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Volumn 289, Issue 15, 2014, Pages 10900-10908

Inhibiting tyrosine phosphorylation of protein kinase Cδ (PKCδ) protects the salivary gland from radiation damage

Author keywords

[No Author keywords available]

Indexed keywords

CELL DEATH; ENZYME INHIBITION; HISTOLOGY; IRRADIATION; PHOSPHORYLATION; RADIATION DAMAGE; RADIOTHERAPY; TISSUE;

EID: 84898632704     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.551366     Document Type: Article
Times cited : (24)

References (49)
  • 3
    • 33646257584 scopus 로고    scopus 로고
    • Protein kinase Cδ activates topoisomerase IIα to induce apoptotic cell death in response to DNA damage
    • Yoshida, K., Yamaguchi, T., Shinagawa, H., Taira, N., Nakayama, K. I., and Miki, Y. (2006) Protein kinase Cδ activates topoisomerase IIα to induce apoptotic cell death in response to DNA damage. Mol. Cell. Biol. 26, 3414-3431
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 3414-3431
    • Yoshida, K.1    Yamaguchi, T.2    Shinagawa, H.3    Taira, N.4    Nakayama, K.I.5    Miki, Y.6
  • 4
    • 33846827369 scopus 로고    scopus 로고
    • Endometrial cancer cell survival and apoptosis is regulated by protein kinase Cα andδ
    • Haughian, J. M., Jackson, T. A., Koterwas, D. M., and Bradford, A. P. (2006) Endometrial cancer cell survival and apoptosis is regulated by protein kinase Cα andδ. Endocr. Relat. Cancer 13, 1251-1267
    • (2006) Endocr. Relat. Cancer , vol.13 , pp. 1251-1267
    • Haughian, J.M.1    Jackson, T.A.2    Koterwas, D.M.3    Bradford, A.P.4
  • 5
    • 74249091716 scopus 로고    scopus 로고
    • Protein kinase Cδ mediates arterial injury responses through regulation of vascular smooth muscle cell apoptosis
    • Yamanouchi, D., Kato, K., Ryer, E. J., Zhang, F., and Liu, B. (2010) Protein kinase Cδ mediates arterial injury responses through regulation of vascular smooth muscle cell apoptosis. Cardiovasc. Res. 85, 434-443
    • (2010) Cardiovasc. Res. , vol.85 , pp. 434-443
    • Yamanouchi, D.1    Kato, K.2    Ryer, E.J.3    Zhang, F.4    Liu, B.5
  • 7
    • 33646480748 scopus 로고    scopus 로고
    • Protein kinase PKCδ and c-Abl are required for mitochondrial apoptosis induction by genotoxic stress in the absence of p53, p73 and Fas receptor
    • Lasfer, M., Davenne, L., Vadrot, N., Alexia, C., Sadji-Ouatas, Z., Bringuier, A. F., Feldmann, G., Pessayre, D., and Reyl-Desmars, F. (2006) Protein kinase PKCδ and c-Abl are required for mitochondrial apoptosis induction by genotoxic stress in the absence of p53, p73 and Fas receptor. FEBS Lett. 580, 2547-2552
    • (2006) FEBS Lett. , vol.580 , pp. 2547-2552
    • Lasfer, M.1    Davenne, L.2    Vadrot, N.3    Alexia, C.4    Sadji-Ouatas, Z.5    Bringuier, A.F.6    Feldmann, G.7    Pessayre, D.8    Reyl-Desmars, F.9
  • 9
    • 34547956887 scopus 로고    scopus 로고
    • Induction of apoptosis is driven by nuclear retention of protein kinase Cδ
    • DeVries-Seimon, T. A., Ohm, A. M., Humphries, M. J., and Reyland, M. E. (2007) Induction of apoptosis is driven by nuclear retention of protein kinase Cδ. J. Biol. Chem. 282, 22307-22314
    • (2007) J. Biol. Chem. , vol.282 , pp. 22307-22314
    • Devries-Seimon, T.A.1    Ohm, A.M.2    Humphries, M.J.3    Reyland, M.E.4
  • 10
    • 0037110732 scopus 로고    scopus 로고
