메뉴 건너뛰기




Volumn 179, Issue 7, 2007, Pages 4480-4491

Surfactant protein A activation of atypical protein kinase C ζ in IκB-α-dependent anti-inflammatory immune regulation

Author keywords

[No Author keywords available]

Indexed keywords

I KAPPA B ALPHA; I KAPPA B BETA; LIPOPOLYSACCHARIDE; PROTEIN KINASE C ZETA; SURFACTANT PROTEIN A; TUMOR NECROSIS FACTOR ALPHA;

EID: 48749088893     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.179.7.4480     Document Type: Article
Times cited : (26)

References (61)
  • 1
    • 0036199682 scopus 로고    scopus 로고
    • The pulmonary collectins, SP-A and SP-D, orchestrate innate immunity in the lung
    • McCormack, F. X., and J. A. Whitsett. 2002. The pulmonary collectins, SP-A and SP-D, orchestrate innate immunity in the lung. J. Clin. Invest. 109: 707-712.
    • (2002) J. Clin. Invest , vol.109 , pp. 707-712
    • McCormack, F.X.1    Whitsett, J.A.2
  • 2
    • 11244287371 scopus 로고    scopus 로고
    • Immunoregulatory functions of surfactant proteins
    • Wright, J. R. 2005. Immunoregulatory functions of surfactant proteins. Nat. Rev. Immunol. 5: 58-68.
    • (2005) Nat. Rev. Immunol , vol.5 , pp. 58-68
    • Wright, J.R.1
  • 3
    • 0036008385 scopus 로고    scopus 로고
    • Distinct roles for lung collectins in pulmonary host defense
    • Shepherd, V. L. 2002. Distinct roles for lung collectins in pulmonary host defense. Am. J. Respir. Cell Mol. Biol. 26: 257-260.
    • (2002) Am. J. Respir. Cell Mol. Biol , vol.26 , pp. 257-260
    • Shepherd, V.L.1
  • 4
    • 0035094928 scopus 로고    scopus 로고
    • Pulmonary collectins and innate host defense of the lung
    • Levine, A. M., and J. A. Whitsett. 2001. Pulmonary collectins and innate host defense of the lung. Microbes Infect. 3: 161-166.
    • (2001) Microbes Infect , vol.3 , pp. 161-166
    • Levine, A.M.1    Whitsett, J.A.2
  • 5
    • 0034090641 scopus 로고    scopus 로고
    • Surfactant-associated protein A inhibits LPS-induced cytokine and nitric oxide production in vivo
    • Borron, P., J. C. McIntosh, T. R. Korfhagen, J. A. Whitsett, J. Taylor, and J. R. Wright. 2000. Surfactant-associated protein A inhibits LPS-induced cytokine and nitric oxide production in vivo. Am. J. Physiol. 278: L840-L847.
    • (2000) Am. J. Physiol , vol.278
    • Borron, P.1    McIntosh, J.C.2    Korfhagen, T.R.3    Whitsett, J.A.4    Taylor, J.5    Wright, J.R.6
  • 6
    • 0035989383 scopus 로고    scopus 로고
    • Activation of second messenger pathways in alveolar macrophages by endotoxin
    • Monick, M. M., and G. W. Hunninghake. 2002. Activation of second messenger pathways in alveolar macrophages by endotoxin. Eur. Respir. J. 20: 210-222.
    • (2002) Eur. Respir. J , vol.20 , pp. 210-222
    • Monick, M.M.1    Hunninghake, G.W.2
  • 8
    • 4644252704 scopus 로고    scopus 로고
    • The acute respiratory distress syndrome
    • Piantadosi, C. A., and D. A. Schwartz. 2004. The acute respiratory distress syndrome. Ann. Intern. Med. 141: 460-470.
    • (2004) Ann. Intern. Med , vol.141 , pp. 460-470
    • Piantadosi, C.A.1    Schwartz, D.A.2
  • 10
    • 0033532629 scopus 로고    scopus 로고
    • MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4
    • Shimazu, R., S. Akashi, H. Ogata, Y. Nagai, K. Fukudome, K. Miyake, and M. Kimoto. 1999. MD-2, a molecule that confers lipopolysaccharide responsiveness on Toll-like receptor 4. J. Exp. Med. 189: 1777-1782.
