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Volumn 10, Issue 2, 2005, Pages 341-348

Phosphorylation of Bad is not essential for PKB-mediated survival signaling in hemopoietic cells

Author keywords

Bad; Cytokine; Phosphorylation; Survival

Indexed keywords

CERAMIDE; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; INTERLEUKIN 3; INTERLEUKIN 4; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN BAD; PROTEIN KINASE B; SERINE;

EID: 18044364020     PISSN: 13608185     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10495-005-0808-4     Document Type: Article
Times cited : (10)

References (57)
  • 1
    • 0029900071 scopus 로고    scopus 로고
    • Cytokine regulation of apoptosis in hematopoietic precursor cells
    • Park JR. Cytokine regulation of apoptosis in hematopoietic precursor cells. Curr. Opinion in Hematology 1996; 3: 191.
    • (1996) Curr. Opinion in Hematology , vol.3 , pp. 191
    • Park, J.R.1
  • 2
    • 0030057331 scopus 로고    scopus 로고
    • Control of apoptosis in hematopoiesis and leukemia by cytokines, tumor suppressor and oncogenes
    • Lotem, J, Sachs L. Control of apoptosis in hematopoiesis and leukemia by cytokines, tumor suppressor and oncogenes. Leukemia 1996; 10: 925.
    • (1996) Leukemia , vol.10 , pp. 925
    • Lotem, J.1    Sachs, L.2
  • 3
    • 0026448779 scopus 로고
    • Prolongation of survival of human polymorphonuclear neutrophils by granulocyte-macrophage colony-stimulating factor is caused by inhibition of programmed cell death
    • Brach MA, deVos S, Gruss HJ, Herrmann F. Prolongation of survival of human polymorphonuclear neutrophils by granulocyte-macrophage colony-stimulating factor is caused by inhibition of programmed cell death. Blood 1992; 80: 2920.
    • (1992) Blood , vol.80 , pp. 2920
    • Brach, M.A.1    DeVos, S.2    Gruss, H.J.3    Herrmann, F.4
  • 4
    • 0028834557 scopus 로고
    • Role of phosphatidylinositol 3-OH-kinase activity in the inhibition of apoptosis in haemopoietic cells: Phosphatidylinositol 3-OH-kinase inhibitors reveal a difference in signalling between interleukin3 and granulocyte- macrophage colony stimulating factor
    • Scheid MP, Lauener RW, Duronio V. Role of phosphatidylinositol 3-OH-kinase activity in the inhibition of apoptosis in haemopoietic cells: Phosphatidylinositol 3-OH-kinase inhibitors reveal a difference in signalling between interleukin3 and granulocyte-macrophage colony stimulating factor. Biochem J 1995; 312: 159.
    • (1995) Biochem J , vol.312 , pp. 159
    • Scheid, M.P.1    Lauener, R.W.2    Duronio, V.3
  • 5
    • 0034469271 scopus 로고    scopus 로고
    • Regulation of neutrophil apoptosis: A role for protein kinase C and phosphatidylinositol-3-kinase
    • Webb PR, Wang, KQ, Scheel-Toellner D, Pongracz J, Salmon M, Lord JM. Regulation of neutrophil apoptosis: A role for protein kinase C and phosphatidylinositol-3-kinase. Apoptosis 2000; 5: 451.
    • (2000) Apoptosis , vol.5 , pp. 451
    • Webb, P.R.1    Wang, K.Q.2    Scheel-Toellner, D.3    Pongracz, J.4    Salmon, M.5    Lord, J.M.6
  • 6
    • 0030026693 scopus 로고    scopus 로고
    • Requirement for phosphatidylinositol 3′-kinase to protect hemopoietic progenitors against apoptosis depends upon the extracellular survival factor
    • Minshall C, Arkins S, Freund GG, Kelley KW Requirement for phosphatidylinositol 3′-kinase to protect hemopoietic progenitors against apoptosis depends upon the extracellular survival factor. J Immunol 1996; 156: 939.
