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Volumn 25, Issue 12, 2011, Pages 4358-4368

AMP-activated protein kinase enhances the phagocytic ability of macrophages and neutrophils

Author keywords

Cytoskeleton; Efferocytosis; Inflammation; Phagocytosis

Indexed keywords

ACTIN; CYTOPLASMIC LINKER PROTEIN 170; CYTOSKELETON PROTEIN; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; P21 ACTIVATED KINASE 1; P21 ACTIVATED KINASE 2; RAC1 PROTEIN; UNCLASSIFIED DRUG;

EID: 82655173730     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.11-190587     Document Type: Article
Times cited : (109)

References (54)
  • 2
    • 67650914230 scopus 로고    scopus 로고
    • AMPK in health and disease
    • Steinberg, G. R., and Kemp, B. E. (2009) AMPK in health and disease. Physiol. Rev. 89, 1025-1078
    • (2009) Physiol. Rev. , vol.89 , pp. 1025-1078
    • Steinberg, G.R.1    Kemp, B.E.2
  • 4
    • 33847080728 scopus 로고    scopus 로고
    • AMP-activated protein kinase in metabolic control and insulin signaling
    • Towler, M. C., and Hardie, D. G. (2007) AMP-activated protein kinase in metabolic control and insulin signaling. Circ. Res. 100, 328-341
    • (2007) Circ. Res. , vol.100 , pp. 328-341
    • Towler, M.C.1    Hardie, D.G.2
  • 5
    • 0034141355 scopus 로고    scopus 로고
    • The regulation of AMP-activated protein kinase by phosphorylation
    • DOI 10.1042/0264-6021:3450437
    • Stein, S. C., Woods, A., Jones, N. A., Davison, M. D., and Carling, D. (2000) The regulation of AMP-activated protein kinase by phosphorylation. Biochem. J. 345, 437-443 (Pubitemid 30099070)
    • (2000) Biochemical Journal , vol.345 , Issue.3 , pp. 437-443
    • Stein, S.C.1    Woods, A.2    Jones, N.A.3    Davison, M.D.4    Cabling, D.5
  • 6
    • 57849090443 scopus 로고    scopus 로고
    • The glycogen-binding domain on the AMPK beta subunit allows the kinase to act as a glycogen sensor
    • McBride, A., Ghilagaber, S., Nikolaev, A., and Hardie, D. G. (2009) The glycogen-binding domain on the AMPK beta subunit allows the kinase to act as a glycogen sensor. Cell Metab. 9, 23-34
    • (2009) Cell Metab. , vol.9 , pp. 23-34
    • McBride, A.1    Ghilagaber, S.2    Nikolaev, A.3    Hardie, D.G.4
  • 7
    • 77958501463 scopus 로고    scopus 로고
    • Exposure to hydrogen peroxide induces oxidation and activation of AMP-activated protein kinase
    • Zmijewski, J. W., Banerjee, S., Bae, H., Friggeri, A., Lazarowski, E. R., and Abraham, E. (2010) Exposure to hydrogen peroxide induces oxidation and activation of AMP-activated protein kinase. J. Biol. Chem. 285, 33154-33164
    • (2010) J. Biol. Chem. , vol.285 , pp. 33154-33164
    • Zmijewski, J.W.1    Banerjee, S.2    Bae, H.3    Friggeri, A.4    Lazarowski, E.R.5    Abraham, E.6
  • 8
    • 0029910018 scopus 로고    scopus 로고
    • Characterization of the AMP-activated protein kinase kinase from rat liver and identification of threonine 172 as the major site at which it phosphorylates AMP-activated protein kinase
    • DOI 10.1074/jbc.271.44.27879
    • Hawley, S. A., Davison, M., Woods, A., Davies, S. P., Beri, R. K., Carling, D., and Hardie, D. G. (1996) Characterization of the AMP-activated protein kinase kinase from rat liver and identification of threonine 172 as the major site at which it phosphorylates AMP-activated protein kinase. J. Biol. Chem. 271, 27879-27887 (Pubitemid 26367365)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.44 , pp. 27879-27887