    • (1999) J. Exp. Med , vol.189 , pp. 1777-1782
    • Shimazu, R.1    Akashi, S.2    Ogata, H.3    Nagai, Y.4    Fukudome, K.5    Miyake, K.6    Kimoto, M.7
  • 11
    • 3142724031 scopus 로고    scopus 로고
    • Toll-like receptor signalling
    • Akira, S., and K. Takeda. 2004. Toll-like receptor signalling. Nat. Rev. Immunol. 4: 499-511.
    • (2004) Nat. Rev. Immunol , vol.4 , pp. 499-511
    • Akira, S.1    Takeda, K.2
  • 12
    • 0034647693 scopus 로고    scopus 로고
    • Signal-dependent and -independent degradation of free and NF-κB-bound IκBα
    • Pando, M. P., and I. M. Verma. 2000. Signal-dependent and -independent degradation of free and NF-κB-bound IκBα. J. Biol. Chem. 275: 21278-21286.
    • (2000) J. Biol. Chem , vol.275 , pp. 21278-21286
    • Pando, M.P.1    Verma, I.M.2
  • 13
    • 26944443968 scopus 로고    scopus 로고
    • Distinct roles of IκB proteins in regulating constitutive NF-κB activity
    • Tergaonkar, V., R. G. Correa, M. Ikawa, and I. M. Verma. 2005. Distinct roles of IκB proteins in regulating constitutive NF-κB activity. Nat. Cell Biol. 7: 921-923.
    • (2005) Nat. Cell Biol , vol.7 , pp. 921-923
    • Tergaonkar, V.1    Correa, R.G.2    Ikawa, M.3    Verma, I.M.4
  • 14
    • 0028986075 scopus 로고
    • Control of IκB-α proteolysis by site-specific, signal-induced phosphorylation
    • Brown, K., S. Gerstberger, L. Carlson, G. Franzoso, and U. Siebenlist. 1995. Control of IκB-α proteolysis by site-specific, signal-induced phosphorylation. Science 267: 1485-1488.
    • (1995) Science , vol.267 , pp. 1485-1488
    • Brown, K.1    Gerstberger, S.2    Carlson, L.3    Franzoso, G.4    Siebenlist, U.5
  • 15
    • 0036234459 scopus 로고    scopus 로고
    • Missing pieces in the NF-κB puzzle
    • Ghosh, S., and M. Karin. 2002. Missing pieces in the NF-κB puzzle. Cell 109 (Suppl. 1): S81-S96.
    • (2002) Cell , vol.109 , Issue.SUPPL. 1
    • Ghosh, S.1    Karin, M.2
  • 16
    • 0027462682 scopus 로고
    • Mutual regulation of the transcriptional activator NF-κB and its inhibitor, IκB-α
    • Brown, K., S. Park, T. Kanno, G. Franzoso, and U. Siebenlist. 1993. Mutual regulation of the transcriptional activator NF-κB and its inhibitor, IκB-α. Proc. Natl. Acad. Sci. USA 90: 2532-2536.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2532-2536
    • Brown, K.1    Park, S.2    Kanno, T.3    Franzoso, G.4    Siebenlist, U.5
  • 17
    • 2342522110 scopus 로고    scopus 로고
    • Shaping the nuclear action of NF-κB
    • Chen, L. F., and W. C. Greene. 2004. Shaping the nuclear action of NF-κB. Nat. Rev. Mol. Cell Biol. 5: 392-401.
    • (2004) Nat. Rev. Mol. Cell Biol , vol.5 , pp. 392-401
    • Chen, L.F.1    Greene, W.C.2
  • 18
    • 0029793838 scopus 로고    scopus 로고
    • Surfactant protein A protects growing cells and reduces TNF-α activity from LPS-stimulated macrophages
    • McIntosh, J. C., S. Mervin-Blake, E. Conner, and J. R. Wright. 1996. Surfactant protein A protects growing cells and reduces TNF-α activity from LPS-stimulated macrophages. Am. J. Physiol. 271: L310-L319.
    • (1996) Am. J. Physiol , vol.271
    • McIntosh, J.C.1    Mervin-Blake, S.2    Conner, E.3    Wright, J.R.4
  • 19
    • 0033168699 scopus 로고    scopus 로고
    • Pulmonary surfactant protein A modulates the cellular response to smooth and rough lipopolysaccharides by interaction with CD14
    • Sano, H., H. Sohma, T. Muta, S. Nomura, D. R. Voelker, and Y. Kuroki. 1999. Pulmonary surfactant protein A modulates the cellular response to smooth and rough lipopolysaccharides by interaction with CD14. J. Immunol. 163: 387-395.
