메뉴 건너뛰기




Volumn 81, Issue 1, 2004, Pages 233-242

The tumor promoter 12-O-tetradecanoylphorbol 13-acetate (TPA) provokes a prolonged morphologic response and ERK activation in Tsc2-null renal tumor cells

Author keywords

Protein kinase C; TPA; Tsc2

Indexed keywords

BISINDOLYLMALEIMIDE; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEIN KINASE C; RAP PROTEIN; TUBERIN; TUMOR PROMOTER; TUMOR SUPPRESSOR PROTEIN;

EID: 4444292225     PISSN: 10966080     EISSN: None     Source Type: Journal    
DOI: 10.1093/toxsci/kfh183     Document Type: Article
Times cited : (19)

References (34)
  • 1
    • 0037028305 scopus 로고    scopus 로고
    • Tuberin the tuberous sclerosis complex 2 tumor suppressor gene product, regulates Rho activation, cell adhesion and migration
    • Astrinidis, A., Cash, T. P., Hunter, D. S., Walker, C. L., Chernoff, J., and Henske, E. P. (2002). Tuberin, the tuberous sclerosis complex 2 tumor suppressor gene product, regulates Rho activation, cell adhesion and migration. Oncogene 21, 8470-8476.
    • (2002) Oncogene , vol.21 , pp. 8470-8476
    • Astrinidis, A.1    Cash, T.P.2    Hunter, D.S.3    Walker, C.L.4    Chernoff, J.5    Henske, E.P.6
  • 3
    • 0028239183 scopus 로고
    • Differential Raf requirement for activation of mitogen-activated protein kinase by growth factors, phorbol esters, and calcium
    • Chao, T. S., Foster, D. A., Rapp, U. R., and Rosner, M. R. (1994). Differential Raf requirement for activation of mitogen-activated protein kinase by growth factors, phorbol esters, and calcium. J. Biol. Chem. 269, 7337-7341.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7337-7341
    • Chao, T.S.1    Foster, D.A.2    Rapp, U.R.3    Rosner, M.R.4
  • 4
    • 0034105859 scopus 로고    scopus 로고
    • Protein kinase C in human renal cell carcinomas: Role in invasion and differential isoenzyme expression
    • Engers, R., Mrzyk, S., Springer, E., Fabbro, D., Weissgerber, G., Gernharz, C. D., and Gabbert, H. E. (2000). Protein kinase C in human renal cell carcinomas: Role in invasion and differential isoenzyme expression. Br. J. Cancer 82, 1063-1069.
    • (2000) Br. J. Cancer , vol.82 , pp. 1063-1069
    • Engers, R.1    Mrzyk, S.2    Springer, E.3    Fabbro, D.4    Weissgerber, G.5    Gernharz, C.D.6    Gabbert, H.E.7
  • 5
    • 0026470327 scopus 로고
    • Hereditary renal cell carcinoma in the Eker rat: A rodent familial cancer syndrome
    • Everitt, J. I., Goldsworthy, T. L., Wolf, D. C., and Walker, C. L. (1992). Hereditary renal cell carcinoma in the Eker rat: A rodent familial cancer syndrome. J. Urol. 148, 1932-1936.
    • (1992) J. Urol. , vol.148 , pp. 1932-1936
    • Everitt, J.I.1    Goldsworthy, T.L.2    Wolf, D.C.3    Walker, C.L.4
  • 6
    • 0031014969 scopus 로고    scopus 로고
    • Rapid Ca2+-mediated activation of Rap1 in human platelets
    • Franke, B., Akkerman, J. W., and Bos, J. L. (1997). Rapid Ca2+-mediated activation of Rap1 in human platelets. Embo J. 16, 252-259.
    • (1997) Embo J. , vol.16 , pp. 252-259
    • Franke, B.1    Akkerman, J.W.2    Bos, J.L.3
  • 7
    • 0000336544 scopus 로고
    • Hereditary renal tumors in the rat: Cell lines from adenocarcinomas induced by the Eker mutation
