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Volumn 50, Issue 4, 2006, Pages 331-335

Analysis of a bacterial lipopolysaccharide-activated serine kinase that phosphorylates p65/L-plastin in macrophages

Author keywords

Lipopolysaccharide; Macrophage; p65 L plastin; Protein kinase

Indexed keywords

BACTERIUM LIPOPOLYSACCHARIDE; CELL PROTEIN; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; L PLASTIN; N [2 (4 BROMOCINNAMYLAMINO)ETHYL] 5 ISOQUINOLINESULFONAMIDE; PEPTIDE; PHOSPHOTRANSFERASE INHIBITOR; PROTEIN SERINE KINASE; SERINE; SYNAPTOTAGMIN I; UNCLASSIFIED DRUG; BACTERIAL POLYSACCHARIDE; LCP1 PROTEIN, MOUSE; PHOSPHOPROTEIN; PROTEIN SERINE THREONINE KINASE;

EID: 33745124379     PISSN: 03855600     EISSN: 13480421     Source Type: Journal    
DOI: 10.1111/j.1348-0421.2006.tb03801.x     Document Type: Article
Times cited : (7)

References (17)
  • 1
    • 0021564388 scopus 로고
    • The cell biology of macrophage activation
    • Adams, D.O., and Hamilton, T.A. 1984. The cell biology of macrophage activation. Annu. Rev. Immunol. 2: 283-318.
    • (1984) Annu. Rev. Immunol , vol.2 , pp. 283-318
    • Adams, D.O.1    Hamilton, T.A.2
  • 2
    • 3142724031 scopus 로고    scopus 로고
    • Toll-like receptor signaling
    • Akira, S., and Takeda, K. 2004. Toll-like receptor signaling. Nat. Rev. Immunol. 4: 499-511.
    • (2004) Nat. Rev. Immunol , vol.4 , pp. 499-511
    • Akira, S.1    Takeda, K.2
  • 3
    • 0026329843 scopus 로고
    • Design and use of peptide substrates for protein kinases
    • Bruce E.K., and Pearson, R.B. 1991. Design and use of peptide substrates for protein kinases. Methods Enzymol. 200: 121-134.
    • (1991) Methods Enzymol , vol.200 , pp. 121-134
    • Bruce, E.K.1    Pearson, R.B.2
  • 4
    • 0034654533 scopus 로고    scopus 로고
    • Role of mitogen-activated protein kinase cascades in mediating lipopolysaccharide-stimulated induction of cyclooxygenase-2 and IL-1β in RAW264 macrophages
    • Caivano, M., and Cohen, P. 2000. Role of mitogen-activated protein kinase cascades in mediating lipopolysaccharide-stimulated induction of cyclooxygenase-2 and IL-1β in RAW264 macrophages. J. Immunol. 164: 3018-3025.
    • (2000) J. Immunol , vol.164 , pp. 3018-3025
    • Caivano, M.1    Cohen, P.2
  • 6
    • 0018625446 scopus 로고
    • Bacterial endotoxins and host immune responses
    • Morrison, D.C., and Ryan, J.L. 1979. Bacterial endotoxins and host immune responses. Adv. Immunol. 28: 293-450.
    • (1979) Adv. Immunol , vol.28 , pp. 293-450
    • Morrison, D.C.1    Ryan, J.L.2
  • 7
    • 0027318571 scopus 로고    scopus 로고
    • Nakano, M., Saito, S., Nakano, Y., Matsumura, M., and Shinomiya, H. Intracellular protein phosphorylation in murine peritoneal macrophages in response to bacterial lipopolysaccharides: effects of kinase-inhibitors and LPS-tolerance. 1993. Immunobiology 187: 272-282.
    • Nakano, M., Saito, S., Nakano, Y., Matsumura, M., and Shinomiya, H. Intracellular protein phosphorylation in murine peritoneal macrophages in response to bacterial lipopolysaccharides: effects of kinase-inhibitors and LPS-tolerance. 1993. Immunobiology 187: 272-282.
  • 8
    • 0023147156 scopus 로고
    • Secretory products of macrophages
    • Nathan, C.F. 1987. Secretory products of macrophages. J. Clin. Invest. 79: 319-324.
    • (1987) J. Clin. Invest , vol.79 , pp. 319-324
    • Nathan, C.F.1
  • 9
    • 0026355413 scopus 로고
    • Protein kinase phosphorylation site sequences and consensus specificity motifs: Tabulations
    • Pearson, R.B., and Kemp, B.E. 1991. Protein kinase phosphorylation site sequences and consensus specificity motifs: tabulations. Methods Enzymol. 200: 62-81.
    • (1991) Methods Enzymol , vol.200 , pp. 62-81
    • Pearson, R.B.1    Kemp, B.E.2
  • 10
    • 0028933571 scopus 로고
    • Complete primary structure and phosphorylation site of the 65-kDa macrophage protein phosphorylated by stimulation with bacterial lipopolysaccharide
