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Volumn 66, Issue 14, 2006, Pages 7261-7269

Differential effect of bryostatin 1 and phorbol 12-myristate 13-acetate on HOP-92 cell proliferation is mediated by down-regulation of protein kinase Cδ

Author keywords

[No Author keywords available]

Indexed keywords

BRYOSTATIN 1; ISOENZYME; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEIN KINASE C DELTA; SMALL INTERFERING RNA;

EID: 33746912263     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-05-4177     Document Type: Article
Times cited : (32)

References (56)
  • 1
    • 0028082161 scopus 로고
    • Protein kinase C-a question of specificity
    • Dekker LV, Parker PJ. Protein kinase C-a question of specificity. Trends Biochem Sci 1994;19:73-7.
    • (1994) Trends Biochem Sci , vol.19 , pp. 73-77
    • Dekker, L.V.1    Parker, P.J.2
  • 2
    • 0032209522 scopus 로고    scopus 로고
    • Signaling through protein kinase C
    • Toker A. Signaling through protein kinase C. Front Biosci 1998;3:D1134-47.
    • (1998) Front Biosci , vol.3
    • Toker, A.1
  • 5
    • 0027418816 scopus 로고
    • Overexpression of protein kinase C-δ and -ε in NIH 3T3 cells induces opposite effects on growth, morphology, anchorage dependence, and tumorigenicity
    • Mischak H, Goodnight JA, Kolch W, et al. Overexpression of protein kinase C-δ and -ε in NIH 3T3 cells induces opposite effects on growth, morphology, anchorage dependence, and tumorigenicity. J Biol Chem 1993;268:6090-6.
    • (1993) J Biol Chem , vol.268 , pp. 6090-6096
    • Mischak, H.1    Goodnight, J.A.2    Kolch, W.3
  • 6
    • 0036132855 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of protein kinase Cδ is essential for its apoptotic effect in response to etoposide
    • Blass M, Kronfeld I, Kazimirsky G, Blumberg PM, Brodie C. Tyrosine phosphorylation of protein kinase Cδ is essential for its apoptotic effect in response to etoposide. Mol Cell Biol 2002;22:182-95.
    • (2002) Mol Cell Biol , vol.22 , pp. 182-195
    • Blass, M.1    Kronfeld, I.2    Kazimirsky, G.3    Blumberg, P.M.4    Brodie, C.5
  • 7
    • 0037189498 scopus 로고    scopus 로고
    • Infection of glioma cells with Sindbis virus induces selective activation and tyrosine phosphorylation of protein kinase Cδ. Implications for Sindbis virus-induced apoptosis
    • Zrachia A, Dobroslav M, Blass M, et al. Infection of glioma cells with Sindbis virus induces selective activation and tyrosine phosphorylation of protein kinase Cδ. Implications for Sindbis virus-induced apoptosis. J Biol Chem 2002;277:23693-701.
    • (2002) J Biol Chem , vol.277 , pp. 23693-23701
    • Zrachia, A.1    Dobroslav, M.2    Blass, M.3
  • 8
    • 21244479797 scopus 로고    scopus 로고
    • Roles of tyrosine phosphorylation and cleavage of protein kinase Cδ in its protective effect against tumor necrosis factor-related apoptosis inducing ligand-induced apoptosis
    • Okhrimenko H, Lu W, Xiang C, et al. Roles of tyrosine phosphorylation and cleavage of protein kinase Cδ in its protective effect against tumor necrosis factor-related apoptosis inducing ligand-induced apoptosis. J Biol Chem 2005;280:23643-52.
    • (2005) J Biol Chem , vol.280 , pp. 23643-23652
    • Okhrimenko, H.1    Lu, W.2    Xiang, C.3
  • 9
    • 0025939859 scopus 로고
    • Complexities of the protein kinase C pathway
    • Blumberg PM. Complexities of the protein kinase C pathway. Mol Carcinog 1991;4:339-44.
    • (1991) Mol Carcinog , vol.4 , pp. 339-344
    • Blumberg, P.M.1
  • 10
    • 0031964645 scopus 로고    scopus 로고
    • Anchoring proteins for protein kinase C: A means for isozyme selectivity
    • Mochly-Rosen D, Gordon AS. Anchoring proteins for protein kinase C: a means for isozyme selectivity. FASEB J 1998;12:35-42.