    • Freed, J. J., Howard, S., Lerro, A., Dodson, L., Scsok, D., and Knudson, A. G. (1990). Hereditary renal tumors in the rat: Cell lines from adenocarcinomas induced by the Eker mutation. Proc. Am. Assoc. Cancer Res. 31, 317.
    • (1990) Proc. Am. Assoc. Cancer Res. , vol.31 , pp. 317
    • Freed, J.J.1    Howard, S.2    Lerro, A.3    Dodson, L.4    Scsok, D.5    Knudson, A.G.6
  • 8
    • 0034982971 scopus 로고    scopus 로고
    • TSC1 and TSC2 tumor suppressors antagonize insulin signaling in cell growth
    • Gao, X., and Pan, D. (2001). TSC1 and TSC2 tumor suppressors antagonize insulin signaling in cell growth. Genes Dev. 15, 1383-1392.
    • (2001) Genes Dev. , vol.15 , pp. 1383-1392
    • Gao, X.1    Pan, D.2
  • 10
    • 4444279273 scopus 로고    scopus 로고
    • Receptor toxicology
    • (H. Marquardt, S. Schafer, R. McClellan, and R. Welsch, Eds.), Academic Press, San Diego, CA
    • Gottlicher, M. (1999). Receptor toxicology. In Toxicology (H. Marquardt, S. Schafer, R. McClellan, and R. Welsch, Eds.), pp. 231-243. Academic Press, San Diego, CA.
    • (1999) Toxicology , pp. 231-243
    • Gottlicher, M.1
  • 11
    • 2342504819 scopus 로고    scopus 로고
    • GTPases
    • (B. Hames and D. Glover, Eds.), Oxford University Press, New York
    • Hall, A. (2000). GTPases. In Frontiers in Molecular Biology (B. Hames and D. Glover, Eds.), pp. 67-175. Oxford University Press, New York.
    • (2000) Frontiers in Molecular Biology , pp. 67-175
    • Hall, A.1
  • 12
    • 0029913467 scopus 로고    scopus 로고
    • Differential interaction of the ras family GTP-binding proteins H-Ras, Rap1A, and R-Ras with the putative effector molecules Raf kinase and Ral-guanine nucleotide exchange factor
    • Herrmann, C., Horn, G., Spaargaren, M., and Wittinghofer, A. (1996). Differential interaction of the ras family GTP-binding proteins H-Ras, Rap1A, and R-Ras with the putative effector molecules Raf kinase and Ral-guanine nucleotide exchange factor. J. Biol. Chem. 271, 6794-6800.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6794-6800
    • Herrmann, C.1    Horn, G.2    Spaargaren, M.3    Wittinghofer, A.4
  • 13
    • 0028181082 scopus 로고
    • Identification and characterization of alpha-protein kinase C binding proteins in normal and transformed REF52 cells
    • Hyatt, S. L., Liao, L., Chapline, C., and Jaken, S. (1994). Identification and characterization of alpha-protein kinase C binding proteins in normal and transformed REF52 cells. Biochemistry 33, 1223-1228.
    • (1994) Biochemistry , vol.33 , pp. 1223-1228
    • Hyatt, S.L.1    Liao, L.2    Chapline, C.3    Jaken, S.4
  • 15
    • 0036713778 scopus 로고    scopus 로고
    • TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling
    • Inoki, K., Li, Y., Zhu, T., Wu, J., and Guan, K. L. (2002). TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling. Nat. Cell Biol. 4, 648-657.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 648-657
    • Inoki, K.1    Li, Y.2    Zhu, T.3    Wu, J.4    Guan, K.L.5
  • 16
    • 0024327617 scopus 로고
    • Association of type 3 protein kinase C with focal contacts in rat embryo fibroblasts
    • Jaken, S., Leach, K., and Klauck, T. (1989). Association of type 3 protein kinase C with focal contacts in rat embryo fibroblasts. J Cell. Biol. 109, 697-704.
    • (1989) J. Cell. Biol. , vol.109 , pp. 697-704