    • (1999) J. Immunol , vol.163 , pp. 387-395
    • Sano, H.1    Sohma, H.2    Muta, T.3    Nomura, S.4    Voelker, D.R.5    Kuroki, Y.6
  • 20
    • 0141918823 scopus 로고    scopus 로고
    • By binding SIRPα or calreticulin/CD91, lung collectins act as dual function surveillance molecules to suppress or enhance inflammation
    • Gardai, S. J., Y. Q. Xiao, M. Dickinson, J. A. Nick, D. R. Voelker, K. E. Greene, and P. M. Henson. 2003. By binding SIRPα or calreticulin/CD91, lung collectins act as dual function surveillance molecules to suppress or enhance inflammation. Cell 115: 13-23.
    • (2003) Cell , vol.115 , pp. 13-23
    • Gardai, S.J.1    Xiao, Y.Q.2    Dickinson, M.3    Nick, J.A.4    Voelker, D.R.5    Greene, K.E.6    Henson, P.M.7
  • 21
    • 26844480960 scopus 로고    scopus 로고
    • Interaction of SP-A (surfactant protein A) with bacterial rough lipopolysaccharide (Re-LPS), and effects of SP-A on the binding of Re-LPS to CD14 and LPS-binding protein
    • Garcia-Verdugo, I., F. Sanchez-Barbero, K. Soldau, P. S. Tobias, and C. Casals. 2005. Interaction of SP-A (surfactant protein A) with bacterial rough lipopolysaccharide (Re-LPS), and effects of SP-A on the binding of Re-LPS to CD14 and LPS-binding protein. Biochem. J. 391: 115-124.
    • (2005) Biochem. J , vol.391 , pp. 115-124
    • Garcia-Verdugo, I.1    Sanchez-Barbero, F.2    Soldau, K.3    Tobias, P.S.4    Casals, C.5
  • 22
    • 0034535756 scopus 로고    scopus 로고
    • Surfactant protein A differentially regulates IFN-γ- and LPS-induced nitrite production by rat alveolar macrophages
    • Stamme, C., E. Walsh, and J. R. Wright. 2000. Surfactant protein A differentially regulates IFN-γ- and LPS-induced nitrite production by rat alveolar macrophages. Am. J. Respir. Cell Mol. Biol. 23: 772-779.
    • (2000) Am. J. Respir. Cell Mol. Biol , vol.23 , pp. 772-779
    • Stamme, C.1    Walsh, E.2    Wright, J.R.3
  • 23
    • 0346727497 scopus 로고    scopus 로고
    • Surfactant protein A inhibits alveolar macrophage cytokine production by CD14-independent pathway
    • Alcorn, J. F., and J. R. Wright. 2004. Surfactant protein A inhibits alveolar macrophage cytokine production by CD14-independent pathway. Am. J. Physiol. 286: L129-L136.
    • (2004) Am. J. Physiol , vol.286
    • Alcorn, J.F.1    Wright, J.R.2
  • 24
    • 9744232082 scopus 로고    scopus 로고
    • Accumulation of inhibitory κB-α as a mechanism contributing to the anti-inflammatory effects of surfactant protein-A
    • Wu, Y., S. Adam, L. Hamann, H. Heine, A. J. Ulmer, U. Buwitt-Beckmann, and C. Stamme. 2004. Accumulation of inhibitory κB-α as a mechanism contributing to the anti-inflammatory effects of surfactant protein-A. Am. J. Respir. Cell Mol. Biol. 31: 587-594.
    • (2004) Am. J. Respir. Cell Mol. Biol , vol.31 , pp. 587-594
    • Wu, Y.1    Adam, S.2    Hamann, L.3    Heine, H.4    Ulmer, A.J.5    Buwitt-Beckmann, U.6    Stamme, C.7
  • 25
    • 2442689142 scopus 로고    scopus 로고
    • Pulmonary surfactant protein A inhibits macrophage reactive oxygen intermediate production in response to stimuli by reducing NADPH oxidase activity
    • Crowther, J. E., V. K. Kutala, P. Kuppusamy, J. S. Ferguson, A. A. Beharka, J. L. Zweier, F. X. McCormack, and L. S. Schlesinger. 2004. Pulmonary surfactant protein A inhibits macrophage reactive oxygen intermediate production in response to stimuli by reducing NADPH oxidase activity. J. Immunol. 172: 6866-6874.