    • (1998) FASEB J , vol.12 , pp. 35-42
    • Mochly-Rosen, D.1    Gordon, A.S.2
  • 11
    • 0033601367 scopus 로고    scopus 로고
    • Differential localization of protein kinase Cδ by phorbol esters and related compounds using a fusion protein with green fluorescent protein
    • Wang QJ, Bhattacharyya D, Garfield S, Nacro K, Marquez VE, Blumberg PM. Differential localization of protein kinase Cδ by phorbol esters and related compounds using a fusion protein with green fluorescent protein. J Biol Chem 1999;274:37233-9.
    • (1999) J Biol Chem , vol.274 , pp. 37233-37239
    • Wang, Q.J.1    Bhattacharyya, D.2    Garfield, S.3    Nacro, K.4    Marquez, V.E.5    Blumberg, P.M.6
  • 12
    • 0031466995 scopus 로고    scopus 로고
    • Direct visualization of the translocation of the γ-subspecies of protein kinase C in living cells using fusion proteins with green fluorescent protein
    • Sakai N, Sasaki K, Ikegaki N, Shirai Y, Ono Y, Saito N. Direct visualization of the translocation of the γ-subspecies of protein kinase C in living cells using fusion proteins with green fluorescent protein. J Cell Biol 1997;139:1465-76.
    • (1997) J Cell Biol , vol.139 , pp. 1465-1476
    • Sakai, N.1    Sasaki, K.2    Ikegaki, N.3    Shirai, Y.4    Ono, Y.5    Saito, N.6
  • 13
    • 0032974380 scopus 로고    scopus 로고
    • Translocation and down-regulation of protein kinase C-α, -β, and -γ isoforms during ischemia-reperfusion in rat brain
    • Harada K, Maekawa T, Abu Shama KM, Yamashima T, Yoshida K. Translocation and down-regulation of protein kinase C-α, -β, and -γ isoforms during ischemia-reperfusion in rat brain. J Neurochem 1999;72:2556-64.
    • (1999) J Neurochem , vol.72 , pp. 2556-2564
    • Harada, K.1    Maekawa, T.2    Abu Shama, K.M.3    Yamashima, T.4    Yoshida, K.5
  • 14
    • 0031907117 scopus 로고    scopus 로고
    • Activation of protein kinase C triggers its ubiquitination and degradation
    • Lu Z, Liu D, Hornia A, Devonish W, Pagano M, Foster DA. Activation of protein kinase C triggers its ubiquitination and degradation. Mol Cell Biol 1998;18:839-45.
    • (1998) Mol Cell Biol , vol.18 , pp. 839-845
    • Lu, Z.1    Liu, D.2    Hornia, A.3    Devonish, W.4    Pagano, M.5    Foster, D.A.6
  • 15
    • 0024515583 scopus 로고
    • Limited proteolysis of protein kinase C subspecies by calcium-dependent neutral protease (calpain)
    • Kishimoto A, Mikawa K, Hashimoto K, et al. Limited proteolysis of protein kinase C subspecies by calcium-dependent neutral protease (calpain). J Biol Chem 1989;264:4088-92.
    • (1989) J Biol Chem , vol.264 , pp. 4088-4092
    • Kishimoto, A.1    Mikawa, K.2    Hashimoto, K.3
  • 16
    • 0027304836 scopus 로고
    • Protein kinase C-α but not protein kinase C-ε is differentially down-regulated by bryostatin 1 and tetradecanoyl phorbol 13-acetate in SH-SY5Y human neuroblastoma cells
    • Jalava A, Lintunen M, Heikkila J. Protein kinase C-α but not protein kinase C-ε is differentially down-regulated by bryostatin 1 and tetradecanoyl phorbol 13-acetate in SH-SY5Y human neuroblastoma cells. Biochem Biophys Res Commun 1993;191:472-8.
