메뉴 건너뛰기




Volumn 63, Issue 19, 2003, Pages 6547-6555

Protein kinase Cε is linked to 12-O-tetradecanoylphorbol-13-acetate-induced tumor necrosis factor-α ectodomain shedding and the development of metastatic squamous cell carcinoma in protein kinase Cε transgenic mice

Author keywords

[No Author keywords available]

Indexed keywords

7,12 DIMETHYLBENZ[A]ANTHRACENE; ANTHRACENE DERIVATIVE; CYTOKERATIN; GLUTATHIONE PEROXIDASE; PENTOXIFYLLINE; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEIN KINASE C EPSILON; PROTEIN SERINE THREONINE KINASE; REACTIVE OXYGEN METABOLITE; SUPEROXIDE DISMUTASE; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME INHIBITOR; CARCINOGEN; PRKCE PROTEIN, MOUSE; PROTEIN KINASE C;

EID: 0141918880     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (71)

References (57)
  • 2
    • 0026729695 scopus 로고
    • Multistage carcino genesis in mouse skin
    • DiGiovanni, J. Multistage carcinogenesis in mouse skin. Pharmacol. Ther., 54: 63-128, 1992.
    • (1992) Pharmacol. Ther. , vol.54 , pp. 63-128
    • DiGiovanni, J.1
  • 3
    • 0020511019 scopus 로고
    • Solubilization, purification, and reconstitution of a phorbol ester receptor from the particulate protein fraction of mouse brain
    • Ashendel, C. L., Staller, J. M., and Boutwell, R. K. Solubilization, purification, and reconstitution of a phorbol ester receptor from the particulate protein fraction of mouse brain. Cancer Res., 43: 4327-4332, 1983.
    • (1983) Cancer Res. , vol.43 , pp. 4327-4332
    • Ashendel, C.L.1    Staller, J.M.2    Boutwell, R.K.3
  • 4
    • 0010708038 scopus 로고
    • Specific binding of phorbol ester tumor promoters
    • Driedger, P. E., and Blumberg, P. M. Specific binding of phorbol ester tumor promoters. Proc. Natl. Acad. Sci. USA, 77: 567-571, 1980.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 567-571
    • Driedger, P.E.1    Blumberg, P.M.2
  • 5
    • 0020634260 scopus 로고
    • Protein kinase C as a possible receptor protein of tumor-promoting phorbol esters
    • Kikkawa, U., Takai, Y., Tanaka, Y., Miyake, R., and Nishizuka, Y. Protein kinase C as a possible receptor protein of tumor-promoting phorbol esters. J. Biol. Chem., 258: 11442-11445, 1983.
    • (1983) J. Biol. Chem. , vol.258 , pp. 11442-11445
    • Kikkawa, U.1    Takai, Y.2    Tanaka, Y.3    Miyake, R.4    Nishizuka, Y.5
  • 7
    • 0032104245 scopus 로고    scopus 로고
    • The extended protein kinase C superfamily
    • Mellor, H., and Parker, P. J. The extended protein kinase C superfamily. Biochem. J., 332: 281-292, 1998.
    • (1998) Biochem. J. , vol.332 , pp. 281-292
    • Mellor, H.1    Parker, P.J.2
  • 8
    • 0028811653 scopus 로고
    • Protein kinase C: Structure, function, and regulation
    • Newton, A. C. Protein kinase C: structure, function, and regulation [Review] [78 refs]. J. Biol. Chem., 270: 28495-28498, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28495-28498
    • Newton, A.C.1
  • 9
    • 27644504484 scopus 로고    scopus 로고
    • Modulating protein kinase C signal transduction
    • Mochly-Rosen, D., and Kauvar, L. M. Modulating protein kinase C signal transduction. Adv. Pharmacol., 44: 91-145, 1998.
    • (1998) Adv. Pharmacol. , vol.44 , pp. 91-145
    • Mochly-Rosen, D.1    Kauvar, L.M.2
  • 11
    • 0026451081 scopus 로고
    • Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C
    • Nishizuka, Y. Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. Science, 258: 607-614, 1992.
    • (1992) Science , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 12
    • 0029060391 scopus 로고
    • Protein kinase C and lipid signaling for sustained cellular responses
    • Nishizuka, Y. Protein kinase C and lipid signaling for sustained cellular responses. FASEB J., 9: 484-496, 1995.
