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Volumn 8, Issue 7, 2013, Pages

Adiponectin Inhibits Neutrophil Phagocytosis of Escherichia coli by Inhibition of PKB and ERK 1/2 MAPK Signalling and Mac-1 Activation

Author keywords

[No Author keywords available]

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; 2 MORPHOLINO 8 PHENYLCHROMONE; 5 AMINO 4 IMIDAZOLECARBOXAMIDE RIBOSIDE; ADIPONECTIN; CD11B ANTIGEN; F ACTIN; MITOGEN ACTIVATED PROTEIN KINASE 1;

EID: 84880782020     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0069108     Document Type: Article
Times cited : (27)

References (54)
  • 1
    • 1642299047 scopus 로고    scopus 로고
    • Adipose tissue adiponectin production and adiponectin serum concentration in human obesity and insulin resistance
    • Hoffstedt J, Arvidsson E, Sjolin E, Wahlen K, Arner P, (2004) Adipose tissue adiponectin production and adiponectin serum concentration in human obesity and insulin resistance. J Clin Endocrinol Metab 89: 1391-1396.
    • (2004) J Clin Endocrinol Metab , vol.89 , pp. 1391-1396
    • Hoffstedt, J.1    Arvidsson, E.2    Sjolin, E.3    Wahlen, K.4    Arner, P.5
  • 2
    • 0028787490 scopus 로고
    • A novel serum protein similar to C1q, produced exclusively in adipocytes
    • Scherer PE, Williams S, Fogliano M, Baldini G, Lodish HF, (1995) A novel serum protein similar to C1q, produced exclusively in adipocytes. J Biol Chem 270: 26746-26749.
    • (1995) J Biol Chem , vol.270 , pp. 26746-26749
    • Scherer, P.E.1    Williams, S.2    Fogliano, M.3    Baldini, G.4    Lodish, H.F.5
  • 3
    • 0141924849 scopus 로고    scopus 로고
    • Impaired multimerization of human adiponectin mutants associated with diabetes. Molecular structure and multimer formation of adiponectin
    • Waki H, Yamauchi T, Kamon J, Ito Y, Uchida S, et al. (2003) Impaired multimerization of human adiponectin mutants associated with diabetes. Molecular structure and multimer formation of adiponectin. J Biol Chem 278: 40352-40363.
    • (2003) J Biol Chem , vol.278 , pp. 40352-40363
    • Waki, H.1    Yamauchi, T.2    Kamon, J.3    Ito, Y.4    Uchida, S.5
  • 4
    • 24744457984 scopus 로고    scopus 로고
    • Adiponectin promotes adipocyte differentiation, insulin sensitivity, and lipid accumulation
    • Fu Y, Luo N, Klein RL, Garvey WT, (2005) Adiponectin promotes adipocyte differentiation, insulin sensitivity, and lipid accumulation. J Lipid Res 46: 1369-1379.
    • (2005) J Lipid Res , vol.46 , pp. 1369-1379
    • Fu, Y.1    Luo, N.2    Klein, R.L.3    Garvey, W.T.4
  • 5
    • 0036511213 scopus 로고    scopus 로고
    • Acrp30/adiponectin: An adipokine regulating glucose and lipid metabolism
    • Berg AH, Combs TP, Scherer PE, (2002) Acrp30/adiponectin: An adipokine regulating glucose and lipid metabolism. Trends Endocrinol Metab 13: 84-89.
    • (2002) Trends Endocrinol Metab , vol.13 , pp. 84-89
    • Berg, A.H.1    Combs, T.P.2    Scherer, P.E.3
  • 6
    • 0037180472 scopus 로고    scopus 로고
    • Adiponectin reduces atherosclerosis in apolipoprotein e-deficient mice
    • Okamoto Y, Kihara S, Ouchi N, Nishida M, Arita Y, et al. (2002) Adiponectin reduces atherosclerosis in apolipoprotein e-deficient mice. Circulation 106: 2767-2770.