    • (2004) J. Immunol , vol.172 , pp. 6866-6874
    • Crowther, J.E.1    Kutala, V.K.2    Kuppusamy, P.3    Ferguson, J.S.4    Beharka, A.A.5    Zweier, J.L.6    McCormack, F.X.7    Schlesinger, L.S.8
  • 26
    • 0032797912 scopus 로고    scopus 로고
    • Regulation of protein phosphorylation and pathogen phagocytosis by surfactant protein A
    • Schagat, T. L., M. J. Tino, and J. R. Wright. 1999. Regulation of protein phosphorylation and pathogen phagocytosis by surfactant protein A. Infect. Immun. 67: 4693-4699.
    • (1999) Infect. Immun , vol.67 , pp. 4693-4699
    • Schagat, T.L.1    Tino, M.J.2    Wright, J.R.3
  • 27
    • 0034646558 scopus 로고    scopus 로고
    • PKC-ζ- associated CK2 participates in the turnover of free IκBα
    • Bren, G. D., K. N. Pennington, and C. V. Paya. 2000. PKC-ζ- associated CK2 participates in the turnover of free IκBα. J. Mol. Biol. 297: 1245-1258.
    • (2000) J. Mol. Biol , vol.297 , pp. 1245-1258
    • Bren, G.D.1    Pennington, K.N.2    Paya, C.V.3
  • 28
    • 0034328882 scopus 로고    scopus 로고
    • The atypical protein kinase Cs: Functional specificity mediated by specific protein adapters
    • 1: 399-403
    • Moscat, J., and M. T. Diaz-Meco. 2000. The atypical protein kinase Cs: functional specificity mediated by specific protein adapters. EMBO Rep. 1: 399-403.
    • (2000) EMBO Rep
    • Moscat, J.1    Diaz-Meco, M.T.2
  • 29
    • 0347986633 scopus 로고    scopus 로고
    • Emerging and diverse roles of protein kinase C in immune cell signalling
    • Tan, S. L., and P. J. Parker. 2003. Emerging and diverse roles of protein kinase C in immune cell signalling. Biochem. J. 376: 545-552.
    • (2003) Biochem. J , vol.376 , pp. 545-552
    • Tan, S.L.1    Parker, P.J.2
  • 30
    • 0642376906 scopus 로고    scopus 로고
    • Protein kinase Cζ (PKCζ): Activation mechanisms and cellular functions
    • Hirai, T., and K. Chida. 2003. Protein kinase Cζ (PKCζ): activation mechanisms and cellular functions. J. Biochem. 133: 1-7.
    • (2003) J. Biochem , vol.133 , pp. 1-7
    • Hirai, T.1    Chida, K.2
  • 31
    • 1542284650 scopus 로고    scopus 로고
    • Molecular mechanisms regulating protein kinase Cζ turnover and cellular transformation
    • Le Good, J. A., and D. N. Brindley. 2004. Molecular mechanisms regulating protein kinase Cζ turnover and cellular transformation. Biochem. J. 378: 83-92.
    • (2004) Biochem. J , vol.378 , pp. 83-92
    • Le Good, J.A.1    Brindley, D.N.2
  • 32
    • 0032555927 scopus 로고    scopus 로고
    • Functional redundancy of the nuclear factor κB inhibitors IκBα and IκBβ
    • Cheng, J. D., R. P. Ryseck, R. M. Attar, D. Dambach, and R. Bravo. 1998. Functional redundancy of the nuclear factor κB inhibitors IκBα and IκBβ. J. Exp. Med. 188: 1055-1062.
    • (1998) J. Exp. Med , vol.188 , pp. 1055-1062
    • Cheng, J.D.1    Ryseck, R.P.2    Attar, R.M.3    Dambach, D.4    Bravo, R.5
  • 34
    • 33750844227 scopus 로고    scopus 로고
    • Expression of the atypical protein kinase C (aPKC) isoforms ι/γ and ζ during mouse embryogenesis
    • Kovac, J., H. Oster, and M. Leitges. 2007. Expression of the atypical protein kinase C (aPKC) isoforms ι/γ and ζ during mouse embryogenesis. Gene Expr. Patterns 7: 187-196.