    • Jaken, S.1    Leach, K.2    Klauck, T.3
  • 17
    • 0037108682 scopus 로고    scopus 로고
    • Activated mammalian target of rapamycin pathway in the pathogenesis of tuberous sclerosis complex renal tumors
    • Kenerson, H. L., Aicher, L. D., True, L. D., and Yeung, R. S. (2002). Activated mammalian target of rapamycin pathway in the pathogenesis of tuberous sclerosis complex renal tumors. Cancer Res. 62, 5645-5650.
    • (2002) Cancer Res. , vol.62 , pp. 5645-5650
    • Kenerson, H.L.1    Aicher, L.D.2    True, L.D.3    Yeung, R.S.4
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0033775869 scopus 로고    scopus 로고
    • The TSC1 tumour suppressor hamartin regulates cell adhesion through ERM proteins and the GTPase Rho
    • Lamb, R. F., Roy, C., Diefenbach, T. J., Vinters, H. V., Johnson, M. W., Jay, D. G., and Hall, A. (2000). The TSC1 tumour suppressor hamartin regulates cell adhesion through ERM proteins and the GTPase Rho. Nat. Cell Biol. 2, 281-287.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 281-287
    • Lamb, R.F.1    Roy, C.2    Diefenbach, T.J.3    Vinters, H.V.4    Johnson, M.W.5    Jay, D.G.6    Hall, A.7
  • 21
    • 0029812896 scopus 로고    scopus 로고
    • Ubiquitination of protein kinase C-alpha and degradation by the proteasome
    • Lee, H. W., Smith, L., Pettit, G. R., Vinitsky, A., and Smith, J. B. (1996). Ubiquitination of protein kinase C-alpha and degradation by the proteasome. J. Biol. Chem. 271, 20973-20976.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20973-20976
    • Lee, H.W.1    Smith, L.2    Pettit, G.R.3    Vinitsky, A.4    Smith, J.B.5
  • 22
    • 0037112803 scopus 로고    scopus 로고
    • Identification of the coding sequences responsible for Tsc2-mediated tumor suppression using a transgenic rat system
    • Momose, S., Kobayashi, T., Mitani, H., Hirabayashi, M., Ito, K., Ueda, M., Nabeshima, Y., and Hino, O. (2002). Identification of the coding sequences responsible for Tsc2-mediated tumor suppression using a transgenic rat system. Hum. Mol. Genet. 11, 2997-3006.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2997-3006
    • Momose, S.1    Kobayashi, T.2    Mitani, H.3    Hirabayashi, M.4    Ito, K.5    Ueda, M.6    Nabeshima, Y.7    Hino, O.8
  • 24
    • 0036855463 scopus 로고    scopus 로고
    • Protein kinase calpha (PKCalpha): Regulation and biological function
    • Nakashima, S. (2002). Protein kinase calpha (PKCalpha): Regulation and biological function. J. Biochem. (Tokyo) 132, 669-675.
    • (2002) J. Biochem. (Tokyo) , vol.132 , pp. 669-675
    • Nakashima, S.1
  • 26
    • 0026528680 scopus 로고
    • A tumour promoter induces alterations in vinculin and actin distribution in human renal epithelium
    • Rahilly, M. A., and Fleming, S. (1992). A tumour promoter induces alterations in vinculin and actin distribution in human renal epithelium. J. Pathol. 166, 283-288.
    • (1992) J. Pathol. , vol.166 , pp. 283-288
    • Rahilly, M.A.1    Fleming, S.2
  • 27
    • 0037108750 scopus 로고    scopus 로고
    • Tuberous sclerosis complex-1 and -2 gene products function together to inhibit mammalian target of rapamycin (mTOR)mediated downstream signaling