    • (2002) Circulation , vol.106 , pp. 2767-2770
    • Okamoto, Y.1    Kihara, S.2    Ouchi, N.3    Nishida, M.4    Arita, Y.5
  • 7
    • 33748992313 scopus 로고    scopus 로고
    • Adipocytokines: Mediators linking adipose tissue, inflammation and immunity
    • Tilg H, Moschen AR, (2006) Adipocytokines: Mediators linking adipose tissue, inflammation and immunity. Nat Rev Immunol 6: 772-783.
    • (2006) Nat Rev Immunol , vol.6 , pp. 772-783
    • Tilg, H.1    Moschen, A.R.2
  • 10
    • 0034999667 scopus 로고    scopus 로고
    • Hypoadiponectinemia in obesity and type 2 diabetes: Close association with insulin resistance and hyperinsulinemia
    • Weyer C, Funahashi T, Tanaka S, Hotta K, Matsuzawa Y, et al. (2001) Hypoadiponectinemia in obesity and type 2 diabetes: Close association with insulin resistance and hyperinsulinemia. J Clin Endocrinol Metab 86: 1930-1935.
    • (2001) J Clin Endocrinol Metab , vol.86 , pp. 1930-1935
    • Weyer, C.1    Funahashi, T.2    Tanaka, S.3    Hotta, K.4    Matsuzawa, Y.5
  • 12
    • 84856006742 scopus 로고    scopus 로고
    • Adiponectin and its globular fragment differentially modulate the oxidative burst of primary human phagocytes
    • Chedid P, Hurtado-Nedelec M, Marion-Gaber B, Bournier O, Hayem G, et al. (2012) Adiponectin and its globular fragment differentially modulate the oxidative burst of primary human phagocytes. Am J Pathol 180: 682-692.
    • (2012) Am J Pathol , vol.180 , pp. 682-692
    • Chedid, P.1    Hurtado-Nedelec, M.2    Marion-Gaber, B.3    Bournier, O.4    Hayem, G.5
  • 13
    • 84862922916 scopus 로고    scopus 로고
    • Adiponectin attenuates lipopolysaccharide-induced acute lung injury through suppression of endothelial cell activation
    • Konter JM, Parker JL, Baez E, Li SZ, Ranscht B, et al. (2012) Adiponectin attenuates lipopolysaccharide-induced acute lung injury through suppression of endothelial cell activation. J Immunol 188: 854-863.
    • (2012) J Immunol , vol.188 , pp. 854-863
    • Konter, J.M.1    Parker, J.L.2    Baez, E.3    Li, S.Z.4    Ranscht, B.5
  • 14
    • 3042699353 scopus 로고    scopus 로고
    • Adiponectin protects LPS-induced liver injury through modulation of TNF-alpha in kk-ay obese mice
    • Masaki T, Chiba S, Tatsukawa H, Yasuda T, Noguchi H, et al. (2004) Adiponectin protects LPS-induced liver injury through modulation of TNF-alpha in kk-ay obese mice. Hepatology 40: 177-184.
    • (2004) Hepatology , vol.40 , pp. 177-184
    • Masaki, T.1    Chiba, S.2    Tatsukawa, H.3    Yasuda, T.4    Noguchi, H.5
  • 15
    • 33646470282 scopus 로고    scopus 로고
    • Adiponectin is a negative regulator of NK cell cytotoxicity
    • Kim KY, Kim JK, Han SH, Lim JS, Kim KI, et al. (2006) Adiponectin is a negative regulator of NK cell cytotoxicity. J Immunol 176: 5958-5964.
    • (2006) J Immunol , vol.176 , pp. 5958-5964
    • Kim, K.Y.1    Kim, J.K.2    Han, S.H.3    Lim, J.S.4    Kim, K.I.5
  • 17
    • 33846784058 scopus 로고    scopus 로고
    • Adiponectin modulates inflammatory reactions via calreticulin receptor-dependent clearance of early apoptotic bodies
    • Takemura Y, Ouchi N, Shibata R, Aprahamian T, Kirber MT, et al. (2007) Adiponectin modulates inflammatory reactions via calreticulin receptor-dependent clearance of early apoptotic bodies. J Clin Invest 117: 375-386.