    • Hawley, S.A.1    Davison, M.2    Woods, A.3    Davies, S.P.4    Beri, R.K.5    Carling, D.6    Hardie, D.G.7
  • 9
    • 0036324142 scopus 로고    scopus 로고
    • The antidiabetic drug metformin activates the AMP-activated protein kinase cascade via an adenine nucleotide-independent mechanism
    • Hawley, S. A., Gadalla, A. E., Olsen, G. S., and Hardie, D. G. (2002) The antidiabetic drug metformin activates the AMP-activated protein kinase cascade via an adenine nucleotide-independent mechanism. Diabetes 51, 2420-2425 (Pubitemid 34827390)
    • (2002) Diabetes , vol.51 , Issue.8 , pp. 2420-2425
    • Hawley, S.A.1    Gadalla, A.E.2    Olsen, G.S.3    Grahame, H.D.4
  • 10
    • 20844451123 scopus 로고    scopus 로고
    • AMP-activated protein kinase: Ancient energy gauge provides clues to modern understanding of metabolism
    • DOI 10.1016/j.cmet.2004.12.003, PII S1550413104000099
    • Kahn, B. B., Alquier, T., Carling, D., and Hardie, D. G. (2005) AMP-activated protein kinase: ancient energy gauge provides clues to modern understanding of metabolism. Cell Metab. 1, 15-25 (Pubitemid 43960587)
    • (2005) Cell Metabolism , vol.1 , Issue.1 , pp. 15-25
    • Kahn, B.B.1    Alquier, T.2    Carling, D.3    Hardie, D.G.4
  • 12
    • 34547124878 scopus 로고    scopus 로고
    • Agonist-modulated regulation of AMP-activated protein kinase (AMPK) in endothelial cells: Evidence for an AMPK → Rac1 → Akt → endothelial nitric-oxide synthase pathway
    • DOI 10.1074/jbc.M702182200
    • Levine, Y. C., Li, G. K., and Michel, T. (2007) Agonist-modulated regulation of AMP-activated protein kinase (AMPK) in endothelial cells. Evidence for an AMPK → Rac1 → Akt → endothelial nitric-oxide synthase pathway. J. Biol. Chem. 282, 20351-20364 (Pubitemid 47100039)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.28 , pp. 20351-20364
    • Levine, Y.C.1    Li, G.K.2    Michel, T.3
  • 14
    • 58849115949 scopus 로고    scopus 로고
    • Adenosine 5′-monophosphate-activated protein kinase promotes macrophage polarization to an anti-inflammatory functional phenotype
    • Sag, D., Carling, D., Stout, R. D., and Suttles, J. (2008) Adenosine 5′-monophosphate-activated protein kinase promotes macrophage polarization to an anti-inflammatory functional phenotype. J. Immunol. 181, 8633-8641
    • (2008) J. Immunol. , vol.181 , pp. 8633-8641
    • Sag, D.1    Carling, D.2    Stout, R.D.3    Suttles, J.4
  • 15
    • 77953335543 scopus 로고    scopus 로고
    • Anti-inflammatory role of cilostazol in vascular smooth muscle cells in vitro and in vivo
    • Aoki, C., Hattori, Y., Tomizawa, A., Jojima, T., and Kasai, K. (2010) Anti-inflammatory role of cilostazol in vascular smooth muscle cells in vitro and in vivo. J. Atheroscler. Thromb. 17, 503-509
    • (2010) J. Atheroscler. Thromb. , vol.17 , pp. 503-509
    • Aoki, C.1    Hattori, Y.2    Tomizawa, A.3    Jojima, T.4    Kasai, K.5
  • 16
    • 0035189594 scopus 로고    scopus 로고
    • Adenosine monophosphate-activated protein kinase mediates the protective effects of ischemic preconditioning on hepatic ischemia-reperfusion injury in the rat
    • DOI 10.1053/jhep.2001.29197
    • Peralta, C., Bartrons, R., Serafin, A., Blázquez, C., Guzmán, M., Prats, N., Xaus, C., Cutillas, B., Gelpí, E., and Roselló-Catafau, J. (2001) Adenosine monophosphate-activated protein kinase mediates the protective effects of ischemic preconditioning on hepatic ischemia-reperfusion injury in the rat. Hepatology 34, 1164-1173 (Pubitemid 33096589)