    • Nuclear import of PKCδ is required for apoptosis: Identification of a novel nuclear import sequence
    • DeVries, T. A., Neville, M. C., and Reyland, M. E. (2002) Nuclear import of PKCδ is required for apoptosis: identification of a novel nuclear import sequence. EMBO J. 21, 6050-6060
    • (2002) EMBO J. , vol.21 , pp. 6050-6060
    • Devries, T.A.1    Neville, M.C.2    Reyland, M.E.3
  • 11
    • 43449109771 scopus 로고    scopus 로고
    • Tyrosine phosphorylation regulates nuclear translocation of PKCδ
    • Humphries, M. J., Ohm, A. M., Schaack, J., Adwan, T. S., and Reyland, M. E. (2008) Tyrosine phosphorylation regulates nuclear translocation of PKCδ. Oncogene 27, 3045-3053
    • (2008) Oncogene , vol.27 , pp. 3045-3053
    • Humphries, M.J.1    Ohm, A.M.2    Schaack, J.3    Adwan, T.S.4    Reyland, M.E.5
  • 12
    • 80053909804 scopus 로고    scopus 로고
    • Regulated binding of importin-α to protein kinase Cδ in response to apoptotic signals facilitates nuclear import
    • Adwan, T. S., Ohm, A. M., Jones, D. N., Humphries, M. J., and Reyland, M. E. (2011) Regulated binding of importin-α to protein kinase Cδ in response to apoptotic signals facilitates nuclear import. J. Biol. Chem. 286, 35716-35724
    • (2011) J. Biol. Chem. , vol.286 , pp. 35716-35724
    • Adwan, T.S.1    Ohm, A.M.2    Jones, D.N.3    Humphries, M.J.4    Reyland, M.E.5
  • 13
    • 0033516666 scopus 로고    scopus 로고
    • Protein kinase Cδ is essential for etoposide-induced apoptosis in salivary gland acinar cells
    • Reyland, M. E., Anderson, S. M., Matassa, A. A., Barzen, K. A., and Quissell, D. O. (1999) Protein kinase Cδ is essential for etoposide-induced apoptosis in salivary gland acinar cells. J. Biol. Chem. 274, 19115-19123
    • (1999) J. Biol. Chem. , vol.274 , pp. 19115-19123
    • Reyland, M.E.1    Anderson, S.M.2    Matassa, A.A.3    Barzen, K.A.4    Quissell, D.O.5
  • 14
    • 84895924663 scopus 로고    scopus 로고
    • Protein kinase Cδ is required for ErbB2-driven mammary gland tumorigenesis and negatively correlates with prognosis in human breast cancer
    • Allen-Petersen, B. L., Carter, C. J., Ohm, A. M., and Reyland, M. E. (2014) Protein kinase Cδ is required for ErbB2-driven mammary gland tumorigenesis and negatively correlates with prognosis in human breast cancer. Oncogene 13, 1306-1315
    • (2014) Oncogene , vol.13 , pp. 1306-1315
    • Allen-Petersen, B.L.1    Carter, C.J.2    Ohm, A.M.3    Reyland, M.E.4
  • 17
    • 63849136153 scopus 로고    scopus 로고
    • Protein kinase C isoforms: Multi-functional regulators of cell life and death
    • Reyland, M. E. (2009) Protein kinase C isoforms: multi-functional regulators of cell life and death. Front. Biosci. 14, 2386-2399
    • (2009) Front. Biosci. , vol.14 , pp. 2386-2399
    • Reyland, M.E.1
  • 18
    • 79955534014 scopus 로고    scopus 로고
    • P23/Tmp21 associates with protein kinase Cδ (PKCδ) and modulates its apoptotic function
    • Wang, H., Xiao, L., and Kazanietz, M. G. (2011) p23/Tmp21 associates with protein kinase Cδ (PKCδ) and modulates its apoptotic function. J. Biol. Chem. 286, 15821-15831
    • (2011) J. Biol. Chem. , vol.286 , pp. 15821-15831
    • Wang, H.1    Xiao, L.2    Kazanietz, M.G.3
  • 19
    • 34250828549 scopus 로고    scopus 로고