    • (1995) FASEB J. , vol.9 , pp. 484-496
    • Nishizuka, Y.1
  • 13
    • 0023052241 scopus 로고
    • Studies and perspectives of protein kinase C
    • Nishizuka, Y. Studies and perspectives of protein kinase C. Science, 233: 305-312, 1986.
    • (1986) Science , vol.233 , pp. 305-312
    • Nishizuka, Y.1
  • 14
    • 0028082161 scopus 로고
    • Protein kinase C-a question of specificity
    • Dekker, L. V., and Parker, P. J. Protein kinase C-a question of specificity. Trends Biochem. Sci., 19: 73-77, 1994.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 73-77
    • Dekker, L.V.1    Parker, P.J.2
  • 15
    • 0028811653 scopus 로고
    • Protein kinase C: Structure, function, and regulation
    • Newton, A. C. Protein kinase C: structure, function, and regulation. J. Biol. Chem., 270: 28495-28498, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28495-28498
    • Newton, A.C.1
  • 16
    • 0027529149 scopus 로고
    • Functional divergence of protein kinase C (PKC) family members. PKC gamma differs from PKC alpha and -beta II and uPKC epsilon in its competence to mediate-12-O-tetradecanoyl phorbol 13-acetate (TPA)-responsive transcriptional activation through a TPA-response element
    • Hata, A., Akita, Y., Suzuki, K., and Ohno, S. Functional divergence of protein kinase C (PKC) family members. PKC gamma differs from PKC alpha and -beta II and uPKC epsilon in its competence to mediate-12-O-tetradecanoyl phorbol 13-acetate (TPA)-responsive transcriptional activation through a TPA-response element. J. Biol. Chem., 268: 9122-9129, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9122-9129
    • Hata, A.1    Akita, Y.2    Suzuki, K.3    Ohno, S.4
  • 17
    • 0027182090 scopus 로고
    • The epsilon isoform of protein kinase C is an oncogene when overexpressed in rat fibroblasts
    • Cacace, A. M., Guadagno, S. N., Krauss, R. S., Fabbro, D., and Weinstein, I. B. The epsilon isoform of protein kinase C is an oncogene when overexpressed in rat fibroblasts. Oncogene, 8: 2095-2104, 1993.
    • (1993) Oncogene , vol.8 , pp. 2095-2104
    • Cacace, A.M.1    Guadagno, S.N.2    Krauss, R.S.3    Fabbro, D.4    Weinstein, I.B.5
  • 18
    • 0027418816 scopus 로고
    • Overexpression of protein kinase C-delta and -epsilon in NIH 3T3 cells induces opposite effects on growth, morphology, anchorage dependence, and tumorigenicity
    • Mischak, H., Goodnight, J. A., Kolch, W., Martiny-Baron, G., Schaechtle, C., Kazanietz, M. G., Blumberg, P. M., Pierce, J. H., and Mushinski, J. F. Overexpression of protein kinase C-delta and -epsilon in NIH 3T3 cells induces opposite effects on growth, morphology, anchorage dependence, and tumorigenicity. J. Biol. Chem., 268: 6090-6096, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6090-6096
    • Mischak, H.1    Goodnight, J.A.2    Kolch, W.3    Martiny-Baron, G.4    Schaechtle, C.5    Kazanietz, M.G.6    Blumberg, P.M.7    Pierce, J.H.8    Mushinski, J.F.9
  • 19
    • 0033951214 scopus 로고    scopus 로고
    • Transgenic mice overexpressing protein kinase C ε in their epidermis exhibit reduced papilloma burden but enhanced carcinoma formation after tumor promotion
    • Reddig, P. J., Dreckschmidt, N. E., Zou, J., Bourguignon, S. E., Oberley, T. D., and Verma, A. K. Transgenic mice overexpressing protein kinase C ε in their epidermis exhibit reduced papilloma burden but enhanced carcinoma formation after tumor promotion. Cancer Res., 60: 595-602, 2000.
    • (2000) Cancer Res. , vol.60 , pp. 595-602
    • Reddig, P.J.1    Dreckschmidt, N.E.2    Zou, J.3    Bourguignon, S.E.4    Oberley, T.D.5    Verma, A.K.6
  • 22
    • 0033568358 scopus 로고    scopus 로고
    • Essential role of tumor necrosis factor alpha (TNF-α) in tumor promotion as revealed by TNF-α-deficient mice
    • Suganuma, M., Okabe, S., Marino, M. W., Sakai, A., Sueoka, E., and Fujiki, H. Essential role of tumor necrosis factor alpha (TNF-α) in tumor promotion as revealed by TNF-α-deficient mice. Cancer Res., 59: 4516-4518, 1999.