    • (2001) Hepatology , vol.34 , Issue.6 , pp. 1164-1173
    • Peralta, C.1    Bartrons, R.2    Serafin, A.3    Blaacutezquez, C.4    Guzmaacuten, M.5    Prats, N.6    Xaus, C.7    Cutillas, B.8    Gelpiacute, E.9    Roselloacute-Catafau, J.10
  • 18
    • 79952402072 scopus 로고    scopus 로고
    • Metformin inhibits HMGB1 release in LPS-treated RAW 264.7 cells and increases survival rate of endotoxaemic mice
    • Tsoyi, K., Jang, H. J., Nizamutdinova, I. T., Kim, Y. M., Lee, Y. S., Kim, H. J., Seo, H. G., Lee, J. H., and Chang, K. C. (2010) Metformin inhibits HMGB1 release in LPS-treated RAW 264.7 cells and increases survival rate of endotoxaemic mice. Br. J. Pharmacol. 162, 1498-1508
    • (2010) Br. J. Pharmacol. , vol.162 , pp. 1498-1508
    • Tsoyi, K.1    Jang, H.J.2    Nizamutdinova, I.T.3    Kim, Y.M.4    Lee, Y.S.5    Kim, H.J.6    Seo, H.G.7    Lee, J.H.8    Chang, K.C.9
  • 19
    • 38549158099 scopus 로고    scopus 로고
    • Phagocytosis and comparative innate immunity: Learning on the fly
    • DOI 10.1038/nri2240, PII NRI2240
    • Stuart, L. M., and Ezekowitz, R. A. (2008) Phagocytosis and comparative innate immunity: learning on the fly. Nat. Rev. Immunol. 8, 131-141 (Pubitemid 351161303)
    • (2008) Nature Reviews Immunology , vol.8 , Issue.2 , pp. 131-141
    • Stuart, L.M.1    Ezekowitz, R.A.2
  • 20
    • 36448961645 scopus 로고    scopus 로고
    • Engulfment of apoptotic cells: Signals for a good meal
    • DOI 10.1038/nri2214, PII NRI2214
    • Ravichandran, K. S., and Lorenz, U. (2007) Engulfment of apoptotic cells: signals for a good meal. Nat. Rev. Immunol. 7, 964-974 (Pubitemid 350166061)
    • (2007) Nature Reviews Immunology , vol.7 , Issue.12 , pp. 964-974
    • Ravichandran, K.S.1    Lorenz, U.2
  • 21
    • 46749138342 scopus 로고    scopus 로고
    • Integrin-dependent phagocytosis - Spreading from microadhesion to new concepts
    • DOI 10.1242/jcs.018036
    • Dupuy, A. G., and Caron, E. (2008) Integrin-dependent phagocytosis: spreading from microadhesion to new concepts. J. Cell Sci. 121, 1773-1783 (Pubitemid 351943370)
    • (2008) Journal of Cell Science , vol.121 , Issue.11 , pp. 1773-1783
    • Dupuy, A.G.1    Caron, E.2
  • 22
    • 3142514390 scopus 로고    scopus 로고
    • Signaling and membrane dynamics during phagocytosis: Many roads lead to the phagos(R)ome
    • DOI 10.1016/j.ceb.2004.06.006, PII S0955067404000754
    • Niedergang, F., and Chavrier, P. (2004) Signaling and membrane dynamics during phagocytosis: many roads lead to the phagos(R)ome. Curr. Opin. Cell Biol. 16, 422-428 (Pubitemid 38903149)
    • (2004) Current Opinion in Cell Biology , vol.16 , Issue.4 , pp. 422-428
    • Niedergang, F.1    Chavrier, P.2
  • 23
    • 0025099677 scopus 로고
    • Phagocytosis of Histoplasma capsulatum yeasts and microconidia by human cultured macrophages and alveolar macrophages. Cellular cytoskeleton requirement for attachment and ingestion
    • Newman, S. L., Bucher, C., Rhodes, J., and Bullock, W. E. (1990) Phagocytosis of Histoplasma capsulatum yeasts and microconidia by human cultured macrophages and alveolar macrophages. Cellular cytoskeleton requirement for attachment and ingestion. J. Clin. Invest. 85, 223-230 (Pubitemid 20030313)
    • (1990) Journal of Clinical Investigation , vol.85 , Issue.1 , pp. 223-230
    • Newman, S.L.1    Bucher, C.2    Rhodes, J.3    Bullock, W.E.4