    • The localization of protein kinase Cδ in different subcellular sites affects its proapoptotic and antiapoptotic functions and the activation of distinct downstream signaling pathways
    • Gomel, R., Xiang, C., Finniss, S., Lee, H. K., Lu, W., Okhrimenko, H., and Brodie, C. (2007) The localization of protein kinase Cδ in different subcellular sites affects its proapoptotic and antiapoptotic functions and the activation of distinct downstream signaling pathways. Mol. Cancer Res. 5, 627-639
    • (2007) Mol. Cancer Res. , vol.5 , pp. 627-639
    • Gomel, R.1    Xiang, C.2    Finniss, S.3    Lee, H.K.4    Lu, W.5    Okhrimenko, H.6    Brodie, C.7
  • 21
    • 78650635555 scopus 로고    scopus 로고
    • Protein kinase Cδ-specific activity reporter reveals agonist-evoked nuclear activity controlled by Src family of kinases
    • Kajimoto, T., Sawamura, S., Tohyama, Y., Mori, Y., and Newton, A. C. (2010) Protein kinase Cδ-specific activity reporter reveals agonist-evoked nuclear activity controlled by Src family of kinases. J. Biol. Chem. 285, 41896-41910
    • (2010) J. Biol. Chem. , vol.285 , pp. 41896-41910
    • Kajimoto, T.1    Sawamura, S.2    Tohyama, Y.3    Mori, Y.4    Newton, A.C.5
  • 22
    • 38949105094 scopus 로고    scopus 로고
    • EGF regulates plasminogen activator inhibitor-1 (PAI-1) by a pathway involving c-Src, PKCδ, and sphingosine kinase 1 in glioblastoma cells
    • Paugh, B. S., Paugh, S. W., Bryan, L., Kapitonov, D., Wilczynska, K. M., Gopalan, S. M., Rokita, H., Milstien, S., Spiegel, S., and Kordula, T. (2008) EGF regulates plasminogen activator inhibitor-1 (PAI-1) by a pathway involving c-Src, PKCδ, and sphingosine kinase 1 in glioblastoma cells. FASEB J. 22, 455-465
    • (2008) FASEB J. , vol.22 , pp. 455-465
    • Paugh, B.S.1    Paugh, S.W.2    Bryan, L.3    Kapitonov, D.4    Wilczynska, K.M.5    Gopalan, S.M.6    Rokita, H.7    Milstien, S.8    Spiegel, S.9    Kordula, T.10
  • 23
    • 34548183625 scopus 로고    scopus 로고
    • Protein kinase Cδ (PKCδ) and Src control PKCδ activation loop phosphorylation in cardiomyocytes
    • Rybin, V. O., Guo, J., Gertsberg, Z., Elouardighi, H., and Steinberg, S. F. (2007) Protein kinase Cδ (PKCδ) and Src control PKCδ activation loop phosphorylation in cardiomyocytes. J. Biol. Chem. 282, 23631-23638
    • (2007) J. Biol. Chem. , vol.282 , pp. 23631-23638
    • Rybin, V.O.1    Guo, J.2    Gertsberg, Z.3    Elouardighi, H.4    Steinberg, S.F.5
  • 24
    • 14844334157 scopus 로고    scopus 로고
    • Phorbol 12-myristate 13-acetate induces epidermal growth factor receptor transactivation via protein kinase Cδ/c-Src pathways in glioblastoma cells
    • Amos, S., Martin, P. M., Polar, G. A., Parsons, S. J., and Hussaini, I. M. (2005) Phorbol 12-myristate 13-acetate induces epidermal growth factor receptor transactivation via protein kinase Cδ/c-Src pathways in glioblastoma cells. J. Biol. Chem. 280, 7729-7738
    • (2005) J. Biol. Chem. , vol.280 , pp. 7729-7738
    • Amos, S.1    Martin, P.M.2    Polar, G.A.3    Parsons, S.J.4    Hussaini, I.M.5
  • 25
    • 0033027608 scopus 로고    scopus 로고
    • Etoposide-induced activation of c-Jun N-terminal kinase (JNK) correlates with drug-induced apoptosis in salivary gland acinar cells