    • Shinomiya, H., Hagi, A., Fukuzumi, M., Mizobuchi, M., Hirata, H., and Utsumi, S. 1995. Complete primary structure and phosphorylation site of the 65-kDa macrophage protein phosphorylated by stimulation with bacterial lipopolysaccharide. J. Immunol. 154: 3471-3478.
    • (1995) J. Immunol , vol.154 , pp. 3471-3478
    • Shinomiya, H.1    Hagi, A.2    Fukuzumi, M.3    Mizobuchi, M.4    Hirata, H.5    Utsumi, S.6
  • 11
    • 0025909326 scopus 로고
    • Purification and characterization of the 65-kDa protein phosphorylated in murine macrophages by stimulation with bacterial lipopolysaccharide
    • Shinomiya, H., Hirata, H., and Nakano, M. 1991. Purification and characterization of the 65-kDa protein phosphorylated in murine macrophages by stimulation with bacterial lipopolysaccharide. J. Immunol. 146: 3617-3626.
    • (1991) J. Immunol , vol.146 , pp. 3617-3626
    • Shinomiya, H.1    Hirata, H.2    Nakano, M.3
  • 12
    • 0028030747 scopus 로고
    • Identification of the 65-kDa phosphoprotein in murine macrophages as a novel protein: Homology with human L-plastin
    • Shinomiya, H., Hirata, H., Saito, S., Yagisawa, H., and Nakano, M. 1994. Identification of the 65-kDa phosphoprotein in murine macrophages as a novel protein: homology with human L-plastin. Biochem. Biophys. Res. Commun. 202: 1631-1639.
    • (1994) Biochem. Biophys. Res. Commun , vol.202 , pp. 1631-1639
    • Shinomiya, H.1    Hirata, H.2    Saito, S.3    Yagisawa, H.4    Nakano, M.5
  • 13
    • 33847164213 scopus 로고    scopus 로고
    • Detection of the activities of multiple protein kinases in LPS-stimulated macrophages by renaturation
    • Shinomiya, H., Murakami, O., Nakano, M., and Utsumi, S. 2001. Detection of the activities of multiple protein kinases in LPS-stimulated macrophages by renaturation. J. Clin. Exp. Hematopathol. 41: 115-118.
    • (2001) J. Clin. Exp. Hematopathol , vol.41 , pp. 115-118
    • Shinomiya, H.1    Murakami, O.2    Nakano, M.3    Utsumi, S.4
  • 14
    • 0025907984 scopus 로고
    • Regulation by phosphorylation of reversible association of a myristoylated protein kinase C substrate with the plasma membrane
    • Thelen, M., Rosen, A., Nairn, A.C., and Aderem, A. 1991. Regulation by phosphorylation of reversible association of a myristoylated protein kinase C substrate with the plasma membrane. Nature 351: 320-323.
    • (1991) Nature , vol.351 , pp. 320-323
    • Thelen, M.1    Rosen, A.2    Nairn, A.C.3    Aderem, A.4
  • 15
    • 0023829270 scopus 로고
    • Endotoxaemia: An early predictor of septicaemia in febrile patients
    • van Deventer, S.J.H., Buller, H.R., ten Cate, A., Sturk, J.W., and Pau, W. 1988. Endotoxaemia: an early predictor of septicaemia in febrile patients. Lancet 1: 605-608.
    • (1988) Lancet , vol.1 , pp. 605-608
    • van Deventer, S.J.H.1    Buller, H.R.2    ten Cate, A.3    Sturk, J.W.4    Pau, W.5
  • 16
    • 0022647023 scopus 로고
    • LPS induces altered phosphate labeling of proteins in murine peritoneal macrophages
    • Weiel, J.E., Hamilton, T.A., and Adams, D.O. 1986. LPS induces altered phosphate labeling of proteins in murine peritoneal macrophages. J. Immunol. 136: 3012-3018.
    • (1986) J. Immunol , vol.136 , pp. 3012-3018
    • Weiel, J.E.1    Hamilton, T.A.2    Adams, D.O.3
  • 17
    • 0026659881 scopus 로고
    • Bacterial lipopolysaccharide induces tyrosine phosphorylation and activation of mitogen-activated protein kinases in macrophages
    • Weinstein, S.L., Sanghera, J.S., Lemke, K., DeFranco, A.L., and Pelech, S.L. 1992. Bacterial lipopolysaccharide induces tyrosine phosphorylation and activation of mitogen-activated protein kinases in macrophages. J. Biol. Chem. 267: 14955-14961.
    • (1992) J. Biol. Chem , vol.267 , pp. 14955-14961
    • Weinstein, S.L.1    Sanghera, J.S.2    Lemke, K.3    DeFranco, A.L.4    Pelech, S.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.