  • 24
    • 52649099109 scopus 로고    scopus 로고
    • Signaling pathways required for macrophage scavenger receptor-mediated phagocytosis: Analysis by scanning cytometry
    • Sulahian, T. H., Imrich, A., Deloid, G., Winkler, A. R., and Kobzik, L. (2008) Signaling pathways required for macrophage scavenger receptor-mediated phagocytosis: analysis by scanning cytometry. Respir. Res. 9, 59
    • (2008) Respir. Res. , vol.9 , pp. 59
    • Sulahian, T.H.1    Imrich, A.2    Deloid, G.3    Winkler, A.R.4    Kobzik, L.5
  • 25
    • 34547772739 scopus 로고    scopus 로고
    • Microtubules regulate PI-3K activity and recruitment to the phagocytic cup during Fcgamma receptor-mediated phagocytosis in nonelicited macrophages
    • DOI 10.1189/jlb.0706469
    • Khandani, A., Eng, E., Jongstra-Bilen, J., Schreiber, A. D., Douda, D., Samavarchi-Tehrani, P., and Harrison, R. E. (2007) Microtubules regulate PI-3K activity and recruitment to the phagocytic cup during Fcgamma receptor-mediated phagocytosis in nonelicited macrophages. J. Leukoc. Biol. 82, 417-428 (Pubitemid 47230653)
    • (2007) Journal of Leukocyte Biology , vol.82 , Issue.2 , pp. 417-428
    • Khandani, A.1    Eng, E.2    Jongstra-Bilen, J.3    Schreiber, A.D.4    Douda, D.5    Samavarchi-Tehrani, P.6    Harrison, R.E.7
  • 26
    • 54549104845 scopus 로고    scopus 로고
    • Crosstalk between small GTPases and polarity proteins in cell polarization
    • Iden, S., and Collard, J. G. (2008) Crosstalk between small GTPases and polarity proteins in cell polarization. Nat. Rev. Mol. Cell. Biol. 9, 846-859
    • (2008) Nat. Rev. Mol. Cell. Biol. , vol.9 , pp. 846-859
    • Iden, S.1    Collard, J.G.2
  • 27
    • 34249942138 scopus 로고    scopus 로고
    • c-Abl-binding Protein Interacts with p21-activated Kinase 2 (PAK-2) to Regulate PDGF-induced Membrane Ruffles
    • DOI 10.1016/j.jmb.2007.04.080, PII S0022283607005803
    • Machuy, N., Campa, F., Thieck, O., and Rudel, T. (2007) c-Abl-binding protein interacts with p21-activated kinase 2 (PAK-2) to regulate PDGF-induced membrane ruffles. J. Mol. Biol. 370, 620-632 (Pubitemid 46879771)
    • (2007) Journal of Molecular Biology , vol.370 , Issue.4 , pp. 620-632
    • Machuy, N.1    Campa, F.2    Thieck, O.3    Rudel, T.4
  • 28
    • 0037114750 scopus 로고    scopus 로고
    • Cdc42/Rac1-dependent activation of the p21-activated kinase (PAK) regulates human platelet lamellipodia spreading: Implication of the cortical-actin binding protein cortactin
    • DOI 10.1182/blood.V100.13.4462
    • Vidal, C., Geny, B., Melle, J., Jandrot-Perrus, M., and Fontenay-Roupie, M. (2002) Cdc42/Rac1-dependent activation of the p21-activated kinase (PAK) regulates human platelet lamellipodia spreading: implication of the cortical-actin binding protein cortactin. Blood 100, 4462-4469 (Pubitemid 35429686)
    • (2002) Blood , vol.100 , Issue.13 , pp. 4462-4469
    • Vidal, C.1    Geny, B.2    Melle, J.3    Jandrot-Perrus, M.4    Fontenay-Roupie, M.5
  • 29
    • 70449112591 scopus 로고    scopus 로고
    • Activation of the WAVE complex by coincident signals controls actin assembly
    • Lebensohn, A. M., and Kirschner, M. W. (2009) Activation of the WAVE complex by coincident signals controls actin assembly. Mol. Cell 36, 512-524
    • (2009) Mol. Cell , vol.36 , pp. 512-524
    • Lebensohn, A.M.1    Kirschner, M.W.2
  • 30
    • 0032573378 scopus 로고    scopus 로고