    • (1999) Cancer Res. , vol.59 , pp. 4516-4518
    • Suganuma, M.1    Okabe, S.2    Marino, M.W.3    Sakai, A.4    Sueoka, E.5    Fujiki, H.6
  • 23
    • 0022416105 scopus 로고
    • Chinese hamster cells deficient in ornithine decarboxylase activity: Reversion by gene amplification and by azacytidine treatment
    • Steglich, C., Grens, A., and Scheffler, I. E. Chinese hamster cells deficient in ornithine decarboxylase activity: reversion by gene amplification and by azacytidine treatment. Somat. Cell Mol. Genet., 11: 11-23, 1985.
    • (1985) Somat. Cell Mol. Genet. , vol.11 , pp. 11-23
    • Steglich, C.1    Grens, A.2    Scheffler, I.E.3
  • 27
    • 0035260351 scopus 로고    scopus 로고
    • Reactive oxygen species mediate tumor necrosis factor alpha-converting, enzyme-dependent ectodomain shedding induced by phorbol myristate acetate
    • Zhang, Z., Oliver, P., Lancaster, J. J., Schwarzenberger, P. O., Joshi, M. S., Cork, J., and Kolls, J. K. Reactive oxygen species mediate tumor necrosis factor alpha-converting, enzyme-dependent ectodomain shedding induced by phorbol myristate acetate. FASEB J., 15: 303-305, 2001.
    • (2001) FASEB J. , vol.15 , pp. 303-305
    • Zhang, Z.1    Oliver, P.2    Lancaster, J.J.3    Schwarzenberger, P.O.4    Joshi, M.S.5    Cork, J.6    Kolls, J.K.7
  • 28
    • 0035444539 scopus 로고    scopus 로고
    • Signal transduction by tumor necrosis factor and its relatives
    • Baud, V., and Karin, M. Signal transduction by tumor necrosis factor and its relatives. Trends Cell Biol., 11: 372-377, 2001.
    • (2001) Trends Cell Biol. , vol.11 , pp. 372-377
    • Baud, V.1    Karin, M.2
  • 29
    • 0034125358 scopus 로고    scopus 로고
    • Role for tumour necrosis factor-alpha receptors in ultraviolet-induced skin tumours
    • Starcher, B. Role for tumour necrosis factor-alpha receptors in ultraviolet-induced skin tumours. Br. J. Dermatol., 142: 1140-1147, 2000.
    • (2000) Br. J. Dermatol. , vol.142 , pp. 1140-1147
    • Starcher, B.1
  • 31
    • 0034640428 scopus 로고    scopus 로고
    • Stimulation-induced down-regulation of tumor necrosis factor-alpha converting enzyme
    • Doedens, J. R., and Black, R. A. Stimulation-induced down-regulation of tumor necrosis factor-alpha converting enzyme. J. Biol. Chem., 275: 14598-14607, 2000.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14598-14607
    • Doedens, J.R.1    Black, R.A.2
  • 32
    • 0022255657 scopus 로고
    • Effects of a biomimetic superoxide dismutase on complete and multistage carcinogenesis in mouse skin
    • Egner, P. A., and Kensler, T. W. Effects of a biomimetic superoxide dismutase on complete and multistage carcinogenesis in mouse skin. Carcinogenesis (Lond.), 6: 1167-1172, 1985.
    • (1985) Carcinogenesis (Lond.) , vol.6 , pp. 1167-1172
    • Egner, P.A.1    Kensler, T.W.2
  • 33
    • 0037169525 scopus 로고    scopus 로고
    • Ebselen, a glutathione peroxidase mimetic seleno-organic compound, as a multifunctional antioxidant. Implication for inflammation-associated carcinogenesis
    • Nakamura, Y., Feng, Q., Kumagai, T., Torikai, K., Ohigashi, H., Osawa, T., Noguchi, N., Niki, E., and Uchida, K. Ebselen, a glutathione peroxidase mimetic seleno-organic compound, as a multifunctional antioxidant. Implication for inflammation-associated carcinogenesis. J. Biol. Chem., 277: 2687-2694, 2002.