    • (1993) Biochem Biophys Res Commun , vol.191 , pp. 472-478
    • Jalava, A.1    Lintunen, M.2    Heikkila, J.3
  • 17
    • 0030941373 scopus 로고    scopus 로고
    • Growth hormone and phorbol esters require specific protein kinase C isoforms to activate mitogen-activated protein kinases in 3T3-442A cells
    • MacKenzie S, Fleming I, Houslay MD, Anderson NG, Kilgour E. Growth hormone and phorbol esters require specific protein kinase C isoforms to activate mitogen-activated protein kinases in 3T3-442A cells. Biochem J 1997;324:159-65.
    • (1997) Biochem J , vol.324 , pp. 159-165
    • MacKenzie, S.1    Fleming, I.2    Houslay, M.D.3    Anderson, N.G.4    Kilgour, E.5
  • 18
    • 0035139097 scopus 로고    scopus 로고
    • A phase II trial of bryostatin 1 in the treatment of metastatic colorectal cancer
    • Zonder JA, Shields AF, Zalupski M, et al. A phase II trial of bryostatin 1 in the treatment of metastatic colorectal cancer. Clin Cancer Res 2001;7:38-42.
    • (2001) Clin Cancer Res , vol.7 , pp. 38-42
    • Zonder, J.A.1    Shields, A.F.2    Zalupski, M.3
  • 19
    • 0034254971 scopus 로고    scopus 로고
    • A Phase II trial of bryostatin-1 for patients with metastatic renal cell carcinoma
    • Pagliaro L, Daliani D, Amato R, et al. A Phase II trial of bryostatin-1 for patients with metastatic renal cell carcinoma. Cancer 2000;89:615-8.
    • (2000) Cancer , vol.89 , pp. 615-618
    • Pagliaro, L.1    Daliani, D.2    Amato, R.3
  • 20
    • 0347995049 scopus 로고    scopus 로고
    • Phase I and correlative study of combination bryostatin 1 and vincristine in relapsed B-cell malignancies
    • Dowlati A, Lazarus HM, Hartman P, et al. Phase I and correlative study of combination bryostatin 1 and vincristine in relapsed B-cell malignancies. Clin Cancer Res 2003;9:5929-35.
    • (2003) Clin Cancer Res , vol.9 , pp. 5929-5935
    • Dowlati, A.1    Lazarus, H.M.2    Hartman, P.3
  • 21
    • 0010543768 scopus 로고
    • Bryostatin, an activator of the calcium phospholipid-dependent protein kinase, blocks phorbol ester-induced differentiation of human promyelocytic leukemia cells HL-60
    • Kraft AS, Smith JB, Berkow RL. Bryostatin, an activator of the calcium phospholipid-dependent protein kinase, blocks phorbol ester-induced differentiation of human promyelocytic leukemia cells HL-60. Proc Natl Acad Sci U S A 1986;83:1334-8.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 1334-1338
    • Kraft, A.S.1    Smith, J.B.2    Berkow, R.L.3
  • 22
    • 0028126624 scopus 로고
    • Bryostatin 1 protects protein kinase C-δ from down-regulation in mouse keratinocytes in parallel with its inhibition of phorbol ester-induced differentiation
    • Szallasi Z, Denning MF, Smith CB, et al. Bryostatin 1 protects protein kinase C-δ from down-regulation in mouse keratinocytes in parallel with its inhibition of phorbol ester-induced differentiation. Mol Pharmacol 1994;46:840-50.
    • (1994) Mol Pharmacol , vol.46 , pp. 840-850
    • Szallasi, Z.1    Denning, M.F.2    Smith, C.B.3
  • 23
    • 0023749283 scopus 로고
    • Bryostatin 1 activates protein kinase C and induces monocytic differentiation of HL-60 cells
    • Stone RM, Sariban E, Pettit GR, Kufe DW. Bryostatin 1 activates protein kinase C and induces monocytic differentiation of HL-60 cells. Blood 1988;72:208-13.
    • (1988) Blood , vol.72 , pp. 208-213
    • Stone, R.M.1    Sariban, E.2    Pettit, G.R.3    Kufe, D.W.4
  • 24
    • 0023603491 scopus 로고
    • Inhibition by bryostatin 1 of the phorbol ester-induced blockage of differentiation in hexamethylene bisacetamide-treated Friend erythroleukemia cells
    • Dell'Aquila ML, Nguyen HT, Herald CL, Pettit GR, Blumberg PM. Inhibition by bryostatin 1 of the phorbol ester-induced blockage of differentiation in hexamethylene bisacetamide-treated Friend erythroleukemia cells. Cancer Res 1987;47:6006-9.