    • Identification of two distinct mechanisms of phagocytosis controlled by different Rho GTPases
    • Caron, E., and Hall, A. (1998) Identification of two distinct mechanisms of phagocytosis controlled by different Rho GTPases. Science 282, 1717-1721 (Pubitemid 28549289)
    • (1998) Science , vol.282 , Issue.5394 , pp. 1717-1721
    • Caron, E.1    Hall, A.2
  • 32
    • 35748939079 scopus 로고    scopus 로고
    • Cytoplasmic linker protein-170 enhances spreading and phagocytosis in activated macrophages by stabilizing microtubules
    • Binker, M. G., Zhao, D. Y., Pang, S. J., and Harrison, R. E. (2007) Cytoplasmic linker protein-170 enhances spreading and phagocytosis in activated macrophages by stabilizing microtubules. J. Immunol. 179, 3780-3791
    • (2007) J. Immunol. , vol.179 , pp. 3780-3791
    • Binker, M.G.1    Zhao, D.Y.2    Pang, S.J.3    Harrison, R.E.4
  • 33
    • 57749093010 scopus 로고    scopus 로고
    • Retinoic acid leads to cytoskeletal rearrangement through AMPK-Rac1 and stimulates glucose uptake through AMPK-p38 MAPK in skeletal muscle cells
    • Lee, Y. M., Lee, J. O., Jung, J. H., Kim, J. H., Park, S. H., Park, J. M., Kim, E. K., Suh, P. G., and Kim, H. S. (2008) Retinoic acid leads to cytoskeletal rearrangement through AMPK-Rac1 and stimulates glucose uptake through AMPK-p38 MAPK in skeletal muscle cells. J. Biol. Chem. 283, 33969-33974
    • (2008) J. Biol. Chem. , vol.283 , pp. 33969-33974
    • Lee, Y.M.1    Lee, J.O.2    Jung, J.H.3    Kim, J.H.4    Park, S.H.5    Park, J.M.6    Kim, E.K.7    Suh, P.G.8    Kim, H.S.9
  • 35
    • 38449114688 scopus 로고    scopus 로고
    • Involvement of vitronectin in lipopolysaccaride-induced acute lung injury
    • Tsuruta, Y., Park, Y. J., Siegal, G. P., Liu, G., and Abraham, E. (2007) Involvement of vitronectin in lipopolysaccaride-induced acute lung injury. J. Immunol. 179, 7079-7086
    • (2007) J. Immunol. , vol.179 , pp. 7079-7086
    • Tsuruta, Y.1    Park, Y.J.2    Siegal, G.P.3    Liu, G.4    Abraham, E.5
  • 36
    • 34547137901 scopus 로고    scopus 로고
    • Exposure to hydrogen peroxide diminishes NF-kappaB activation, IkappaB-α degradation, and proteasome activity in neutrophils
    • DOI 10.1152/ajpcell.00618.2006
    • Zmijewski, J. W., Zhao, X., Xu, Z., and Abraham, E. (2007) Exposure to hydrogen peroxide diminishes NF-κB activation, IκB-α degradation, and proteasome activity in neutrophils. Am. J. Physiol. Cell Physiol. 293, C255-C266 (Pubitemid 47105028)
    • (2007) American Journal of Physiology - Cell Physiology , vol.293 , Issue.1
    • Zmijewski, J.W.1    Zhao, X.2    Xu, Z.3    Abraham, E.4
  • 37
    • 41949118525 scopus 로고    scopus 로고
    • Role of extracellular superoxide in neutrophil activation: Interactions between xanthine oxidase and TLR4 induce proinflammatory cytokine production
    • DOI 10.1152/ajpcell.00454.2007
    • Lorne, E., Zmijewski, J. W., Zhao, X., Liu, G., Tsuruta, Y., Park, Y. J., Dupont, H., and Abraham, E. (2008) Role of extracellular superoxide in neutrophil activation: interactions between xanthine oxidase and TLR4 induce proinflammatory cytokine production. Am. J. Physiol. Cell Physiol. 294, C985-C993 (Pubitemid 351507911)
    • (2008) American Journal of Physiology - Cell Physiology , vol.294 , Issue.4
    • Lorne, E.1    Zmijewski, J.W.2    Zhao, X.3    Liu, G.4    Tsuruta, Y.5    Park, Y.-J.6    Dupont, H.7    Abraham, E.8
  • 38
    • 0018180802 scopus 로고
    • Functional macrophage cell lines transformed by Abelson leukemia virus