    • (2002) J. Biol. Chem. , vol.277 , pp. 2687-2694
    • Nakamura, Y.1    Feng, Q.2    Kumagai, T.3    Torikai, K.4    Ohigashi, H.5    Osawa, T.6    Noguchi, N.7    Niki, E.8    Uchida, K.9
  • 34
    • 0028883765 scopus 로고
    • Altered expression of cyclins and c-fos in R6 cells that overproduce PKC epsilon
    • Han, E. K., Cacace, A. M., Sgambato, A., and Weinstein, I. B. Altered expression of cyclins and c-fos in R6 cells that overproduce PKC epsilon. Carcinogenesis (Lond.), 16: 2423-2428, 1995.
    • (1995) Carcinogenesis (Lond.) , vol.16 , pp. 2423-2428
    • Han, E.K.1    Cacace, A.M.2    Sgambato, A.3    Weinstein, I.B.4
  • 35
    • 0345129995 scopus 로고    scopus 로고
    • Novel roles of specific isoforms of protein kinase C in activation of the c-fos serum response element
    • Soh, J. W., Lee, E. H., Prywes, R., and Weinstein, I. B. Novel roles of specific isoforms of protein kinase C in activation of the c-fos serum response element. Mol. Cell. Biol., 19: 1313-1324, 1999.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1313-1324
    • Soh, J.W.1    Lee, E.H.2    Prywes, R.3    Weinstein, I.B.4
  • 36
    • 0031596745 scopus 로고    scopus 로고
    • Overexpression of PKCepsilon in R6 fibroblasts causes increased production of active TGFbeta
    • Cacace, A. M., Ueffing, M., Han, E. K., Marme, D., and Weinstein, I. B. Overexpression of PKCepsilon in R6 fibroblasts causes increased production of active TGFbeta. J. Cell. Physiol., 175: 314-322, 1998.
    • (1998) J. Cell. Physiol. , vol.175 , pp. 314-322
    • Cacace, A.M.1    Ueffing, M.2    Han, E.K.3    Marme, D.4    Weinstein, I.B.5
  • 37
    • 0033537834 scopus 로고    scopus 로고
    • Protein kinase C regulates integrin-induced activation of the extracellular regulated kinase pathway upstream of She
    • Miranti, C. K., Ohno, S., and Brugge, J. S. Protein kinase C regulates integrin-induced activation of the extracellular regulated kinase pathway upstream of She. J. Biol. Chem., 274: 10571-10581, 1999.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10571-10581
    • Miranti, C.K.1    Ohno, S.2    Brugge, J.S.3
  • 38
    • 0031038588 scopus 로고    scopus 로고
    • Role of diacylglycerol-regulated protein kinase C isotypes in growth factor activation of the Raf-1 protein kinase
    • Cai, H., Smola, U., Wixler, V., Eisenmann-Tappe, I., Diaz-Meco, M. T., Moscat, J., Rapp, U., and Cooper, G. M. Role of diacylglycerol-regulated protein kinase C isotypes in growth factor activation of the Raf-1 protein kinase. Mol. Cell. Biol., 17: 732-741, 1997.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 732-741
    • Cai, H.1    Smola, U.2    Wixler, V.3    Eisenmann-Tappe, I.4    Diaz-Meco, M.T.5    Moscat, J.6    Rapp, U.7    Cooper, G.M.8
  • 39
    • 0031455541 scopus 로고    scopus 로고
    • Protein kinase C-epsilon associates with the Raf-1 kinase and induces the production of growth factors that stimulate Raf-1 activity
    • Ueffing, M., Lovric, J., Philipp, A., Mischak, H., and Kolch, W. Protein kinase C-epsilon associates with the Raf-1 kinase and induces the production of growth factors that stimulate Raf-1 activity. Oncogene, 15: 2921-2927, 1997.
    • (1997) Oncogene , vol.15 , pp. 2921-2927
    • Ueffing, M.1    Lovric, J.2    Philipp, A.3    Mischak, H.4    Kolch, W.5
  • 40
    • 0032446187 scopus 로고    scopus 로고
    • Regulation of smooth muscle actin-myosin interaction and force by calponin
    • Winder, S. J., Allen, B. G., Clement-Chomienne, O., and Walsh, M. P. Regulation of smooth muscle actin-myosin interaction and force by calponin. Acta Physiol. Scand., 164: 415-426, 1998.
    • (1998) Acta Physiol. Scand. , vol.164 , pp. 415-426
    • Winder, S.J.1    Allen, B.G.2    Clement-Chomienne, O.3    Walsh, M.P.4
  • 41
    • 0030445276 scopus 로고    scopus 로고
    • PKC epsilon functions as an oncogene by enhancing activation of the Raf kinase
    • Cacace, A. M., Ueffing, M., Philipp, A., Han, E. K., Kolch, W., and Weinstein, I. B. PKC epsilon functions as an oncogene by enhancing activation of the Raf kinase. Oncogene, 13: 2517-2526, 1996.