    • (1996) J Immunol , vol.156 , pp. 939
    • Minshall, C.1    Arkins, S.2    Freund, G.G.3    Kelley, K.W.4
  • 7
    • 0037017396 scopus 로고    scopus 로고
    • FKHR-L1 can act as a critical effector of cell death induced by cytokine withdrawal: Protein kinase B-enhanced cell survival through maintenance of mitochondnal integrity
    • Dijkers PF, Birkenkamp KU, Lam EW, et al. FKHR-L1 can act as a critical effector of cell death induced by cytokine withdrawal: Protein kinase B-enhanced cell survival through maintenance of mitochondnal integrity. J Cell Biol 2002; 156: 531.
    • (2002) J Cell Biol , vol.156 , pp. 531
    • Dijkers, P.F.1    Birkenkamp, K.U.2    Lam, E.W.3
  • 9
    • 0033119372 scopus 로고    scopus 로고
    • BCL-2 gene family and the regulation of programmed cell death
    • Korsmeyer SJ. BCL-2 gene family and the regulation of programmed cell death. Cancer Res 1999; 59: 1693.
    • (1999) Cancer Res , vol.59 , pp. 1693
    • Korsmeyer, S.J.1
  • 10
    • 0035957653 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK: A requisite gateway to mitochondrial dysfunction and death
    • Wei MC, Zong WX, Cheng EH, et al. Proapoptotic BAX and BAK: A requisite gateway to mitochondrial dysfunction and death. Science 2001; 292: 727.
    • (2001) Science , vol.292 , pp. 727
    • Wei, M.C.1    Zong, W.X.2    Cheng, E.H.3
  • 11
    • 0035876483 scopus 로고    scopus 로고
    • BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak
    • Zong, WX, Lindsten T, Ross AJ, MacGregor GR, Thompson CB. BH3-only proteins that bind pro-survival Bcl-2 family members fail to induce apoptosis in the absence of Bax and Bak. Genes & Development 2001; 15: 1481.
    • (2001) Genes & Development , vol.15 , pp. 1481
    • Zong, W.X.1    Lindsten, T.2    Ross, A.J.3    MacGregor, G.R.4    Thompson, C.B.5
  • 12
    • 0033635733 scopus 로고    scopus 로고
    • BH3-Only proteins - Essential initiators of apoptotic cell death
    • Huang DCS, Strasser A. BH3-Only proteins - Essential initiators of apoptotic cell death. Cell 2000; 103: 839.
    • (2000) Cell , vol.103 , pp. 839
    • Huang, D.C.S.1    Strasser, A.2
  • 13
    • 0030584088 scopus 로고    scopus 로고
    • Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)
    • Zha J, Harada H, Yang E, Jockel J, Korsmeyer SJ. Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L). Cell 1996; 87: 619.
    • (1996) Cell , vol.87 , pp. 619
    • Zha, J.1    Harada, H.2    Yang, E.3    Jockel, J.4    Korsmeyer, S.J.5
  • 14
    • 1842333237 scopus 로고    scopus 로고
    • Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt
    • del Peso L, Gonzalez-Garcia M, Page C, Herrera R, Nunez G. Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt. Science 1997; 278: 687.
    • (1997) Science , vol.278 , pp. 687
    • Del Peso, L.1    Gonzalez-Garcia, M.2    Page, C.3    Herrera, R.4    Nunez, G.5
  • 15
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • Datta SR, Dudek H, Tao X, et al. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell 1997; 91: 231.
    • (1997) Cell , vol.91 , pp. 231
    • Datta, S.R.1    Dudek, H.2    Tao, X.3
  • 16
    • 0032543578 scopus 로고    scopus 로고
    • The kit receptor promotes cell survival via activation of PI 3-kinase and subsequent Akt-mediated phosphorylation of Bad on Ser136
    • Blume-Jensen P, Janknecht R, Hunter T. The kit receptor promotes cell survival via activation of PI 3-kinase and subsequent Akt-mediated phosphorylation of Bad on Ser136. Curr Biol 1998; 8: 779.
    • (1998) Curr Biol , vol.8 , pp. 779
    • Blume-Jensen, P.1    Janknecht, R.2    Hunter, T.3
  • 18
    • 0033581927 scopus 로고    scopus 로고
    • Regulation of BAD phosphorylation at serine 112 by the Ras-mitogen-activated protein kinase pathway
    • Fang XJ, Yu SX, Eder A, et al. Regulation of BAD phosphorylation at serine 112 by the Ras-mitogen-activated protein kinase pathway. Oncogens 1999; 18: 6635.