    • (2007) Gene Expr. Patterns , vol.7 , pp. 187-196
    • Kovac, J.1    Oster, H.2    Leitges, M.3
  • 36
    • 0028971291 scopus 로고
    • Constitutive NF-κB activation, enhanced granulopoiesis, and neonatal lethality in IκBα-deficient mice
    • Beg, A. A., W. C. Sha, R. T. Bronson, and D. Baltimore. 1995. Constitutive NF-κB activation, enhanced granulopoiesis, and neonatal lethality in IκBα-deficient mice. Genes Dev. 9: 2736-2746.
    • (1995) Genes Dev , vol.9 , pp. 2736-2746
    • Beg, A.A.1    Sha, W.C.2    Bronson, R.T.3    Baltimore, D.4
  • 37
    • 85047689695 scopus 로고    scopus 로고
    • IκBα and IκBβ possess injury context-specific functions that uniquely influence hepatic NF-κB induction and inflammation
    • Fan, C., Q. Li, Y. Zhang, X. Liu, M. Luo, D. Abbott, W. Zhou, and J. F. Engelhardt. 2004. IκBα and IκBβ possess injury context-specific functions that uniquely influence hepatic NF-κB induction and inflammation. J. Clin. Invest. 113: 746-755.
    • (2004) J. Clin. Invest , vol.113 , pp. 746-755
    • Fan, C.1    Li, Q.2    Zhang, Y.3    Liu, X.4    Luo, M.5    Abbott, D.6    Zhou, W.7    Engelhardt, J.F.8
  • 38
    • 23444458595 scopus 로고    scopus 로고
    • Pulmonary surfactant protein A activates a phosphatidylinositol 3-kinase/calcium signal transduction pathway in human macrophages: Participation in the up-regulation of mannose receptor activity
    • Beharka, A. A., J. E. Crowther, F. X. McCormack, G. M. Denning, J. Lees, E. Tibesar, and L. S. Schlesinger. 2005. Pulmonary surfactant protein A activates a phosphatidylinositol 3-kinase/calcium signal transduction pathway in human macrophages: participation in the up-regulation of mannose receptor activity. J. Immunol. 175: 2227-2236.
    • (2005) J. Immunol , vol.175 , pp. 2227-2236
    • Beharka, A.A.1    Crowther, J.E.2    McCormack, F.X.3    Denning, G.M.4    Lees, J.5    Tibesar, E.6    Schlesinger, L.S.7
  • 39
    • 0037199972 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase-Akt pathway limits lipopolysaccharide activation of signaling pathways and expression of inflammatory mediators in human monocytic cells
    • Guha, M., and N. Mackman. 2002. The phosphatidylinositol 3-kinase-Akt pathway limits lipopolysaccharide activation of signaling pathways and expression of inflammatory mediators in human monocytic cells. J. Biol. Chem. 277: 32124-32132.
    • (2002) J. Biol. Chem , vol.277 , pp. 32124-32132
    • Guha, M.1    Mackman, N.2
  • 40
    • 0030810216 scopus 로고    scopus 로고
    • Protein kinase C-ζ as a downstream effector of phosphatidylinositol 3-kinase during insulin stimulation in rat adipocytes: Potential role in glucose transport
    • Standaert, M. L., L. Galloway, P. Karnam, G. Bandyopadhyay, J. Moscat, and R. V. Farese. 1997. Protein kinase C-ζ as a downstream effector of phosphatidylinositol 3-kinase during insulin stimulation in rat adipocytes: potential role in glucose transport. J. Biol. Chem. 272: 30075-30082.
    • (1997) J. Biol. Chem , vol.272 , pp. 30075-30082
    • Standaert, M.L.1    Galloway, L.2    Karnam, P.3    Bandyopadhyay, G.4    Moscat, J.5    Farese, R.V.6
  • 41
    • 0032566691 scopus 로고    scopus 로고
    • Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1
    • Le Good, J. A., W. H. Ziegler, D. B. Parekh, D. R. Alessi, P. Cohen, and P. J. Parker. 1998. Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1. Science 281: 2042-2045.
    • (1998) Science , vol.281 , pp. 2042-2045
    • Le Good, J.A.1    Ziegler, W.H.2    Parekh, D.B.3    Alessi, D.R.4    Cohen, P.5    Parker, P.J.6
  • 42
    • 0030985901 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase-dependent activation of protein kinase C-ζ in bacterial lipopolysaccharide-treated human monocytes
    • Herrera-Velit, P., K. L. Knutson, and N. E. Reiner. 1997. Phosphatidylinositol 3-kinase-dependent activation of protein kinase C-ζ in bacterial lipopolysaccharide-treated human monocytes. J. Biol. Chem. 272: 16445-16452.