    • Raschke, W. C., Baird, S., Ralph, P., and Nakoinz, I. (1978) Functional macrophage cell lines transformed by Abelson leukemia virus. Cell 15, 261-267 (Pubitemid 9027529)
    • (1978) Cell , vol.15 , Issue.1 , pp. 261-267
    • Raschke, W.C.1    Baird, S.2    Ralph, P.3    Nakoinz, I.4
  • 39
    • 76249133494 scopus 로고    scopus 로고
    • Matrix metalloproteinase (MMP)-1 and MMP-3 induce macrophage MMP-9: Evidence for the role of TNF-alpha and cyclooxygenase-2
    • Steenport, M., Khan, K. M., Du, B., Barnhard, S. E., Dannenberg, A. J., and Falcone, D. J. (2009) Matrix metalloproteinase (MMP)-1 and MMP-3 induce macrophage MMP-9: evidence for the role of TNF-alpha and cyclooxygenase-2. J. Immunol. 183, 8119-8127
    • (2009) J. Immunol. , vol.183 , pp. 8119-8127
    • Steenport, M.1    Khan, K.M.2    Du, B.3    Barnhard, S.E.4    Dannenberg, A.J.5    Falcone, D.J.6
  • 43
    • 0027318744 scopus 로고
    • A rapid and simple microfluorometric phagocytosis assay
    • Wan, C. P., Park, C. S., and Lau, B. H. (1993) A rapid and simple microfluorometric phagocytosis assay. J. Immunol. Methods 162, 1-7
    • (1993) J. Immunol. Methods , vol.162 , pp. 1-7
    • Wan, C.P.1    Park, C.S.2    Lau, B.H.3
  • 44
    • 2142640818 scopus 로고    scopus 로고
    • 5-Aminoimidazole-4-carboxamide riboside suppresses lipopolysaccharide- induced TNF-α production through inhibition of phosphatidylinositol 3-kinase/Akt activation in RAW 264.7 murine macrophages
    • DOI 10.1016/j.bbrc.2004.04.035, PII S0006291X04007600
    • Jhun, B. S., Jin, Q., Oh, Y. T., Kim, S. S., Kong, Y., Cho, Y. H., Ha, J., Baik, H. H., and Kang, I. (2004) 5-Aminoimidazole-4-carboxamide riboside suppresses lipopolysaccharide-induced TNF-alpha production through inhibition of phosphatidylinositol 3-kinase/Akt activation in RAW 264.7 murine macrophages. Biochem. Biophys. Res. Commun. 318, 372-380 (Pubitemid 38553790)
    • (2004) Biochemical and Biophysical Research Communications , vol.318 , Issue.2 , pp. 372-380
    • Jhun, B.S.1    Jin, Q.2    Oh, Y.T.3    Kim, S.S.4    Kong, Y.5    Cho, Y.H.6    Ha, J.7    Baik, H.H.8    Kang, I.9
  • 45
    • 29244432463 scopus 로고    scopus 로고
    • A WAVE2-Abi1 complex mediates CSF-1-induced F-actin-rich membrane protrusions and migration in macrophages
    • DOI 10.1242/jcs.02638
    • Kheir, W. A., Gevrey, J. C., Yamaguchi, H., Isaac, B., and Cox, D. (2005) A WAVE2-Abi1 complex mediates CSF-1-induced F-actin-rich membrane protrusions and migration in macrophages. J. Cell Sci. 118, 5369-5379 (Pubitemid 41819598)
    • (2005) Journal of Cell Science , vol.118 , Issue.22 , pp. 5369-5379
    • Kheir, W.A.1    Gevrey, J.-C.2    Yamaguchi, H.3    Isaac, B.4    Cox, D.5
  • 46
    • 0033194037 scopus 로고    scopus 로고
    • Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics
    • Edwards, D. C., Sanders, L. C., Bokoch, G. M., and Gill, G. N. (1999) Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. Nat. Cell Biol. 1, 253-259 (Pubitemid 129495774)
    • (1999) Nature Cell Biology , vol.1 , Issue.5 , pp. 253-259
    • Edwards, D.C.1    Sanders, L.C.2    Bokoch, G.M.3    Gill, G.N.4
  • 48
    • 48449084609 scopus 로고    scopus 로고
    • Berberine and its more biologically available derivative, dihydroberberine, inhibit mitochondrial respiratory complex I: A mechanism for the action of berberine to activate AMP-activated protein kinase and improve insulin action