    • Tee, A. R., Fingar, D. C., Manning, B. D., Kwiatkowski, D. J., Cantley, L. C., and Blenis, J. (2002). Tuberous sclerosis complex-1 and -2 gene products function together to inhibit mammalian target of rapamycin (mTOR)mediated downstream signaling. Proc. Natl. Acad. Sci. U.S.A. 99, 13571-13576.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 13571-13576
    • Tee, A.R.1    Fingar, D.C.2    Manning, B.D.3    Kwiatkowski, D.J.4    Cantley, L.C.5    Blenis, J.6
  • 29
    • 0029021621 scopus 로고
    • Identification of tuberin, the tuberous sclerosis-2 product. Tuberin possesses specific Rap1GAP activity
    • Wienecke, R., Konig, A., and DeClue, J. E. (1995). Identification of tuberin, the tuberous sclerosis-2 product. Tuberin possesses specific Rap1GAP activity. J. Biol. Chem. 270, 16409-16414.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16409-16414
    • Wienecke, R.1    Konig, A.2    DeClue, J.E.3
  • 30
    • 0027248964 scopus 로고
    • Isoenzyme specificity of bisindolylmaleimides, selective inhibitors of protein kinase C
    • Wilkinson, S. E., Parker, P. J., and Nixon, J. S. (1993). Isoenzyme specificity of bisindolylmaleimides, selective inhibitors of protein kinase C. Biochem. J. 294, 335-337.
    • (1993) Biochem. J. , vol.294 , pp. 335-337
    • Wilkinson, S.E.1    Parker, P.J.2    Nixon, J.S.3
  • 31
    • 0030972969 scopus 로고    scopus 로고
    • The tuberous sclerosis 2 gene product, tuberin, functions as a Rab5 GTPase activating protein (GAP) in modulating endocytosis
    • Xiao, G. H., Shoarinejad, F., Jin, F., Golemis, E. A., and Yeung, R. S. (1997). The tuberous sclerosis 2 gene product, tuberin, functions as a Rab5 GTPase activating protein (GAP) in modulating endocytosis. J. Biol. Chem. 272, 6097-6100.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6097-6100
    • Xiao, G.H.1    Shoarinejad, F.2    Jin, F.3    Golemis, E.A.4    Yeung, R.S.5
  • 32
    • 0032499282 scopus 로고    scopus 로고
    • Rap1 mediates sustained MAP kinase activation induced by nerve growth factor
    • York, R. D., Yao, H., Dillon, T., Ellig, C. L., Eckert, S. P., McCleskey, E. W., and Stork, P. J. (1998). Rap1 mediates sustained MAP kinase activation induced by nerve growth factor. Nature 392, 622-626.
    • (1998) Nature , vol.392 , pp. 622-626
    • York, R.D.1    Yao, H.2    Dillon, T.3    Ellig, C.L.4    Eckert, S.P.5    McCleskey, E.W.6    Stork, P.J.7
  • 33
    • 0038141979 scopus 로고    scopus 로고
    • Rheb is a direct target of the tuberous sclerosis tumour suppressor proteins
    • Zhang, Y., Gao, X., Saucedo, L. J., Ru, B., Edgar, B. A., and Pan, D. (2003). Rheb is a direct target of the tuberous sclerosis tumour suppressor proteins. Nat. Cell Biol. 5, 578-581.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 578-581
    • Zhang, Y.1    Gao, X.2    Saucedo, L.J.3    Ru, B.4    Edgar, B.A.5    Pan, D.6
  • 34
    • 0032531756 scopus 로고    scopus 로고
    • Extracellular signal-regulated activation of Rap1 fails to interfere in Ras effector signalling
    • Zwartkruis, F. J., Wolthuis, R. M., Nabben, N. M., Franke, B., and Bos, J. L. (1998). Extracellular signal-regulated activation of Rap1 fails to interfere in Ras effector signalling. Embo J. 17, 5905-5912.
    • (1998) Embo J. , vol.17 , pp. 5905-5912
    • Zwartkruis, F.J.1    Wolthuis, R.M.2    Nabben, N.M.3    Franke, B.4    Bos, J.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.