    • (2007) J Clin Invest , vol.117 , pp. 375-386
    • Takemura, Y.1    Ouchi, N.2    Shibata, R.3    Aprahamian, T.4    Kirber, M.T.5
  • 18
    • 0034284038 scopus 로고    scopus 로고
    • Adiponectin, a new member of the family of soluble defense collagens, negatively regulates the growth of myelomonocytic progenitors and the functions of macrophages
    • Yokota T, Oritani K, Takahashi I, Ishikawa J, Matsuyama A, et al. (2000) Adiponectin, a new member of the family of soluble defense collagens, negatively regulates the growth of myelomonocytic progenitors and the functions of macrophages. Blood 96: 1723-1732.
    • (2000) Blood , vol.96 , pp. 1723-1732
    • Yokota, T.1    Oritani, K.2    Takahashi, I.3    Ishikawa, J.4    Matsuyama, A.5
  • 19
    • 79954631240 scopus 로고    scopus 로고
    • Novel immunomodulatory effects of adiponectin on dendritic cell functions
    • Tsang JY, Li D, Ho D, Peng J, Xu A, et al. (2011) Novel immunomodulatory effects of adiponectin on dendritic cell functions. Int Immunopharmacol 11: 604-609.
    • (2011) Int Immunopharmacol , vol.11 , pp. 604-609
    • Tsang, J.Y.1    Li, D.2    Ho, D.3    Peng, J.4    Xu, A.5
  • 20
    • 84863295568 scopus 로고    scopus 로고
    • Adiponectin induces dendritic cell activation via PLCgamma/JNK/NF-kappab pathways, leading to Th1 and Th17 polarization
    • Jung MY, Kim HS, Hong HJ, Youn BS, Kim TS, (2012) Adiponectin induces dendritic cell activation via PLCgamma/JNK/NF-kappab pathways, leading to Th1 and Th17 polarization. J Immunol 188: 2592-2601.
    • (2012) J Immunol , vol.188 , pp. 2592-2601
    • Jung, M.Y.1    Kim, H.S.2    Hong, H.J.3    Youn, B.S.4    Kim, T.S.5
  • 21
    • 17644377258 scopus 로고    scopus 로고
    • How neutrophils kill microbes
    • Segal AW, (2005) How neutrophils kill microbes. Annu Rev Immunol 23: 197-223.
    • (2005) Annu Rev Immunol , vol.23 , pp. 197-223
    • Segal, A.W.1
  • 23
    • 0036216769 scopus 로고    scopus 로고
    • Phagocytosis of microbes: Complexity in action
    • Underhill DM, Ozinsky A, (2002) Phagocytosis of microbes: Complexity in action. Annu Rev Immunol 20: 825-852.
    • (2002) Annu Rev Immunol , vol.20 , pp. 825-852
    • Underhill, D.M.1    Ozinsky, A.2
  • 24
    • 0028446566 scopus 로고
    • The dynamic regulation of integrin adhesiveness
    • Diamond MS, Springer TA, (1994) The dynamic regulation of integrin adhesiveness. Curr Biol 4: 506-517.
    • (1994) Curr Biol , vol.4 , pp. 506-517
    • Diamond, M.S.1    Springer, T.A.2
  • 25
    • 0031790002 scopus 로고    scopus 로고
    • Bacterial phagocytosis activates extracellular signal-regulated kinase and p38 mitogen-activated protein kinase cascades in human neutrophils
    • McLeish KR, Klein JB, Coxon PY, Head KZ, Ward RA, (1998) Bacterial phagocytosis activates extracellular signal-regulated kinase and p38 mitogen-activated protein kinase cascades in human neutrophils. J Leukoc Biol 64: 835-844.