    • (1999) Oncogens , vol.18 , pp. 6635
    • Fang, X.J.1    Yu, S.X.2    Eder, A.3
  • 20
    • 0032698075 scopus 로고    scopus 로고
    • Cell survival promoted by the Ras-MAPK signaling pathway by transcription-dependent and -independent mechanisms
    • Bonni A, Brunet A., West AE, Datta SR, Takasu MA, Greenberg ME. Cell survival promoted by the Ras-MAPK signaling pathway by transcription-dependent and -independent mechanisms. Science 1999; 286: 1358.
    • (1999) Science , vol.286 , pp. 1358
    • Bonni, A.1    Brunet, A.2    West, A.E.3    Datta, S.R.4    Takasu, M.A.5    Greenberg, M.E.6
  • 21
    • 0034711239 scopus 로고    scopus 로고
    • Protein kinase C theta and epsilon promote T-cell survival by a rsk-dependent phosphorylation and mactivation of BAD
    • Bertolotto C, Maulon L, Filippa N, Baier G, Auberger P. Protein kinase C theta and epsilon promote T-cell survival by a rsk-dependent phosphorylation and mactivation of BAD. J Biol Chem 2000; 275: 37246.
    • (2000) J Biol Chem , vol.275 , pp. 37246
    • Bertolotto, C.1    Maulon, L.2    Filippa, N.3    Baier, G.4    Auberger, P.5
  • 22
    • 0033635235 scopus 로고    scopus 로고
    • 14-3-3 Proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation
    • Datta SR, Katsov A, Hu L, et al. 14-3-3 proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation. Mol Cell 2000; 6: 41.
    • (2000) Mol Cell , vol.6 , pp. 41
    • Datta, S.R.1    Katsov, A.2    Hu, L.3
  • 23
    • 0035206813 scopus 로고    scopus 로고
    • 14-3-3 Inhibits Bad-induced cell death through interaction with serine-136
    • Masters SC, Yang H, Datta SR, Greenberg ME, Fu H. 14-3-3 inhibits Bad-induced cell death through interaction with serine-136. Mol Pharmacol 2001; 60: 1325.
    • (2001) Mol Pharmacol , vol.60 , pp. 1325
    • Masters, S.C.1    Yang, H.2    Datta, S.R.3    Greenberg, M.E.4    Fu, H.5
  • 24
    • 0034682812 scopus 로고    scopus 로고
    • BAD ser-155 phosphorylation regulates BAD/Bcl-XL interaction and cell survival
    • Tan Y, Demeter MR, Ruan H, Comb MJ. BAD ser-155 phosphorylation regulates BAD/Bcl-XL interaction and cell survival. J Biol Chem 2000; 275: 25865.
    • (2000) J Biol Chem , vol.275 , pp. 25865
    • Tan, Y.1    Demeter, M.R.2    Ruan, H.3    Comb, M.J.4
  • 25
    • 0034637606 scopus 로고    scopus 로고
    • Growth factors inactivate the cell death promoter BAD by phosphorylation of its BH3 domain on Ser(155)
    • Zhou XM, Liu YM, Payne G, Lutz RJ, Chittenden T. Growth factors inactivate the cell death promoter BAD by phosphorylation of its BH3 domain on Ser(155). J Biol Chem 2000; 275: 25046.
    • (2000) J Biol Chem , vol.275 , pp. 25046
    • Zhou, X.M.1    Liu, Y.M.2    Payne, G.3    Lutz, R.J.4    Chittenden, T.5
  • 26
    • 0034661857 scopus 로고    scopus 로고
    • Regulation of BAD by cAMP-dependent protein kinase is mediated via phosphorylation of a novel site, Ser(155)
    • Lizcano JM, Morrice N, Cohen P. Regulation of BAD by cAMP-dependent protein kinase is mediated via phosphorylation of a novel site, Ser(155). Biochem J 2000; 349: 547.
    • (2000) Biochem J , vol.349 , pp. 547
    • Lizcano, J.M.1    Morrice, N.2    Cohen, P.3
  • 27
    • 0036660617 scopus 로고    scopus 로고
    • Phenylephrine promotes phosphorylation of Bad in cardiac myocytes through the extracellular signal-regulated kinases 1/2 and protein kinase A
    • Valks DM, Cook SA, Pham FH, Morrison PR, Clerk A, Sugden PH. Phenylephrine promotes phosphorylation of Bad in cardiac myocytes through the extracellular signal-regulated kinases 1/2 and protein kinase A. J Mol Cell Cardiol 2002; 34: 749.