    • Turner, N., Li, J. Y., Gosby, A., To, S. W., Cheng, Z., Miyoshi, H., Taketo, M. M., Cooney, G. J., Kraegen, E. W., James, D. E., Hu, L. H., Li, J., and Ye, J. M. (2008) Berberine and its more biologically available derivative, dihydroberberine, inhibit mitochondrial respiratory complex I: a mechanism for the action of berberine to activate AMP-activated protein kinase and improve insulin action. Diabetes 57, 1414-1418
    • (2008) Diabetes , vol.57 , pp. 1414-1418
    • Turner, N.1    Li, J.Y.2    Gosby, A.3    To, S.W.4    Cheng, Z.5    Miyoshi, H.6    Taketo, M.M.7    Cooney, G.J.8    Kraegen, E.W.9    James, D.E.10    Hu, L.H.11    Li, J.12    Ye, J.M.13
  • 49
    • 77949265454 scopus 로고    scopus 로고
    • Metformin increases phagocytosis and acidifies lysosomal/endosomal compartments in AMPK-dependent manner in rat primary microglia
    • Labuzek, K., Liber, S., Gabryel, B., Adamczyk, J., and Okopien, B. (2010) Metformin increases phagocytosis and acidifies lysosomal/endosomal compartments in AMPK-dependent manner in rat primary microglia. Naunyn Schmiedebergs Arch. Pharmacol. 381, 171-186
    • (2010) Naunyn Schmiedebergs Arch. Pharmacol. , vol.381 , pp. 171-186
    • Labuzek, K.1    Liber, S.2    Gabryel, B.3    Adamczyk, J.4    Okopien, B.5
  • 50
    • 0037413824 scopus 로고    scopus 로고
    • Microtubule-dependent regulation of Rho GTPases during internalisation of Yersinia pseudotuberculosis
    • DOI 10.1016/S0014-5793(02)03745-6, PII S0014579302037456
    • McGee, K., Holmfeldt, P., and Fällman, M. (2003) Microtubule-dependent regulation of Rho GTPases during internalisation of Yersinia pseudotuberculosis. FEBS Lett. 533, 35-41 (Pubitemid 36206378)
    • (2003) FEBS Letters , vol.533 , Issue.1-3 , pp. 35-41
    • McGee, K.1    Holmfeldt, P.2    Fallman, M.3
  • 52
    • 27644563566 scopus 로고    scopus 로고
    • Interactions between CLIP-170, tubulin, and microtubules: Implications for the mechanism of CLIP-170 plus-end tracking behavior
    • DOI 10.1091/mbc.E04-12-1106
    • Folker, E. S., Baker, B. M., and Goodson, H. V. (2005) Interactions between CLIP-170, tubulin, and microtubules: implications for the mechanism of Clip-170 plus-end tracking behavior. Mol. Biol. Cell 16, 5373-5384 (Pubitemid 41566846)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.11 , pp. 5373-5384
    • Folker, E.S.1    Baker, B.M.2    Goodson, H.V.3
  • 53
    • 59449094652 scopus 로고    scopus 로고
    • The microtubule-binding protein CLIP-170 coordinates mDia1 and actin reorganization during CR3-mediated phagocytosis
    • Lewkowicz, E., Herit, F., Le Clainche, C., Bourdoncle, P., Perez, F., and Niedergang, F. (2008) The microtubule-binding protein CLIP-170 coordinates mDia1 and actin reorganization during CR3-mediated phagocytosis. J. Cell Biol. 183, 1287-1298
    • (2008) J. Cell Biol. , vol.183 , pp. 1287-1298
    • Lewkowicz, E.1    Herit, F.2    Le Clainche, C.3    Bourdoncle, P.4    Perez, F.5    Niedergang, F.6
  • 54
    • 0032896022 scopus 로고    scopus 로고
    • Disruption of filamentous actin inhibits human macrophage fusion
    • DeFife, K. M., Jenney, C. R., Colton, E., and Anderson, J. M. (1999) Disruption of filamentous actin inhibits human macrophage fusion. FASEB J. 13, 823-832 (Pubitemid 29220695)
    • (1999) FASEB Journal , vol.13 , Issue.8 , pp. 823-832
    • DeFife, K.M.1    Jenney, C.R.2    Colton, E.3    Anderson, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.