    • (1998) J Leukoc Biol , vol.64 , pp. 835-844
    • McLeish, K.R.1    Klein, J.B.2    Coxon, P.Y.3    Head, K.Z.4    Ward, R.A.5
  • 26
    • 0033555931 scopus 로고    scopus 로고
    • A requirement for phosphatidylinositol 3-kinase in pseudopod extension
    • Cox D, Tseng CC, Bjekic G, Greenberg S, (1999) A requirement for phosphatidylinositol 3-kinase in pseudopod extension. J Biol Chem 274: 1240-1247.
    • (1999) J Biol Chem , vol.274 , pp. 1240-1247
    • Cox, D.1    Tseng, C.C.2    Bjekic, G.3    Greenberg, S.4
  • 27
    • 0036909507 scopus 로고    scopus 로고
    • Signal transduction during Fc receptor-mediated phagocytosis
    • Garcia-Garcia E, Rosales C, (2002) Signal transduction during Fc receptor-mediated phagocytosis. J Leukoc Biol 72: 1092-1108.
    • (2002) J Leukoc Biol , vol.72 , pp. 1092-1108
    • Garcia-Garcia, E.1    Rosales, C.2
  • 28
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies SP, Reddy H, Caivano M, Cohen P, (2000) Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem J 351: 95-105.
    • (2000) Biochem J , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 29
    • 0028170210 scopus 로고
    • A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4h-1-benzopyran-4-one (LY294002)
    • Vlahos CJ, Matter WF, Hui KY, Brown RF, (1994) A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4h-1-benzopyran-4-one (LY294002). J Biol Chem 269: 5241-5248.
    • (1994) J Biol Chem , vol.269 , pp. 5241-5248
    • Vlahos, C.J.1    Matter, W.F.2    Hui, K.Y.3    Brown, R.F.4
  • 30
    • 77954095496 scopus 로고    scopus 로고
    • PI3k is involved in L-selectin- and PSGL-1-mediated neutrophil rolling on E-selectin via F-actin redistribution and assembly
    • Luo J, Xu T, Wang X, Ba X, Feng X, et al. (2010) PI3k is involved in L-selectin- and PSGL-1-mediated neutrophil rolling on E-selectin via F-actin redistribution and assembly. J Cell Biochem 110: 910-919.
    • (2010) J Cell Biochem , vol.110 , pp. 910-919
    • Luo, J.1    Xu, T.2    Wang, X.3    Ba, X.4    Feng, X.5
  • 31
    • 34548226931 scopus 로고    scopus 로고
    • Heme induces neutrophil migration and reactive oxygen species generation through signaling pathways characteristic of chemotactic receptors
    • Porto BN, Alves LS, Fernandez PL, Dutra TP, Figueiredo RT, et al. (2007) Heme induces neutrophil migration and reactive oxygen species generation through signaling pathways characteristic of chemotactic receptors. J Biol Chem 282: 24430-24436.
    • (2007) J Biol Chem , vol.282 , pp. 24430-24436
    • Porto, B.N.1    Alves, L.S.2    Fernandez, P.L.3    Dutra, T.P.4    Figueiredo, R.T.5
  • 32
    • 0030903025 scopus 로고    scopus 로고
    • Interleukin 8-stimulated phosphatidylinositol-3-kinase activity regulates the migration of human neutrophils independent of extracellular signal-regulated kinase and p38 mitogen-activated protein kinases
    • Knall C, Worthen GS, Johnson GL, (1997) Interleukin 8-stimulated phosphatidylinositol-3-kinase activity regulates the migration of human neutrophils independent of extracellular signal-regulated kinase and p38 mitogen-activated protein kinases. Proc Natl Acad Sci U S A 94: 3052-3057.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 3052-3057
    • Knall, C.1    Worthen, G.S.2    Johnson, G.L.3
  • 33
    • 15744384142 scopus 로고    scopus 로고
    • Stimulation of intracellular Ca2+ elevation in neutrophils by thiol-oxidizing phenylarsine oxide
    • Wang JP, Tsai JJ, Chen YS, Hsu MF, (2005) Stimulation of intracellular Ca2+ elevation in neutrophils by thiol-oxidizing phenylarsine oxide. Biochem Pharmacol 69: 1225-1234.
