide induces Bcl-2 dephosphorylation via a mechanism involving mitochondrial PP2A. J. Biol. Chem. 174: 20296-20300.
    • (1999) J. Biol. Chem. , vol.174 , pp. 20296-20300
    • Ruvolo, P.P.1    Deng, X.2    Ito, T.3    Carr, B.K.4    May, W.S.5
  • 40
    • 0035817624 scopus 로고    scopus 로고
    • Expression of alpha-catenin in alpha-catenin-deficient cells increases resistance to sphingosine-induced apoptosis
    • Matsubara, S. & Ozawa, M. (2001) Expression of alpha-catenin in alpha-catenin-deficient cells increases resistance to sphingosine-induced apoptosis. J. Cell Biol. 154: 573-584.
    • (2001) J. Cell Biol. , vol.154 , pp. 573-584
    • Matsubara, S.1    Ozawa, M.2
  • 41
    • 0038541971 scopus 로고    scopus 로고
    • Sphingomyelin protects against apoptosis and hyperproliferation induced by deoxycholate: Potential implications for colon cancer
    • Moschetta, A., Portincasa, P., van Erpecum, K. J., Debellis, L., Vanberge-Henegouwen, G. P. & Palasciano, G. (2003) Sphingomyelin protects against apoptosis and hyperproliferation induced by deoxycholate: potential implications for colon cancer. Dig. Dis. Sci. 48: 1094-1101.
    • (2003) Dig. Dis. Sci. , vol.48 , pp. 1094-1101
    • Moschetta, A.1    Portincasa, P.2    Van Erpecum, K.J.3    Debellis, L.4    Vanberge-Henegouwen, G.P.5    Palasciano, G.6
  • 42
    • 0033577858 scopus 로고    scopus 로고
    • Overexpression of protein kinase C β II induces colonic hyperproliferation and increased sensitivity to colon carcinogenesis
    • Murray, N. R., Davidson, L. A., Chapkin, R. S., Gustafson, W. C., Schattenberg, D. G. & Fields, A. P. (1999) Overexpression of protein kinase C β II induces colonic hyperproliferation and increased sensitivity to colon carcinogenesis. J. Cell Biol. 145: 699-711.
    • (1999) J. Cell Biol. , vol.145 , pp. 699-711
    • Murray, N.R.1    Davidson, L.A.2    Chapkin, R.S.3    Gustafson, W.C.4    Schattenberg, D.G.5    Fields, A.P.6
  • 43
    • 0028491116 scopus 로고
    • Regulation and functions of the glycogen synthase kinase-3 subfamily
    • Woodgett, J. R. (1994) Regulation and functions of the glycogen synthase kinase-3 subfamily. Sem. Cancer Biol. 5: 269-275.
    • (1994) Sem. Cancer Biol. , vol.5 , pp. 269-275
    • Woodgett, J.R.1
  • 44
    • 0033558227 scopus 로고    scopus 로고
    • Activation of caspase-3-like proteases in apoptosis induced by sphingosine and other long-chain bases in Hep3B hepatoma cells
    • Hung, W. C., Chang, H. C. & Chuang, L. Y. (1999) Activation of caspase-3-like proteases in apoptosis induced by sphingosine and other long-chain bases in Hep3B hepatoma cells. Biochem. J. 338: 161-166.
    • (1999) Biochem. J. , vol.338 , pp. 161-166
    • Hung, W.C.1    Chang, H.C.2    Chuang, L.Y.3
  • 45
    • 0034717184 scopus 로고    scopus 로고
    • Involvement of sphingosine in mitochondria-dependent Fas-induced apoptosis of type II Jurkat T cells
    • Cuvillier, O., Edsall, L. & Spiegel, S. (2000) Involvement of sphingosine in mitochondria-dependent Fas-induced apoptosis of type II Jurkat T cells. J. Biol. Chem. 275: 15691-15700.
    • (2000) J. Biol. Chem. , vol.275 , pp. 15691-15700
    • Cuvillier, O.1    Edsall, L.2    Spiegel, S.3
  • 47
    • 0034717270 scopus 로고    scopus 로고
    • Apoptosis-induced cleavage of β-catenin by caspase-3 results in proteolytic fragments with reduced transactivation potential
    • Steinhusen, U., Badock, V., Bauer, A., Behrens, J., Wittman-Liebold, B., Durken, B. & Bommert, K. (2000) Apoptosis-induced cleavage of β-catenin by caspase-3 results in proteolytic fragments with reduced transactivation potential. J. Biol. Chem. 275: 16345-16353.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16345-16353
    • Steinhusen, U.1    Badock, V.2    Bauer, A.3    Behrens, J.4    Wittman-Liebold, B.5    Durken, B.6    Bommert, K.7
  • 48
    • 0032170317 scopus 로고    scopus 로고
    • TCF-4 binds beta-catenin and is expressed in distinct regions of the embryonic brain and limbs
    • Cho, E. A. & Dressler, G. R. (1998) TCF-4 binds beta-catenin and is expressed in distinct regions of the embryonic brain and limbs. Mech. Dev. 77: 9-18.
    • (1998) Mech. Dev. , vol.77 , pp. 9-18
    • Cho, E.A.1    Dressler, G.R.2
  • 50
    • 0035966119 scopus 로고    scopus 로고
    • Differential regulation of two alternatively spliced isoforms of hypoxia-inducible factor-1α in activated T lymphocytes
    • Lukahev, D., Caldwell, C., Ohta, A., Chen, P. & Sitkovsky, M. (2001) Differential regulation of two alternatively spliced isoforms of hypoxia-inducible factor-1α in activated T lymphocytes. J. Biol. Chem. 276: 48754-48763.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48754-48763
    • Lukahev, D.1    Caldwell, C.2    Ohta, A.3    Chen, P.4    Sitkovsky, M.5
  • 51
    • 10644283807 scopus 로고    scopus 로고
    • Hypoxia inducible factor-1: Oxygen regulation of trophoblast differentiation in normal and pre-exlamptic pregnancies - A review
    • Caniggia, I. & Winter, J. L. (2002) Hypoxia inducible factor-1: oxygen regulation of trophoblast differentiation in normal and pre-exlamptic pregnancies - a review. Placenta 23: S47-S57.
    • (2002) Placenta , vol.23
    • Caniggia, I.1    Winter, J.L.2


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