    • (2002) J Mol Cell Cardiol , vol.34 , pp. 749
    • Valks, D.M.1    Cook, S.A.2    Pham, F.H.3    Morrison, P.R.4    Clerk, A.5    Sugden, P.H.6
  • 28
    • 0034699352 scopus 로고    scopus 로고
    • Phosphorylation of the pro-apoptotic protein BAD on serine 155, a novel site, contributes to cell survival (vol. 10, p. 1151, 2000)
    • Virdee K, Parone PA, Tolkovsky AM. Phosphorylation of the pro-apoptotic protein BAD on serine 155, a novel site, contributes to cell survival (vol. 10, p. 1151, 2000). Curr Biol 2000; 10: 1151.
    • (2000) Curr Biol , vol.10 , pp. 1151
    • Virdee, K.1    Parone, P.A.2    Tolkovsky, A.M.3
  • 29
    • 0034699352 scopus 로고    scopus 로고
    • Phosphorylation of the pro-apoptotic protein BAD on serine 155, a novel site, contributes to cell survival
    • Virdee K, Parone PA, Tolkovsky AM. Phosphorylation of the pro-apoptotic protein BAD on serine 155, a novel site, contributes to cell survival. Curr Biol 2000; 10: 1151.
    • (2000) Curr Biol , vol.10 , pp. 1151
    • Virdee, K.1    Parone, P.A.2    Tolkovsky, A.M.3
  • 30
    • 0032750817 scopus 로고    scopus 로고
    • Hepatocyte growth factor promotes renal epithelial cell survival by dual mechanisms
    • Liu Y. Hepatocyte growth factor promotes renal epithelial cell survival by dual mechanisms. Am J Physiol 1999; 277: F624.
    • (1999) Am J Physiol , vol.277
    • Liu, Y.1
  • 31
    • 0032506514 scopus 로고    scopus 로고
    • Calcium promotes cell survival through CaM-K kinase activation of the protein-kinase-B pathway
    • Yano S, Tokumitsu H, Soderling TR. Calcium promotes cell survival through CaM-K kinase activation of the protein-kinase-B pathway. Nature 1998; 396: 584.
    • (1998) Nature , vol.396 , pp. 584
    • Yano, S.1    Tokumitsu, H.2    Soderling, T.R.3
  • 32
    • 3142691373 scopus 로고    scopus 로고
    • Interleukin-7 inactivates the pro-apoptotic protein Bad promoting T cell survival
    • Li WQ, Jiang Q, Khaled AR, Keller JR, Durum SK. Interleukin-7 inactivates the pro-apoptotic protein Bad promoting T cell survival. J Biol Chem 2004; 279: 29160.
    • (2004) J Biol Chem , vol.279 , pp. 29160
    • Li, W.Q.1    Jiang, Q.2    Khaled, A.R.3    Keller, J.R.4    Durum, S.K.5
  • 33
    • 0032560514 scopus 로고    scopus 로고
    • Dissociation of cytokine-induced phosphorylation of Bad and activation of PKB/akt: Involvement of MEK upstream of Bad phosphorylation
    • Scheid MP, Duronio V. Dissociation of cytokine-induced phosphorylation of Bad and activation of PKB/akt: Involvement of MEK upstream of Bad phosphorylation. Proc Nat Acad Sci USA 1998; 95: 7439.
    • (1998) Proc Nat Acad Sci USA , vol.95 , pp. 7439
    • Scheid, M.P.1    Duronio, V.2
  • 34
    • 0033964671 scopus 로고    scopus 로고
    • Insulin-mediated stimulation of protein kinase Akt: A potent survival signaling cascade for endothelial cells
    • Hermann C, Assmus B, Urbich C, Zeiher AM, Dimmeler S. Insulin-mediated stimulation of protein kinase Akt: A potent survival signaling cascade for endothelial cells. Arterioscler Thromb Vasc Biol 2000; 20: 402.