    • Anderson, S. M., Reyland, M. E., Hunter, S., Deisher, L. M., Barzen, K. A., and Quissell, D. O. (1999) Etoposide-induced activation of c-Jun N-terminal kinase (JNK) correlates with drug-induced apoptosis in salivary gland acinar cells. Cell Death Differ. 6, 454-462
    • (1999) Cell Death Differ. , vol.6 , pp. 454-462
    • Anderson, S.M.1    Reyland, M.E.2    Hunter, S.3    Deisher, L.M.4    Barzen, K.A.5    Quissell, D.O.6
  • 26
    • 49649097536 scopus 로고    scopus 로고
    • Phorbol 12-myristate 13-acetate-dependent protein kinase Cδ-Tyr-311 phosphorylation in cardiomyocyte caveolae
    • Rybin, V. O., Guo, J., Gertsberg, Z., Feinmark, S. J., and Steinberg, S. F. (2008) Phorbol 12-myristate 13-acetate-dependent protein kinase Cδ-Tyr-311 phosphorylation in cardiomyocyte caveolae. J. Biol. Chem. 283, 17777-17788
    • (2008) J. Biol. Chem. , vol.283 , pp. 17777-17788
    • Rybin, V.O.1    Guo, J.2    Gertsberg, Z.3    Feinmark, S.J.4    Steinberg, S.F.5
  • 27
    • 84872243145 scopus 로고    scopus 로고
    • Tyrosine kinase inhibitors: Views of selectivity, sensitivity, and clinical performance
    • Levitzki, A. (2013) Tyrosine kinase inhibitors: views of selectivity, sensitivity, and clinical performance. Annu. Rev. Pharmacol. Toxicol. 53, 161-185
    • (2013) Annu. Rev. Pharmacol. Toxicol. , vol.53 , pp. 161-185
    • Levitzki, A.1
  • 28
    • 17144369501 scopus 로고    scopus 로고
    • Oxidative activation of protein kinase Cδ through the C1 domain. Effects on gap junctions
    • Lin, D., and Takemoto, D. J. (2005) Oxidative activation of protein kinase Cδ through the C1 domain. Effects on gap junctions. J. Biol. Chem. 280, 13682-13693
    • (2005) J. Biol. Chem. , vol.280 , pp. 13682-13693
    • Lin, D.1    Takemoto, D.J.2
  • 29
    • 27144547509 scopus 로고    scopus 로고
    • Action of the Src family kinase inhibitor, dasatinib (BMS-354825), on human prostate cancer cells
    • Nam, S., Kim, D., Cheng, J. Q., Zhang, S., Lee, J. H., Buettner, R., Mirosevich, J., Lee, F. Y., and Jove, R. (2005) Action of the Src family kinase inhibitor, dasatinib (BMS-354825), on human prostate cancer cells. Cancer Res. 65, 9185-9189
    • (2005) Cancer Res. , vol.65 , pp. 9185-9189
    • Nam, S.1    Kim, D.2    Cheng, J.Q.3    Zhang, S.4    Lee, J.H.5    Buettner, R.6    Mirosevich, J.7    Lee, F.Y.8    Jove, R.9
  • 30
    • 42049123098 scopus 로고    scopus 로고
    • Target spectrum of the BCR-ABL inhibitors imatinib, nilotinib and dasatinib
    • Hantschel, O., Rix, U., and Superti-Furga, G. (2008) Target spectrum of the BCR-ABL inhibitors imatinib, nilotinib and dasatinib. Leuk. Lymphoma 49, 615-619
    • (2008) Leuk. Lymphoma , vol.49 , pp. 615-619
    • Hantschel, O.1    Rix, U.2    Superti-Furga, G.3
  • 31
  • 32
    • 84858706707 scopus 로고    scopus 로고
    • A new orally active, aminothiol radioprotector-free of nausea and hypotension side effects at its highest radioprotective doses
    • Soref, C. M., Hacker, T. A., and Fahl, W. E. (2012) A new orally active, aminothiol radioprotector-free of nausea and hypotension side effects at its highest radioprotective doses. Int. J. Radiat. Oncol. Biol. Phys. 82, e701-7
    • (2012) Int. J. Radiat. Oncol. Biol. Phys. , vol.82
    • Soref, C.M.1    Hacker, T.A.2    Fahl, W.E.3
  • 36
    • 84863644570 scopus 로고    scopus 로고
    • Oxidative stress,DNAdamage, and c-Abl signaling: At the crossroad in neurodegenerative diseases?