    • (2005) Biochem Pharmacol , vol.69 , pp. 1225-1234
    • Wang, J.P.1    Tsai, J.J.2    Chen, Y.S.3    Hsu, M.F.4
  • 34
    • 80053968646 scopus 로고    scopus 로고
    • The NADPH oxidase cytosolic component p67phox is constitutively phosphorylated in human neutrophils: Regulation by a protein tyrosine kinase, MEK1/2 and phosphatases 1/2a
    • Dang PM, Raad H, Derkawi RA, Boussetta T, Paclet MH, et al. (2011) The NADPH oxidase cytosolic component p67phox is constitutively phosphorylated in human neutrophils: Regulation by a protein tyrosine kinase, MEK1/2 and phosphatases 1/2a. Biochem Pharmacol 82: 1145-1152.
    • (2011) Biochem Pharmacol , vol.82 , pp. 1145-1152
    • Dang, P.M.1    Raad, H.2    Derkawi, R.A.3    Boussetta, T.4    Paclet, M.H.5
  • 35
    • 33744531652 scopus 로고    scopus 로고
    • Mechanics of neutrophil phagocytosis: Experiments and quantitative models
    • Herant M, Heinrich V, Dembo M, (2006) Mechanics of neutrophil phagocytosis: Experiments and quantitative models. J Cell Sci 119: 1903-1913.
    • (2006) J Cell Sci , vol.119 , pp. 1903-1913
    • Herant, M.1    Heinrich, V.2    Dembo, M.3
  • 36
    • 50649090270 scopus 로고    scopus 로고
    • Cortactin branches out: Roles in regulating protrusive actin dynamics
    • Ammer AG, Weed SA, (2008) Cortactin branches out: Roles in regulating protrusive actin dynamics. Cell Motil Cytoskeleton 65: 687-707.
    • (2008) Cell Motil Cytoskeleton , vol.65 , pp. 687-707
    • Ammer, A.G.1    Weed, S.A.2
  • 37
    • 41849148596 scopus 로고    scopus 로고
    • The tyrosine kinase syk promotes phagocytosis of francisella through the activation of ERK
    • Parsa KV, Butchar JP, Rajaram MV, Cremer TJ, Tridandapani S, (2008) The tyrosine kinase syk promotes phagocytosis of francisella through the activation of ERK. Mol Immunol 45: 3012-3021.
    • (2008) Mol Immunol , vol.45 , pp. 3012-3021
    • Parsa, K.V.1    Butchar, J.P.2    Rajaram, M.V.3    Cremer, T.J.4    Tridandapani, S.5
  • 38
    • 70350100445 scopus 로고    scopus 로고
    • Systemic lupus erythematosus and C1q: A quantitative elisa for determining c1q levels in serum
    • Dillon SP, D'Souza A, Kurien BT, Scofield RH, (2009) Systemic lupus erythematosus and C1q: A quantitative elisa for determining c1q levels in serum. Biotechnol J 4: 1210-1214.
    • (2009) Biotechnol J , vol.4 , pp. 1210-1214
    • Dillon, S.P.1    D'Souza, A.2    Kurien, B.T.3    Scofield, R.H.4
  • 39
    • 23944488210 scopus 로고    scopus 로고
    • Absence of complement receptor 3 results in reduced binding and ingestion of mycobacterium tuberculosis but has no significant effect on the induction of reactive oxygen and nitrogen intermediates or on the survival of the bacteria in resident and interferon-gamma activated macrophages
    • Rooyakkers AW, Stokes RW, (2005) Absence of complement receptor 3 results in reduced binding and ingestion of mycobacterium tuberculosis but has no significant effect on the induction of reactive oxygen and nitrogen intermediates or on the survival of the bacteria in resident and interferon-gamma activated macrophages. Microb Pathog 39: 57-67.