    • (2000) Arterioscler Thromb Vasc Biol , vol.20 , pp. 402
    • Hermann, C.1    Assmus, B.2    Urbich, C.3    Zeiher, A.M.4    Dimmeler, S.5
  • 35
    • 0033564734 scopus 로고    scopus 로고
    • Cytokine-induced protein kinase B activation and bad phosphorylation do not correlate with cell survival of hemopoietic cells
    • Hinton HJ, Welham MJ. Cytokine-induced protein kinase B activation and bad phosphorylation do not correlate with cell survival of hemopoietic cells. J Immunol 1999; 162: 7002.
    • (1999) J Immunol , vol.162 , pp. 7002
    • Hinton, H.J.1    Welham, M.J.2
  • 36
    • 18544367200 scopus 로고    scopus 로고
    • Inhibition of phosphorylation of BAD and Raf-1 by Akt sensitizes human ovarian cancer cells to paclitaxel
    • Mabuchi S, Ohmichi M, Kimura A, et al. Inhibition of phosphorylation of BAD and Raf-1 by Akt sensitizes human ovarian cancer cells to paclitaxel. J Biol Chem 2002; 277: 33490.
    • (2002) J Biol Chem , vol.277 , pp. 33490
    • Mabuchi, S.1    Ohmichi, M.2    Kimura, A.3
  • 37
    • 0037031828 scopus 로고    scopus 로고
    • Signal transduction from N-cadherin increases Bcl-2. Regulation of the phosphatidylinositol 3-kinase/Akt pathway by homophilic adhesion and actin cytoskeletal organization
    • Tran NL, Adams DG, Vaillancourt RR, Heimark RL. Signal transduction from N-cadherin increases Bcl-2. Regulation of the phosphatidylinositol 3-kinase/Akt pathway by homophilic adhesion and actin cytoskeletal organization. J Biol Chem 2002; 277: 32905.
    • (2002) J Biol Chem , vol.277 , pp. 32905
    • Tran, N.L.1    Adams, D.G.2    Vaillancourt, R.R.3    Heimark, R.L.4
  • 38
    • 2542428498 scopus 로고    scopus 로고
    • Nicotine induces multi-site phosphorylation of Bad in association with suppression of apoptosis
    • Jin Z, Gao F, Flagg T, Deng X. Nicotine induces multi-site phosphorylation of Bad in association with suppression of apoptosis. J Biol Chem 2004; 279: 23837.
    • (2004) J Biol Chem , vol.279 , pp. 23837
    • Jin, Z.1    Gao, F.2    Flagg, T.3    Deng, X.4
  • 39
    • 0033537768 scopus 로고    scopus 로고
    • 2+-induced apoptosis through calcineurin dephosphorylation of BAD
    • 2+-induced apoptosis through calcineurin dephosphorylation of BAD. Science 1999; 284: 339.
    • (1999) Science , vol.284 , pp. 339
    • Wang, H.G.1    Pathan, N.2    Ethell, I.M.3
  • 40
    • 0342657806 scopus 로고    scopus 로고
    • Protein phosphatase 1alpha is a Ras-activated Bad phosphatase that regulates interleukin-2 deprivation-induced apoptosis
    • Ayllon V, Martinez AC, Garcia A, Cayla X, Rebollo A. Protein phosphatase 1alpha is a Ras-activated Bad phosphatase that regulates interleukin-2 deprivation-induced apoptosis. EMBO J 2000; 19: 2237.
    • (2000) EMBO J , vol.19 , pp. 2237
    • Ayllon, V.1    Martinez, A.C.2    Garcia, A.3    Cayla, X.4    Rebollo, A.5
  • 41
    • 0035283087 scopus 로고    scopus 로고
    • Protein phosphatase 2A activates the proapoptotic function of BAD in interleukin- 3-dependent lymphoid cells by a mechanism requiring 14-3-3 dissociation
    • Chiang CW, Harris G, Ellig C, et al. Protein phosphatase 2A activates the proapoptotic function of BAD in interleukin- 3-dependent lymphoid cells by a mechanism requiring 14-3-3 dissociation. Blood 2001; 97: 1289.
    • (2001) Blood , vol.97 , pp. 1289
    • Chiang, C.W.1    Harris, G.2    Ellig, C.3
  • 42
    • 0031919157 scopus 로고    scopus 로고
    • Regulation of ceramide production and apoptosis
    • Kolesnick RN, Kronke M. Regulation of ceramide production and apoptosis. Ann Rev.0 Physiol 1998; 60: 643.