    • Gonfloni, S., Maiani, E., Di Bartolomeo, C., Diederich, M., and Cesareni, G. (2012) Oxidative stress,DNAdamage, and c-Abl signaling: at the crossroad in neurodegenerative diseases? Int. J. Cell Biol. 2012, 683097-683107
    • (2012) Int. J. Cell Biol. , vol.2012 , pp. 683097-683107
    • Gonfloni, S.1    Maiani, E.2    Di Bartolomeo, C.3    Diederich, M.4    Cesareni, G.5
  • 37
    • 70449490047 scopus 로고    scopus 로고
    • Lyn, PKCδ, SHIP-1 interactions regulate GPVI-mediated platelet-dense granule secretion
    • Chari, R., Kim, S., Murugappan, S., Sanjay, A., Daniel, J. L., and Kunapuli, S. P. (2009) Lyn, PKCδ, SHIP-1 interactions regulate GPVI-mediated platelet-dense granule secretion. Blood 114, 3056-3063
    • (2009) Blood , vol.114 , pp. 3056-3063
    • Chari, R.1    Kim, S.2    Murugappan, S.3    Sanjay, A.4    Daniel, J.L.5    Kunapuli, S.P.6
  • 38
    • 79959934717 scopus 로고    scopus 로고
    • Inhibition of PKCδ reduces cisplatin-induced nephrotoxicity without blocking chemotherapeutic efficacy in mouse models of cancer
    • Pabla, N., Dong, G., Jiang, M., Huang, S., Kumar, M. V., Messing, R. O., and Dong, Z. (2011) Inhibition of PKCδ reduces cisplatin-induced nephrotoxicity without blocking chemotherapeutic efficacy in mouse models of cancer. J. Clin. Invest. 121, 2709-2722
    • (2011) J. Clin. Invest. , vol.121 , pp. 2709-2722
    • Pabla, N.1    Dong, G.2    Jiang, M.3    Huang, S.4    Kumar, M.V.5    Messing, R.O.6    Dong, Z.7
  • 40
    • 4444233869 scopus 로고    scopus 로고
    • Src tyrosine kinase regulates insulin-induced activation of protein kinase C (PKC)δ in skeletal muscle
    • Rosenzweig, T., Aga-Mizrachi, S., Bak, A., and Sampson, S. R. (2004) Src tyrosine kinase regulates insulin-induced activation of protein kinase C (PKC)δ in skeletal muscle. Cell. Signal. 16, 1299-1308
    • (2004) Cell. Signal. , vol.16 , pp. 1299-1308
    • Rosenzweig, T.1    Aga-Mizrachi, S.2    Bak, A.3    Sampson, S.R.4
  • 41
    • 0037160074 scopus 로고    scopus 로고
    • Ligand-independent trans-activation of the platelet-derived growth factor receptor by reactive oxygen species requires protein kinase Cδ and c-Src
    • Saito, S., Frank, G. D., Mifune, M., Ohba, M., Utsunomiya, H., Motley, E. D., Inagami, T., and Eguchi, S. (2002) Ligand-independent trans-activation of the platelet-derived growth factor receptor by reactive oxygen species requires protein kinase Cδ and c-Src. J. Biol. Chem. 277, 44695-44700
    • (2002) J. Biol. Chem. , vol.277 , pp. 44695-44700
    • Saito, S.1    Frank, G.D.2    Mifune, M.3    Ohba, M.4    Utsunomiya, H.5    Motley, E.D.6    Inagami, T.7    Eguchi, S.8
  • 42
    • 23344444562 scopus 로고    scopus 로고