    • (2005) Microb Pathog , vol.39 , pp. 57-67
    • Rooyakkers, A.W.1    Stokes, R.W.2
  • 40
    • 0242580737 scopus 로고    scopus 로고
    • Fcgamma-receptors induce mac-1 (CD11b/CD18) mobilization and accumulation in the phagocytic cup for optimal phagocytosis
    • Jongstra-Bilen J, Harrison R, Grinstein S, (2003) Fcgamma-receptors induce mac-1 (CD11b/CD18) mobilization and accumulation in the phagocytic cup for optimal phagocytosis. J Biol Chem 278: 45720-45729.
    • (2003) J Biol Chem , vol.278 , pp. 45720-45729
    • Jongstra-Bilen, J.1    Harrison, R.2    Grinstein, S.3
  • 41
    • 0036065586 scopus 로고    scopus 로고
    • CR3 (CD11b/CD18) and CR4 (CD11c/CD18) are involved in complement-independent antibody-mediated phagocytosis of cryptococcus neoformans
    • Taborda CP, Casadevall A, (2002) CR3 (CD11b/CD18) and CR4 (CD11c/CD18) are involved in complement-independent antibody-mediated phagocytosis of cryptococcus neoformans. Immunity 16: 791-802.
    • (2002) Immunity , vol.16 , pp. 791-802
    • Taborda, C.P.1    Casadevall, A.2
  • 42
    • 34247643153 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase signaling pathway exerts protective effects during sepsis by controlling C5a-mediated activation of innate immune functions
    • Wrann CD, Tabriz NA, Barkhausen T, Klos A, van Griensven M, et al. (2007) The phosphatidylinositol 3-kinase signaling pathway exerts protective effects during sepsis by controlling C5a-mediated activation of innate immune functions. J Immunol 178: 5940-5948.
    • (2007) J Immunol , vol.178 , pp. 5940-5948
    • Wrann, C.D.1    Tabriz, N.A.2    Barkhausen, T.3    Klos, A.4    van Griensven, M.5
  • 43
    • 73449123691 scopus 로고    scopus 로고
    • Role of phosphatidylinositol-3-kinase (PI3k), extracellular signal-regulated kinase (ERK) and nuclear transcription factor kappa beta (NF-kbeta) on neutrophil phagocytic process of candida albicans
    • Giraldo E, Martin-Cordero L, Hinchado MD, Garcia JJ, Ortega E, (2010) Role of phosphatidylinositol-3-kinase (PI3k), extracellular signal-regulated kinase (ERK) and nuclear transcription factor kappa beta (NF-kbeta) on neutrophil phagocytic process of candida albicans. Mol Cell Biochem 333: 115-120.
    • (2010) Mol Cell Biochem , vol.333 , pp. 115-120
    • Giraldo, E.1    Martin-Cordero, L.2    Hinchado, M.D.3    Garcia, J.J.4    Ortega, E.5
  • 44
    • 11144252845 scopus 로고    scopus 로고
    • PD98059 and U0126 activate AMP-activated protein kinase by increasing the cellular AMP:ATP ratio and not via inhibition of the MAP kinase pathway
    • Dokladda K, Green KA, Pan DA, Hardie DG, (2005) PD98059 and U0126 activate AMP-activated protein kinase by increasing the cellular AMP:ATP ratio and not via inhibition of the MAP kinase pathway. FEBS Lett 579: 236-240.
    • (2005) FEBS Lett , vol.579 , pp. 236-240
    • Dokladda, K.1    Green, K.A.2    Pan, D.A.3    Hardie, D.G.4
  • 45
    • 0033845499 scopus 로고    scopus 로고
    • Role of the cytoskeleton in rapid activation of CD11b/CD18 function and its subsequent downregulation in neutrophils
    • Anderson SI, Hotchin NA, Nash GB, (2000) Role of the cytoskeleton in rapid activation of CD11b/CD18 function and its subsequent downregulation in neutrophils. J Cell Sci 113: 2737-2745.