    • (1987) Cancer Res , vol.47 , pp. 6006-6009
    • Dell'Aquila, M.L.1    Nguyen, H.T.2    Herald, C.L.3    Pettit, G.R.4    Blumberg, P.M.5
  • 25
    • 0029757465 scopus 로고    scopus 로고
    • Dephosphorylation of activated protein kinase C contributes to downregulation by bryostatin
    • Lee HW, Smith L, Pettit GR, Bingham Smith J. Dephosphorylation of activated protein kinase C contributes to downregulation by bryostatin. Am J Physiol 1996;271:C304-11.
    • (1996) Am J Physiol , vol.271
    • Lee, H.W.1    Smith, L.2    Pettit, G.R.3    Bingham Smith, J.4
  • 26
    • 0027322773 scopus 로고
    • Inhibition of phorbol ester-induced T cell proliferation by bryostatin is associated with rapid degradation of protein kinase C
    • Isakov N, Galron D, Mustelin T, Pettit GR, Altman A. Inhibition of phorbol ester-induced T cell proliferation by bryostatin is associated with rapid degradation of protein kinase C. J Immunol 1993;150:1195-204.
    • (1993) J Immunol , vol.150 , pp. 1195-1204
    • Isakov, N.1    Galron, D.2    Mustelin, T.3    Pettit, G.R.4    Altman, A.5
  • 27
    • 0028055160 scopus 로고
    • Differential regulation of protein kinase C isozymes by bryostatin 1 and phorbol 12-myristate 13-acetate in NIH 3T3 fibroblasts
    • Szallasi Z, Smith CB, Pettit GR, Blumberg PM. Differential regulation of protein kinase C isozymes by bryostatin 1 and phorbol 12-myristate 13-acetate in NIH 3T3 fibroblasts. J Biol Chem 1994;269:2118-24.
    • (1994) J Biol Chem , vol.269 , pp. 2118-2124
    • Szallasi, Z.1    Smith, C.B.2    Pettit, G.R.3    Blumberg, P.M.4
  • 28
    • 0029892167 scopus 로고    scopus 로고
    • The bryostatins inhibit growth of B16/F10 melanoma cells in vitro through a protein kinase C-independent mechanism: Dissociation of activities using 26-epi-bryostatin 1
    • Szallasi Z, Du L, Levine R, et al. The bryostatins inhibit growth of B16/F10 melanoma cells in vitro through a protein kinase C-independent mechanism: dissociation of activities using 26-epi-bryostatin 1. Cancer Res 1996;56:2105-11.
    • (1996) Cancer Res , vol.56 , pp. 2105-2111
    • Szallasi, Z.1    Du, L.2    Levine, R.3
  • 29
    • 0040909283 scopus 로고    scopus 로고
    • Regulation of caspase activation and cis-diamminedichloroplatinum(II)- induced cell death by protein kinase C
    • Basu A, Akkaraju GR. Regulation of caspase activation and cis-diamminedichloroplatinum(II)-induced cell death by protein kinase C. Biochemistry 1999;38:4245-51.
    • (1999) Biochemistry , vol.38 , pp. 4245-4251
    • Basu, A.1    Akkaraju, G.R.2
  • 30
    • 0031455382 scopus 로고    scopus 로고
    • The catalytic domain of protein kinase Cδ confers protection from down-regulation induced by bryostatin 1
    • Lorenzo PS, Bogi K, Acs P, Pettit GR, Blumberg PM. The catalytic domain of protein kinase Cδ confers protection from down-regulation induced by bryostatin 1. J Biol Chem 1997;272:33338-43.
    • (1997) J Biol Chem , vol.272 , pp. 33338-33343
    • Lorenzo, P.S.1    Bogi, K.2    Acs, P.3    Pettit, G.R.4    Blumberg, P.M.5
  • 31
    • 0343819883 scopus 로고    scopus 로고
    • Differential roles of the tandem C1 domains of protein kinase Cδ in the biphasic down-regulation induced by bryostatin 1
    • Lorenzo PS, Bogi K, Hughes KM, et al. Differential roles of the tandem C1 domains of protein kinase Cδ in the biphasic down-regulation induced by bryostatin 1. Cancer Res 1999;59:6137-44.