    • Tyrosine phosphorylation regulates the proteolytic activation of protein kinase Cδ in dopaminergic neuronal cells
    • Kaul, S., Anantharam, V., Yang, Y., Choi, C. J., Kanthasamy, A., and Kanthasamy, A. G. (2005) Tyrosine phosphorylation regulates the proteolytic activation of protein kinase Cδ in dopaminergic neuronal cells. J. Biol. Chem. 280, 28721-28730
    • (2005) J. Biol. Chem. , vol.280 , pp. 28721-28730
    • Kaul, S.1    Anantharam, V.2    Yang, Y.3    Choi, C.J.4    Kanthasamy, A.5    Kanthasamy, A.G.6
  • 43
    • 0037113925 scopus 로고    scopus 로고
    • Zinc release from protein kinase C as the common event during activation by lipid second messenger or reactive oxygen
    • Korichneva, I., Hoyos, B., Chua, R., Levi, E., and Hammerling, U. (2002) Zinc release from protein kinase C as the common event during activation by lipid second messenger or reactive oxygen. J. Biol. Chem. 277, 44327-44331
    • (2002) J. Biol. Chem. , vol.277 , pp. 44327-44331
    • Korichneva, I.1    Hoyos, B.2    Chua, R.3    Levi, E.4    Hammerling, U.5
  • 46
    • 84859613225 scopus 로고    scopus 로고
    • Pro-apoptotic gene knockdown mediated by nanocomplexed siRNA reduces radiation damage in primary salivary gland cultures
    • Arany, S., Xu, Q., Hernady, E., Benoit, D. S., Dewhurst, S., and Ovitt, C. E. (2012) Pro-apoptotic gene knockdown mediated by nanocomplexed siRNA reduces radiation damage in primary salivary gland cultures. J. Cell. Biochem. 113, 1955-1965
    • (2012) J. Cell. Biochem. , vol.113 , pp. 1955-1965
    • Arany, S.1    Xu, Q.2    Hernady, E.3    Benoit, D.S.4    Dewhurst, S.5    Ovitt, C.E.6
  • 47
    • 84878560006 scopus 로고    scopus 로고
    • Nanoparticlemediated gene silencing confers radioprotection to salivary glands in vivo
    • Arany, S., Benoit, D. S., Dewhurst, S., and Ovitt, C. E. (2013) Nanoparticlemediated gene silencing confers radioprotection to salivary glands in vivo. Mol. Ther. 21, 1182-1194
    • (2013) Mol. Ther. , vol.21 , pp. 1182-1194
    • Arany, S.1    Benoit, D.S.2    Dewhurst, S.3    Ovitt, C.E.4
  • 49
    • 84865649644 scopus 로고    scopus 로고
    • Degradation of epidermal growth factor receptor mediates dasatinib-induced apoptosis in head and neck squamous cell carcinoma cells
    • Lin, Y. C., Wu, M. H., Wei, T. T., Chuang, S. H., Chen, K. F., Cheng, A. L., and Chen, C. C. (2012) Degradation of epidermal growth factor receptor mediates dasatinib-induced apoptosis in head and neck squamous cell carcinoma cells. Neoplasia 14, 463-475
    • (2012) Neoplasia , vol.14 , pp. 463-475
    • Lin, Y.C.1    Wu, M.H.2    Wei, T.T.3    Chuang, S.H.4    Chen, K.F.5    Cheng, A.L.6    Chen, C.C.7


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