    • (2000) J Cell Sci , vol.113 , pp. 2737-2745
    • Anderson, S.I.1    Hotchin, N.A.2    Nash, G.B.3
  • 46
    • 0024801641 scopus 로고
    • Constitutive and stimulus-induced phosphorylation of CD11/CD18 leukocyte adhesion molecules
    • Chatila TA, Geha RS, Arnaout MA, (1989) Constitutive and stimulus-induced phosphorylation of CD11/CD18 leukocyte adhesion molecules. J Cell Biol 109: 3435-3444.
    • (1989) J Cell Biol , vol.109 , pp. 3435-3444
    • Chatila, T.A.1    Geha, R.S.2    Arnaout, M.A.3
  • 47
    • 0030459125 scopus 로고    scopus 로고
    • A role for phosphoinositide 3-kinase in the completion of macropinocytosis and phagocytosis by macrophages
    • Araki N, Johnson MT, Swanson JA, (1996) A role for phosphoinositide 3-kinase in the completion of macropinocytosis and phagocytosis by macrophages. J Cell Biol 135: 1249-1260.
    • (1996) J Cell Biol , vol.135 , pp. 1249-1260
    • Araki, N.1    Johnson, M.T.2    Swanson, J.A.3
  • 48
    • 82655173730 scopus 로고    scopus 로고
    • AMP-activated protein kinase enhances the phagocytic ability of macrophages and neutrophils
    • Bae HB, Zmijewski JW, Deshane JS, Tadie JM, Chaplin DD, et al. (2011) AMP-activated protein kinase enhances the phagocytic ability of macrophages and neutrophils. Faseb J 25: 4358-4368.
    • (2011) Faseb J , vol.25 , pp. 4358-4368
    • Bae, H.B.1    Zmijewski, J.W.2    Deshane, J.S.3    Tadie, J.M.4    Chaplin, D.D.5
  • 49
  • 50
    • 84859896425 scopus 로고    scopus 로고
    • Rage binds C1q and enhances C1q-mediated phagocytosis
    • Ma W, Rai V, Hudson BI, Song F, Schmidt AM, et al. (2012) Rage binds C1q and enhances C1q-mediated phagocytosis. Cell Immunol 274: 72-82.
    • (2012) Cell Immunol , vol.274 , pp. 72-82
    • Ma, W.1    Rai, V.2    Hudson, B.I.3    Song, F.4    Schmidt, A.M.5
  • 51
    • 12944289732 scopus 로고    scopus 로고
    • Ageing and plasma adiponectin concentration in apparently healthy males and females
    • Adamczak M, Rzepka E, Chudek J, Wiecek A, (2005) Ageing and plasma adiponectin concentration in apparently healthy males and females. Clin Endocrinol 62: 114-118.
    • (2005) Clin Endocrinol , vol.62 , pp. 114-118
    • Adamczak, M.1    Rzepka, E.2    Chudek, J.3    Wiecek, A.4
  • 53
    • 78650040592 scopus 로고    scopus 로고
    • The burden of obesity on infectious disease
    • Karlsson EA, Beck MA, (2010) The burden of obesity on infectious disease. Exp Biol Med 235: 1412-1424.
    • (2010) Exp Biol Med , vol.235 , pp. 1412-1424
    • Karlsson, E.A.1    Beck, M.A.2
  • 54
    • 0019971627 scopus 로고
    • A rapid one-step method for the isolation of human-granulocytes from whole-blood
    • Jepsen LV, Skottun T, (1982) A rapid one-step method for the isolation of human-granulocytes from whole-blood. Scand J Clin Lab Inv 42: 235-238.
    • (1982) Scand J Clin Lab Inv , vol.42 , pp. 235-238
    • Jepsen, L.V.1    Skottun, T.2


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