    • (1998) Ann Rev.0 Physiol , vol.60 , pp. 643
    • Kolesnick, R.N.1    Kronke, M.2
  • 43
    • 0037203342 scopus 로고    scopus 로고
    • Ceramide in apoptosis: An overview and current perspectives
    • Pettus BJ, Chalfant CE, Hannun YA. Ceramide in apoptosis: an overview and current perspectives. Biochim Biophys Acta 2002; 1585: 114.
    • (2002) Biochim Biophys Acta , vol.1585 , pp. 114
    • Pettus, B.J.1    Chalfant, C.E.2    Hannun, Y.A.3
  • 44
    • 0034607914 scopus 로고    scopus 로고
    • Ceramide inhibits protein kinase B/Akt by promoting dephosphorylation of serine 473
    • Schubert KM, Scheid MP, Duronio V. Ceramide inhibits protein kinase B/Akt by promoting dephosphorylation of serine 473. J Biol Chem 2000; 275: 13330.
    • (2000) J Biol Chem , vol.275 , pp. 13330
    • Schubert, K.M.1    Scheid, M.P.2    Duronio, V.3
  • 46
    • 0037354119 scopus 로고    scopus 로고
    • Ceramide-induced neuronal apoptosis is associated with dephosphorylation of Akt, BAD, FKHR, GSK-3beta, and induction of the mitochondrial-dependent intrinsic caspase pathway
    • Stoica BA, Movsesyan VA, Lea PMT, Faden AI. Ceramide-induced neuronal apoptosis is associated with dephosphorylation of Akt, BAD, FKHR, GSK-3beta, and induction of the mitochondrial-dependent intrinsic caspase pathway. Mol Cell Neurosci 2003; 22: 365.
    • (2003) Mol Cell Neurosci , vol.22 , pp. 365
    • Stoica, B.A.1    Movsesyan, V.A.2    Lea, P.M.T.3    Faden, A.I.4
  • 47
    • 0037155283 scopus 로고    scopus 로고
    • Identification of a novel phosphorylation site, Ser-170, as a regulator of bad proapoptotic activity
    • Dramsi S, Scheid MP, Maiti A, et al. Identification of a novel phosphorylation site, Ser-170, as a regulator of bad proapoptotic activity. J Biol Chem 2002; 277: 6399.
    • (2002) J Biol Chem , vol.277 , pp. 6399
    • Dramsi, S.1    Scheid, M.P.2    Maiti, A.3
  • 48
    • 0032496239 scopus 로고    scopus 로고
    • Construction and characterization of a conditionally active version of the serine/threonine kinase Akt
    • Kohn AD, Barthel A, Kovacina KS, et al. Construction and characterization of a conditionally active version of the serine/threonine kinase Akt. J Biol Chem 1998; 273: 11937.
    • (1998) J Biol Chem , vol.273 , pp. 11937
    • Kohn, A.D.1    Barthel, A.2    Kovacina, K.S.3
  • 49
    • 0035654579 scopus 로고    scopus 로고
    • Oxidized low density lipoprotein inhibits macrophage apoptosis through activation of the PI 3-kinase/PKB pathway
    • Hundal RS, Salh BS, Schrader JW, Gomez-Munoz A, Duronio V, Steinbrecher UP. Oxidized low density lipoprotein inhibits macrophage apoptosis through activation of the PI 3-kinase/PKB pathway. J Lipid Res 2001; 42: 1483.
    • (2001) J Lipid Res , vol.42 , pp. 1483
    • Hundal, R.S.1    Salh, B.S.2    Schrader, J.W.3    Gomez-Munoz, A.4    Duronio, V.5    Steinbrecher, U.P.6
  • 50
    • 0026808525 scopus 로고
    • Tyrosme phosphorylation of receptor beta subunits and common substrates in response to interleukin-3 and granulocyte-macrophage colony-stimulating factor
    • Duronio V, Clark-Lewis I, Federsppiel B, Wieler JS, Schrader JW. Tyrosme phosphorylation of receptor beta subunits and common substrates in response to interleukin-3 and granulocyte-macrophage colony-stimulating factor. J Biol Chem 1992; 267: 21856.