    • (1999) Cancer Res , vol.59 , pp. 6137-6144
    • Lorenzo, P.S.1    Bogi, K.2    Hughes, K.M.3
  • 32
    • 0025331728 scopus 로고
    • Differentiation capacity of human non-small-cell lung cancer cell lines after exposure to phorbol ester
    • Salge U, Kilian P, Neumann K, Elsasser HP, Havemann K, Heidtmann HH. Differentiation capacity of human non-small-cell lung cancer cell lines after exposure to phorbol ester. Int J Cancer 1990;45:1143-50.
    • (1990) Int J Cancer , vol.45 , pp. 1143-1150
    • Salge, U.1    Kilian, P.2    Neumann, K.3    Elsasser, H.P.4    Havemann, K.5    Heidtmann, H.H.6
  • 33
    • 0035829436 scopus 로고    scopus 로고
    • Iridals are a novel class of ligands for phorbol ester receptors with modest selectivity for the RasGRP receptor subfamily
    • Shao L, Lewin NE, Lorenzo PS, et al. Iridals are a novel class of ligands for phorbol ester receptors with modest selectivity for the RasGRP receptor subfamily. J Med Chem 2001;44:3872-80.
    • (2001) J Med Chem , vol.44 , pp. 3872-3880
    • Shao, L.1    Lewin, N.E.2    Lorenzo, P.S.3
  • 34
    • 0034042882 scopus 로고    scopus 로고
    • Bryostatin 1 induces prolonged activation of extracellular regulated protein kinases in and apoptosis of LNCaP human prostate cancer cells overexpressing protein kinase Cα
    • Gschwend JE, Fair WR, Powell CT. Bryostatin 1 induces prolonged activation of extracellular regulated protein kinases in and apoptosis of LNCaP human prostate cancer cells overexpressing protein kinase Cα. Mol Pharmacol 2000;57:1224-34.
    • (2000) Mol Pharmacol , vol.57 , pp. 1224-1234
    • Gschwend, J.E.1    Fair, W.R.2    Powell, C.T.3
  • 35
    • 0030987070 scopus 로고    scopus 로고
    • Regulation of protein kinase C
    • Newton AC. Regulation of protein kinase C. Curr Opin Cell Biol 1997;9:161-7.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 161-167
    • Newton, A.C.1
  • 36
    • 0032547233 scopus 로고    scopus 로고
    • Transforming growth factor-β1-induced activation of the Raf-MEK-MAPK signaling pathway in rat lung fibroblasts via a PKC-dependent mechanism
    • Axmann A, Seidel D, Reimann T, Hempel U, Wenzel KW. Transforming growth factor-β1-induced activation of the Raf-MEK-MAPK signaling pathway in rat lung fibroblasts via a PKC-dependent mechanism. Biochem Biophys Res Commun 1998;249:456-60.
    • (1998) Biochem Biophys Res Commun , vol.249 , pp. 456-460
    • Axmann, A.1    Seidel, D.2    Reimann, T.3    Hempel, U.4    Wenzel, K.W.5
  • 38
    • 1542619344 scopus 로고    scopus 로고
    • Protein kinase C isozymes as potential targets for anticancer therapy
    • Hofmann J. Protein kinase C isozymes as potential targets for anticancer therapy. Curr Cancer Drug Targets 2004;4:125-46.
    • (2004) Curr Cancer Drug Targets , vol.4 , pp. 125-146
    • Hofmann, J.1
  • 39
  • 40
    • 0027212503 scopus 로고
    • Nonpromoting 12-deoxyphorbol 13-esters inhibit phorbol 12-myristate 13-acetate induced tumor promotion in CD-1 mouse skin
    • Szallasi Z, Krsmanovic L, Blumberg PM. Nonpromoting 12-deoxyphorbol 13-esters inhibit phorbol 12-myristate 13-acetate induced tumor promotion in CD-1 mouse skin. Cancer Res 1993;53:2507-12.