    • (1996) Oncogene , vol.13 , pp. 2517-2526
    • Cacace, A.M.1    Ueffing, M.2    Philipp, A.3    Han, E.K.4    Kolch, W.5    Weinstein, I.B.6
  • 42
    • 0035800770 scopus 로고    scopus 로고
    • Constitutive association of c-N-Ras with c-Raf-1 and protein kinase C epsilon in latent signaling modules
    • Hamilton, M., Liao, J., Catheart, M. K., and Wolfman, A. Constitutive association of c-N-Ras with c-Raf-1 and protein kinase C epsilon in latent signaling modules. J. Biol. Chem., 276: 29079-29090, 2001.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29079-29090
    • Hamilton, M.1    Liao, J.2    Catheart, M.K.3    Wolfman, A.4
  • 43
    • 0032565768 scopus 로고    scopus 로고
    • Protein kinase C epsilon is oncogenic in colon epithelial cells by interaction with the ras signal transduction pathway
    • Perletti, G. P., Concari, P., Brusaferri, S., Marras, E., Piccinini, F., and Tashjian, A. H., Jr. Protein kinase C epsilon is oncogenic in colon epithelial cells by interaction with the ras signal transduction pathway. Oncogene, 16: 3345-3348, 1998.
    • (1998) Oncogene , vol.16 , pp. 3345-3348
    • Perletti, G.P.1    Concari, P.2    Brusaferri, S.3    Marras, E.4    Piccinini, F.5    Tashjian A.H., Jr.6
  • 45
    • 0022178181 scopus 로고
    • Cachectin/tumor necrosis factor: Production, distribution, and metabolic fate in vivo
    • Beutler, B. A., Milsark, I. W., and Cerami, A. Cachectin/tumor necrosis factor: production, distribution, and metabolic fate in vivo. J. Immunol., 135: 3972-3977, 1985.
    • (1985) J. Immunol. , vol.135 , pp. 3972-3977
    • Beutler, B.A.1    Milsark, I.W.2    Cerami, A.3
  • 46
    • 0025959668 scopus 로고
    • Mutational analysis of the transin (rat stromelysin) autoinhibitor region demonstrates a role for residues surrounding the "cysteine switch"
    • Park, A. J., Matrisian, L. M., Kells, A. F., Pearson, R., Yuan, Z. Y., and Navre, M. Mutational analysis of the transin (rat stromelysin) autoinhibitor region demonstrates a role for residues surrounding the "cysteine switch." J. Biol. Chem., 266: 1584-1590, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1584-1590
    • Park, A.J.1    Matrisian, L.M.2    Kells, A.F.3    Pearson, R.4    Yuan, Z.Y.5    Navre, M.6
  • 47
    • 0025096722 scopus 로고
    • Multiple modes of activation of latent human fibroblast collagenase: Evidence for the role of a Cys73 active-site zinc complex in latency and a "cysteine switch" mechanism for activation
    • Springman, E. B., Angleton, E. L., Birkedal-Hansen, H., and Van Wart, H. E. Multiple modes of activation of latent human fibroblast collagenase: evidence for the role of a Cys73 active-site zinc complex in latency and a "cysteine switch" mechanism for activation. Proc. Natl. Acad. Sci. USA, 87: 364-368, 1990.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 364-368
    • Springman, E.B.1    Angleton, E.L.2    Birkedal-Hansen, H.3    Van Wart, H.E.4
  • 48
    • 10544246489 scopus 로고    scopus 로고
    • Reactive oxygen species produced by macrophage-derived foam cells regulate the activity of vascular matrix metalloproteinases in vitro. Implications for atherosclerotic plaque stability
    • Rajagopalan, S., Meng, X. P., Ramasamy, S., Harrison, D. G., and Galis, Z. S. Reactive oxygen species produced by macrophage-derived foam cells regulate the activity of vascular matrix metalloproteinases in vitro. Implications for atherosclerotic plaque stability. J. Clin. Investig., 98: 2572-2579, 1996.
    • (1996) J. Clin. Investig. , vol.98 , pp. 2572-2579
    • Rajagopalan, S.1    Meng, X.P.2    Ramasamy, S.3    Harrison, D.G.4    Galis, Z.S.5
  • 49
    • 0028872942 scopus 로고
    • Nitric oxide activates metalloprotease enzymes in articular cartilage
    • Murrell, G. A., Jang, D., and Williams, R. J. Nitric oxide activates metalloprotease enzymes in articular cartilage. Biochem. Biophys. Res. Commun., 206; 15-21, 1995.