    • (1992) J Biol Chem , vol.267 , pp. 21856
    • Duronio, V.1    Clark-Lewis, I.2    Federsppiel, B.3    Wieler, J.S.4    Schrader, J.W.5
  • 51
    • 0028123081 scopus 로고
    • Multiple hemopoietins, with the exception of interleukin-4, induce modification of She and mSos1, but not their translocation
    • Welham MJ, Duronio V, Leslie KB, Bowtell D, Schrader JW. Multiple hemopoietins, with the exception of interleukin-4, induce modification of She and mSos1, but not their translocation. J Biol Chem 1994; 269: 21165.
    • (1994) J Biol Chem , vol.269 , pp. 21165
    • Welham, M.J.1    Duronio, V.2    Leslie, K.B.3    Bowtell, D.4    Schrader, J.W.5
  • 52
    • 0026671246 scopus 로고
    • Multiple hemopoietic growth factors stimulate activation of mitogen-activated protein kinase family members
    • Welham MJ, Duronio V, Sanghera JS, Pelech SL, Schrader JW. Multiple hemopoietic growth factors stimulate activation of mitogen-activated protein kinase family members. J Immunol 1992; 149: 1683.
    • (1992) J Immunol , vol.149 , pp. 1683
    • Welham, M.J.1    Duronio, V.2    Sanghera, J.S.3    Pelech, S.L.4    Schrader, J.W.5
  • 53
    • 0027992342 scopus 로고
    • Multiple cytokines activate phosphatidylinositol 3-kinase in hemopoietic cells. Association of the enzyme with vanous tyrosine-phosphorylated proteins
    • Gold MR, Duronio V, Saxena SP, Schrader JW, Aebersold R. Multiple cytokines activate phosphatidylinositol 3-kinase in hemopoietic cells. Association of the enzyme with vanous tyrosine-phosphorylated proteins. J Biol Chem 1994; 269: 5403.
    • (1994) J Biol Chem , vol.269 , pp. 5403
    • Gold, M.R.1    Duronio, V.2    Saxena, S.P.3    Schrader, J.W.4    Aebersold, R.5
  • 54
    • 0032947828 scopus 로고    scopus 로고
    • Ceramide and cyclic adenosine monophosphate (cAMP) induce cAMP response element binding protein phosphorylation via distinct signaling pathways while having opposite effects on myeloid cell survival
    • Scheid MP, Foltz IN, Young PR, Schrader JW, Duronio V. Ceramide and cyclic adenosine monophosphate (cAMP) induce cAMP response element binding protein phosphorylation via distinct signaling pathways while having opposite effects on myeloid cell survival. Blood 1999; 93: 217.
    • (1999) Blood , vol.93 , pp. 217
    • Scheid, M.P.1    Foltz, I.N.2    Young, P.R.3    Schrader, J.W.4    Duronio, V.5
  • 55
    • 0042090272 scopus 로고    scopus 로고
    • Oxidized low density lipoprotein inhibits macrophage apoptosis by blocking ceramide generation, thereby maintaining protein kinase B activation and Bel-XL levels
    • Hundal RS, Gomez-Munoz A, Kong JY, et al. Oxidized low density lipoprotein inhibits macrophage apoptosis by blocking ceramide generation, thereby maintaining protein kinase B activation and Bel-XL levels. J Biol Chem 2003; 278: 24399.
    • (2003) J Biol Chem , vol.278 , pp. 24399
    • Hundal, R.S.1    Gomez-Munoz, A.2    Kong, J.Y.3
  • 56
    • 0036849192 scopus 로고    scopus 로고
    • Survival factor-mediated BAD phosphorylation raises the mitochondrial threshold for apoptosis
    • Datta SR, Ranger AM, Lin MZ, et al. Survival factor-mediated BAD phosphorylation raises the mitochondrial threshold for apoptosis. Dev Cell 2002; 3: 631.
    • (2002) Dev Cell , vol.3 , pp. 631
    • Datta, S.R.1    Ranger, A.M.2    Lin, M.Z.3
  • 57
    • 0042424706 scopus 로고    scopus 로고
    • Bad-deficient mice develop diffuse large B cell lymphoma
    • Ranger AM, Zha J, Harada H, et al. Bad-deficient mice develop diffuse large B cell lymphoma. Proc Natl Acad Sci USA 2003; 100: 9324.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 9324
    • Ranger, A.M.1    Zha, J.2    Harada, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.