    • (1993) Cancer Res , vol.53 , pp. 2507-2512
    • Szallasi, Z.1    Krsmanovic, L.2    Blumberg, P.M.3
  • 41
    • 0024312538 scopus 로고
    • Display and analysis of patterns of differential activity of drugs against human tumor cell lines: Development of mean graph and COMPARE algorithm
    • Paull KD, Shoemaker RH, Hodes L, et al. Display and analysis of patterns of differential activity of drugs against human tumor cell lines: development of mean graph and COMPARE algorithm. J Natl Cancer Inst 1989;81:1088-92.
    • (1989) J Natl Cancer Inst , vol.81 , pp. 1088-1092
    • Paull, K.D.1    Shoemaker, R.H.2    Hodes, L.3
  • 42
    • 0026472991 scopus 로고
    • Cell division arrest induced by phorbol ester in CHO cells overexpressing protein kinase C-δ subspecies
    • Watanabe T, Ono Y, Taniyama Y, et al. Cell division arrest induced by phorbol ester in CHO cells overexpressing protein kinase C-δ subspecies. Proc Natl Acad Sci U S A 1992;89:10159-63.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 10159-10163
    • Watanabe, T.1    Ono, Y.2    Taniyama, Y.3
  • 44
    • 0028303818 scopus 로고
    • Opposite effects of the overexpression of protein kinase C γ and δ on the growth properties of human glioma cell line U251 MG
    • Mishima K, Ohno S, Shitara N, Yamaoka K, Suzuki K. Opposite effects of the overexpression of protein kinase C γ and δ on the growth properties of human glioma cell line U251 MG. Biochem Biophys Res Commun 1994;201:363-72.
    • (1994) Biochem Biophys Res Commun , vol.201 , pp. 363-372
    • Mishima, K.1    Ohno, S.2    Shitara, N.3    Yamaoka, K.4    Suzuki, K.5
  • 45
    • 0031001002 scopus 로고    scopus 로고
    • Enhancement of migration by protein kinase Cα and inhibition of proliferation and cell cycle progression by protein kinase Cδ in capillary endothelial cells
    • Harrington EO, Loffler J, Nelson PR, Kent KC, Simons M, Ware JA. Enhancement of migration by protein kinase Cα and inhibition of proliferation and cell cycle progression by protein kinase Cδ in capillary endothelial cells. J Biol Chem 1997;272:7390-7.
    • (1997) J Biol Chem , vol.272 , pp. 7390-7397
    • Harrington, E.O.1    Loffler, J.2    Nelson, P.R.3    Kent, K.C.4    Simons, M.5    Ware, J.A.6
  • 46
    • 0033597645 scopus 로고    scopus 로고
    • Protein kinase Cδ inhibition of S-phase transition in capillary endothelial cells involves the cyclin-dependent kinase inhibitor p27(Kip1)
    • Ashton AW, Watanabe G, Albanese C, Harrington EO, Ware JA, Pestell RG. Protein kinase Cδ inhibition of S-phase transition in capillary endothelial cells involves the cyclin-dependent kinase inhibitor p27(Kip1). J Biol Chem 1999;274:20805-11.
    • (1999) J Biol Chem , vol.274 , pp. 20805-20811
    • Ashton, A.W.1    Watanabe, G.2    Albanese, C.3    Harrington, E.O.4    Ware, J.A.5    Pestell, R.G.6
  • 47
    • 0037246123 scopus 로고    scopus 로고
    • Regulation of cell apoptosis by protein kinase Cδ
    • Brodie C, Blumberg PM. Regulation of cell apoptosis by protein kinase Cδ. Apoptosis 2003;8:19-27.
    • (2003) Apoptosis , vol.8 , pp. 19-27
    • Brodie, C.1    Blumberg, P.M.2
  • 48
    • 20444400826 scopus 로고    scopus 로고
    • PKCδ-induced activation of MAPK pathway is required for bFGF-stimulated proliferation of coronary smooth muscle cells
    • Skaletz-Rorowski A, Eschert H, Leng J, et al. PKCδ-induced activation of MAPK pathway is required for bFGF-stimulated proliferation of coronary smooth muscle cells. Cardiovasc Res 2005;67:142-50.