    • (1995) Biochem. Biophys. Res. Commun. , vol.206 , pp. 15-21
    • Murrell, G.A.1    Jang, D.2    Williams, R.J.3
  • 50
    • 0031570730 scopus 로고    scopus 로고
    • Activation of human neutrophil procollagenase by nitrogen dioxide and peroxynitrite: A novel mechanism for procollagenase activation involving nitric oxide
    • Okamoto, T., Akaike, T., Nagano, T., Miyajima, S., Suga, M., Ando, M., Ichimori, K., and Maeda, H. Activation of human neutrophil procollagenase by nitrogen dioxide and peroxynitrite: a novel mechanism for procollagenase activation involving nitric oxide. Arch. Biochem. Biophys., 342: 261-274, 1997.
    • (1997) Arch. Biochem. Biophys. , vol.342 , pp. 261-274
    • Okamoto, T.1    Akaike, T.2    Nagano, T.3    Miyajima, S.4    Suga, M.5    Ando, M.6    Ichimori, K.7    Maeda, H.8
  • 51
    • 0030044490 scopus 로고    scopus 로고
    • Nitric oxide stimulates the activity of a 72-kDa neutral matrix metalloproteinase in cultured rat mesangial cells
    • Trachtman, H., Futterweit, S., Garg, P., Reddy, K., and Singhal, P. C. Nitric oxide stimulates the activity of a 72-kDa neutral matrix metalloproteinase in cultured rat mesangial cells. Biochem. Biophys. Res. Commun., 218: 704-708, 1996.
    • (1996) Biochem. Biophys. Res. Commun. , vol.218 , pp. 704-708
    • Trachtman, H.1    Futterweit, S.2    Garg, P.3    Reddy, K.4    Singhal, P.C.5
  • 52
    • 0027231850 scopus 로고
    • Inhibition of endogenous TNF formation by pentoxifylline
    • Zabel, P., Schade, F. U., and Schlaak, M. Inhibition of endogenous TNF formation by pentoxifylline. Immunobiology, 187: 447-463, 1993.
    • (1993) Immunobiology , vol.187 , pp. 447-463
    • Zabel, P.1    Schade, F.U.2    Schlaak, M.3
  • 53
    • 0029784572 scopus 로고    scopus 로고
    • Inhibition of pro-inflammatory cytokine gene expression and papilloma growth during murine multistage carcinogenesis by pentoxifylline
    • Robertson, F. M., Ross, M. S., Tober, K. L., Long, B. W., and Oberyszyn, T. M. Inhibition of pro-inflammatory cytokine gene expression and papilloma growth during murine multistage carcinogenesis by pentoxifylline. Carcinogenesis (Lond.), 17: 1719-1728, 1996.
    • (1996) Carcinogenesis (Lond.) , vol.17 , pp. 1719-1728
    • Robertson, F.M.1    Ross, M.S.2    Tober, K.L.3    Long, B.W.4    Oberyszyn, T.M.5
  • 54
    • 0020057239 scopus 로고
    • Comparison of the effects of 3-isobutyl-1-methylxanthine and adenosine cyclic 3′:5′-monophosphate on the induction of skin tumors by the initiation-promotion protocol and by the complete carcinogenesis process
    • Perchellet, J. P., and Boutwell, R. K. Comparison of the effects of 3-isobutyl-1-methylxanthine and adenosine cyclic 3′:5′ -monophosphate on the induction of skin tumors by the initiation-promotion protocol and by the complete carcinogenesis process. Carcinogenesis (Lond.), 3: 53-60, 1982.
    • (1982) Carcinogenesis (Lond.) , vol.3 , pp. 53-60
    • Perchellet, J.P.1    Boutwell, R.K.2
  • 55
  • 56
    • 0027203921 scopus 로고
    • Reduction of p53 gene dosage does not increase initiation or promotion but enhances malignant progression of chemically induced skin tumors
    • Kemp, C. J., Donehower, L. A., Bradley, A., and Balmain, A. Reduction of p53 gene dosage does not increase initiation or promotion but enhances malignant progression of chemically induced skin tumors. Cell, 74: 813-822, 1993.
    • (1993) Cell , vol.74 , pp. 813-822
    • Kemp, C.J.1    Donehower, L.A.2    Bradley, A.3    Balmain, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.