    • (1997) J. Biol. Chem , vol.272 , pp. 16445-16452
    • Herrera-Velit, P.1    Knutson, K.L.2    Reiner, N.E.3
  • 44
    • 0034651539 scopus 로고    scopus 로고
    • Multiple pathways control protein kinase C phosphorylation
    • Parekh, D. B., W. Ziegler, and P. J. Parker. 2000. Multiple pathways control protein kinase C phosphorylation. EMBO J. 19: 496-503.
    • (2000) EMBO J , vol.19 , pp. 496-503
    • Parekh, D.B.1    Ziegler, W.2    Parker, P.J.3
  • 45
    • 0042525909 scopus 로고    scopus 로고
    • Essential role of RelA Ser311 phosphorylation by ζPKC in NF-κB transcriptional activation
    • Duran, A., M. T. Diaz-Meco, and J. Moscat. 2003. Essential role of RelA Ser311 phosphorylation by ζPKC in NF-κB transcriptional activation. EMBO J. 22: 3910-3918.
    • (2003) EMBO J , vol.22 , pp. 3910-3918
    • Duran, A.1    Diaz-Meco, M.T.2    Moscat, J.3
  • 46
    • 4344652068 scopus 로고    scopus 로고
    • Targeted deletion of protein kinase Creveals a distribution of functions between the two atypical protein kinase C isoforms
    • Soloff, R. S., C. Katayama, M. Y. Lin, J. R. Feramisco, and S. M. Hedrick. 2004. Targeted deletion of protein kinase Creveals a distribution of functions between the two atypical protein kinase C isoforms. J. Immunol. 173: 3250-3260.
    • (2004) J. Immunol , vol.173 , pp. 3250-3260
    • Soloff, R.S.1    Katayama, C.2    Lin, M.Y.3    Feramisco, J.R.4    Hedrick, S.M.5
  • 47
    • 0034698127 scopus 로고    scopus 로고
    • Surfactant proteins A and D bind CD14 by different mechanisms
    • Sano, H., H. Chiba, D. Iwaki, H. Sohma, D. R. Voelker, and Y. Kuroki. 2000. Surfactant proteins A and D bind CD14 by different mechanisms. J. Biol. Chem. 275: 22442-22451.
    • (2000) J. Biol. Chem , vol.275 , pp. 22442-22451
    • Sano, H.1    Chiba, H.2    Iwaki, D.3    Sohma, H.4    Voelker, D.R.5    Kuroki, Y.6
  • 48
    • 0036731527 scopus 로고    scopus 로고
    • Surfactant protein A inhibits lipopolysaccharide-induced immune cell activation by preventing the interaction of lipopolysaccharide with lipopolysaccharide- binding protein
    • Stamme, C., M. Muller, L. Hamann, T. Gutsmann, and U. Seydel. 2002. Surfactant protein A inhibits lipopolysaccharide-induced immune cell activation by preventing the interaction of lipopolysaccharide with lipopolysaccharide- binding protein. Am. J. Respir. Cell Mol. Biol. 27: 353-360.
    • (2002) Am. J. Respir. Cell Mol. Biol , vol.27 , pp. 353-360
    • Stamme, C.1    Muller, M.2    Hamann, L.3    Gutsmann, T.4    Seydel, U.5
  • 49
    • 0029666261 scopus 로고    scopus 로고
    • Characterization of IκB kinases: IκB-α is not phosphorylated by Raf-1 or protein kinase C isozymes, but is a casein kinase II substrate
    • Janosch, P., M. Schellerer, T. Seitz, P. Reim, M. Eulitz, M. Brielmeier, W. Kolch, J. M. Sedivy, and H. Mischak. 1996. Characterization of IκB kinases: IκB-α is not phosphorylated by Raf-1 or protein kinase C isozymes, but is a casein kinase II substrate. J. Biol. Chem. 271: 13868-13874.
    • (1996) J. Biol. Chem , vol.271 , pp. 13868-13874
    • Janosch, P.1    Schellerer, M.2    Seitz, T.3    Reim, P.4    Eulitz, M.5    Brielmeier, M.6    Kolch, W.7    Sedivy, J.M.8    Mischak, H.9
  • 50
    • 0037121923 scopus 로고    scopus 로고
    • PDK1-dependent activation of atypical PKC leads to degradation of the p21 tumor modifier protein
    • Scott, M. T., A. Ingram, and K. L. Ball. 2002. PDK1-dependent activation of atypical PKC leads to degradation of the p21 tumor modifier protein. EMBO J. 21: 6771-6780.