    • (2005) Cardiovasc Res , vol.67 , pp. 142-150
    • Skaletz-Rorowski, A.1    Eschert, H.2    Leng, J.3
  • 49
    • 0027971632 scopus 로고
    • Interferons block protein kinase C-dependent but not-independent activation of Raf-1 and mitogen-activated protein kinases and mitogenesis in NIH 3T3 cells
    • Xu J, Rockow S, Kim S, Xiong W, Li W. Interferons block protein kinase C-dependent but not-independent activation of Raf-1 and mitogen-activated protein kinases and mitogenesis in NIH 3T3 cells. Mol Cell Biol 1994;14:8018-27.
    • (1994) Mol Cell Biol , vol.14 , pp. 8018-8027
    • Xu, J.1    Rockow, S.2    Kim, S.3    Xiong, W.4    Li, W.5
  • 50
    • 0037397365 scopus 로고    scopus 로고
    • 1 is required for DNA synthesis in serum-induced cell cycle progression
    • 1 is required for DNA synthesis in serum-induced cell cycle progression. Genes Cells 2003;8:311-24.
    • (2003) Genes Cells , vol.8 , pp. 311-324
    • Kitamura, K.1    Mizuno, K.2    Etoh, A.3
  • 51
    • 0037443030 scopus 로고    scopus 로고
    • Altered protein kinase C (PKC) isoforms in non-small cell lung cancer cells: PKCδ promotes cellular survival and chemotherapeutic resistance
    • Clark AS, West KA, Blumberg PM, Dennis PA. Altered protein kinase C (PKC) isoforms in non-small cell lung cancer cells: PKCδ promotes cellular survival and chemotherapeutic resistance. Cancer Res 2003;63:780-6.
    • (2003) Cancer Res , vol.63 , pp. 780-786
    • Clark, A.S.1    West, K.A.2    Blumberg, P.M.3    Dennis, P.A.4
  • 52
    • 0032076149 scopus 로고    scopus 로고
    • The pathogenesis of squamous cell cancer: Lessons learned from studies of skin carcinogenesis
    • Yuspa SH. The pathogenesis of squamous cell cancer: lessons learned from studies of skin carcinogenesis. J Dermatol Sci 1998;17:1-7.
    • (1998) J Dermatol Sci , vol.17 , pp. 1-7
    • Yuspa, S.H.1
  • 53
    • 10944238407 scopus 로고    scopus 로고
    • Distinctive activation mechanisms and functions for protein kinase Cδ
    • Steinberg SF. Distinctive activation mechanisms and functions for protein kinase Cδ. Biochem J 2004;384:449-59.
    • (2004) Biochem J , vol.384 , pp. 449-459
    • Steinberg, S.F.1
  • 54
    • 0036947279 scopus 로고    scopus 로고
    • Protein kinase Cδ (PKCδ): Activation mechanisms and functions
    • Kikkawa U, Matsuzaki H, Yamamoto T. Protein kinase Cδ (PKCδ): activation mechanisms and functions. J Biochem (Tokyo) 2002;132:831-9.
    • (2002) J Biochem (Tokyo) , vol.132 , pp. 831-839
    • Kikkawa, U.1    Matsuzaki, H.2    Yamamoto, T.3
  • 55
    • 0042466484 scopus 로고    scopus 로고
    • Antisense strategies targeting protein kinase C: Preclinical and clinical development
    • Tortora G, Ciardiello F. Antisense strategies targeting protein kinase C: preclinical and clinical development. Semin Oncol 2003;30:26-31.
    • (2003) Semin Oncol , vol.30 , pp. 26-31
    • Tortora, G.1    Ciardiello, F.2
  • 56
    • 22844435317 scopus 로고    scopus 로고
    • A novel diacylglycerol-lactone shows marked selectivity in vitro among C1 domains of protein kinase C (PKC) isoforms α and δ as well as selectivity for RasGRP compared with PKCα
    • Pu Y, Perry NA, Yang D, et al. A novel diacylglycerol-lactone shows marked selectivity in vitro among C1 domains of protein kinase C (PKC) isoforms α and δ as well as selectivity for RasGRP compared with PKCα. J Biol Chem 2005;280:27329-38.
    • (2005) J Biol Chem , vol.280 , pp. 27329-27338
    • Pu, Y.1    Perry, N.A.2    Yang, D.3


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