    • (2002) EMBO J , vol.21 , pp. 6771-6780
    • Scott, M.T.1    Ingram, A.2    Ball, K.L.3
  • 52
    • 0033538336 scopus 로고    scopus 로고
    • Inactivation of the inhibitory κB protein kinase/nuclear factor κB pathway by Par-4 expression potentiates tumor necrosis factor α-induced apoptosis
    • Diaz-Meco, M. T., M. J. Lallena, A. Monjas, S. Frutos, and J. Moscat. 1999. Inactivation of the inhibitory κB protein kinase/nuclear factor κB pathway by Par-4 expression potentiates tumor necrosis factor α-induced apoptosis. J. Biol. Chem. 274: 19606-19612.
    • (1999) J. Biol. Chem , vol.274 , pp. 19606-19612
    • Diaz-Meco, M.T.1    Lallena, M.J.2    Monjas, A.3    Frutos, S.4    Moscat, J.5
  • 56
    • 0027535742 scopus 로고
    • Activation of the ζ isozyme of protein kinase C by phosphatidylinositol 3,4,5-trisphosphate
    • Nakanishi, H., K. A. Brewer, and J. H. Exton. 1993. Activation of the ζ isozyme of protein kinase C by phosphatidylinositol 3,4,5-trisphosphate. J. Biol. Chem. 268: 13-16.
    • (1993) J. Biol. Chem , vol.268 , pp. 13-16
    • Nakanishi, H.1    Brewer, K.A.2    Exton, J.H.3
  • 57
    • 0028567280 scopus 로고
    • Phosphatidic acid activation of protein kinase C-ζ overexpressed in COS cells: Comparison with other protein kinase C isotypes and other acidic lipids
    • Limatola, C., D. Schaap, W. H. Moolenaar, and W. J. van Blitterswijk. 1994. Phosphatidic acid activation of protein kinase C-ζ overexpressed in COS cells: comparison with other protein kinase C isotypes and other acidic lipids. Biochem. J. 304: 1001-1008.
    • (1994) Biochem. J , vol.304 , pp. 1001-1008
    • Limatola, C.1    Schaap, D.2    Moolenaar, W.H.3    van Blitterswijk, W.J.4
  • 58
    • 0029003788 scopus 로고
    • PKCζ is a molecular switch in signal transduction of TNF-α, bifunctionally regulated by ceramide and arachidonic acid
    • Muller, G., M. Ayoub, P. Storz, J. Rennecke, D. Fabbro, and K. Pfizenmaier. 1995. PKCζ is a molecular switch in signal transduction of TNF-α, bifunctionally regulated by ceramide and arachidonic acid. EMBO J. 14: 1961-1969.
    • (1995) EMBO J , vol.14 , pp. 1961-1969
    • Muller, G.1    Ayoub, M.2    Storz, P.3    Rennecke, J.4    Fabbro, D.5    Pfizenmaier, K.6
  • 59
    • 0034307664 scopus 로고    scopus 로고
    • Lipopolysaccharide induces jun N-terminal kinase activation in macrophages by a novel Cdc42/Rac-independent pathway involving sequential activation of protein kinase Cζ and phosphatidylcholine- dependent phospholipase C
    • Procyk, K. J., M. R. Rippo, R. Testi, F. Hofmann, P. J. Parker, and M. Baccarini. 2000. Lipopolysaccharide induces jun N-terminal kinase activation in macrophages by a novel Cdc42/Rac-independent pathway involving sequential activation of protein kinase Cζ and phosphatidylcholine- dependent phospholipase C. Blood 96: 2592-2598.
    • (2000) Blood , vol.96 , pp. 2592-2598
    • Procyk, K.J.1    Rippo, M.R.2    Testi, R.3    Hofmann, F.4    Parker, P.J.5    Baccarini, M.6
  • 60
    • 0034057863 scopus 로고    scopus 로고
    • Protein kinase C binding partners
    • Jaken, S., and P. J. Parker. 2000. Protein kinase C binding partners. BioEssays 22: 245-254.
    • (2000) BioEssays , vol.22 , pp. 245-254
    • Jaken, S.1    Parker, P.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.