메뉴 건너뛰기




Volumn 186, Issue 11, 2011, Pages 6474-6484

Pre-B cell colony-enhancing factor (PBEF/Nampt/Visfatin) primes neutrophils for augmented respiratory burst activity through partial assembly of the NADPH oxidase

Author keywords

[No Author keywords available]

Indexed keywords

DAPORINAD; MITOGEN ACTIVATED PROTEIN KINASE P38; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE PHOSPHORIBOSYLTRANSFERASE; OXIDOREDUCTASE; PHOSPHATIDYLINOSITOL 3 KINASE; RAC PROTEIN; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE P40 SUBUNIT; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE P47 SUBUNIT; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE P67 SUBUNIT; THREONINE; UNCLASSIFIED DRUG;

EID: 79958071347     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1003706     Document Type: Article
Times cited : (21)

References (53)
  • 1
    • 0024465567 scopus 로고
    • An assessment of the effects of glucocorticoids on degranulation, chemotaxis, binding to vascular endothelium and formation of leukotriene B4 by purified human neutrophils
    • Schleimer, R. P., H. S. Freeland, S. P. Peters, K. E. Brown, and C. P. Derse. 1989. An assessment of the effects of glucocorticoids on degranulation, chemotaxis, binding to vascular endothelium and formation of leukotriene B4 by purified human neutrophils. J. Pharmacol. Exp. Ther. 250: 598-605.
    • (1989) J. Pharmacol. Exp. Ther. , vol.250 , pp. 598-605
    • Schleimer, R.P.1    Freeland, H.S.2    Peters, S.P.3    Brown, K.E.4    Derse, C.P.5
  • 2
    • 0042196164 scopus 로고    scopus 로고
    • Science review: Cell membrane expression (connectivity) regulates neutrophil delivery, function and clearance
    • Seely, A. J., J. L. Pascual, and N. V. Christou. 2003. Science review: cell membrane expression (connectivity) regulates neutrophil delivery, function and clearance. Crit. Care 7: 291-307.
    • (2003) Crit. Care , vol.7 , pp. 291-307
    • Seely, A.J.1    Pascual, J.L.2    Christou, N.V.3
  • 3
    • 0035043710 scopus 로고    scopus 로고
    • The neutrophil: Function and regulation in innate and humoral immunity
    • Burg, N. D., and M. H. Pillinger. 2001. The neutrophil: function and regulation in innate and humoral immunity. Clin. Immunol. 99: 7-17.
    • (2001) Clin. Immunol. , vol.99 , pp. 7-17
    • Burg, N.D.1    Pillinger, M.H.2
  • 6
    • 0015086829 scopus 로고
    • Enzymatic basis of metabolic stimulation in leucocytes during phagocytosis: The role of activated NADPH oxidase
    • Patriarca, P., R. Cramer, S. Moncalvo, F. Rossi, and D. Romeo. 1971. Enzymatic basis of metabolic stimulation in leucocytes during phagocytosis: the role of activated NADPH oxidase. Arch. Biochem. Biophys. 145: 255-262.
    • (1971) Arch. Biochem. Biophys. , vol.145 , pp. 255-262
    • Patriarca, P.1    Cramer, R.2    Moncalvo, S.3    Rossi, F.4    Romeo, D.5
  • 7
    • 0024215472 scopus 로고
    • Two cytosolic neutrophil oxidase components absent in autosomal chronic granulomatous disease
    • Volpp, B. D., W. M. Nauseef, and R. A. Clark. 1988. Two cytosolic neutrophil oxidase components absent in autosomal chronic granulomatous disease. Science 242: 1295-1297.
    • (1988) Science , vol.242 , pp. 1295-1297
    • Volpp, B.D.1    Nauseef, W.M.2    Clark, R.A.3
  • 8
    • 0024376120 scopus 로고
    • Recombinant 47-kilodalton cytosol factor restores NADPH oxidase in chronic granulomatous disease
    • Lomax, K. J., T. L. Leto, H. Nunoi, J. I. Gallin, and H. L. Malech. 1989. Recombinant 47-kilodalton cytosol factor restores NADPH oxidase in chronic granulomatous disease. Science 245: 409-412.
    • (1989) Science , vol.245 , pp. 409-412
    • Lomax, K.J.1    Leto, T.L.2    Nunoi, H.3    Gallin, J.I.4    Malech, H.L.5
  • 10
    • 0025165130 scopus 로고
    • Assembly and activation of the NADPH:O2 Oxidoreductase in human neutrophils after stimulation with phorbol myristate acetate
    • Ambruso, D. R., B. G. Bolscher, P. M. Stokman, A. J. Verhoeven, and D. Roos. 1990. Assembly and activation of the NADPH:O2 oxidoreductase in human neutrophils after stimulation with phorbol myristate acetate. J. Biol. Chem. 265: 924-930.
    • (1990) J. Biol. Chem. , vol.265 , pp. 924-930
    • Ambruso, D.R.1    Bolscher, B.G.2    Stokman, P.M.3    Verhoeven, A.J.4    Roos, D.5
  • 11
    • 0025259712 scopus 로고
    • Two cytosolic components of the human neutrophil respiratory burst oxidase translocate to the plasma membrane during cell activation
    • Clark, R. A., B. D. Volpp, K. G. Leidal, and W. M. Nauseef. 1990. Two cytosolic components of the human neutrophil respiratory burst oxidase translocate to the plasma membrane during cell activation. J. Clin. Invest. 85: 714-721.
    • (1990) J. Clin. Invest. , vol.85 , pp. 714-721
    • Clark, R.A.1    Volpp, B.D.2    Leidal, K.G.3    Nauseef, W.M.4
  • 12
    • 0242544055 scopus 로고    scopus 로고
    • Phagocytosis by neutrophils
    • DOI 10.1016/j.micinf.2003.09.014
    • Lee, W. L., R. E. Harrison, and S. Grinstein. 2003. Phagocytosis by neutrophils. Microbes Infect. 5: 1299-1306. (Pubitemid 37410243)
    • (2003) Microbes and Infection , vol.5 , Issue.14 , pp. 1299-1306
    • Lee, W.L.1    Harrison, R.E.2    Grinstein, S.3
  • 13
    • 0020633208 scopus 로고
    • Exposure of human neutrophils to chemotactic factors potentiates activation of the respiratory burst enzyme
    • Bender, J. G., L. C. McPhail, and D. E. Van Epps. 1983. Exposure of human neutrophils to chemotactic factors potentiates activation of the respiratory burst enzyme. J. Immunol. 130: 2316-2323.
    • (1983) J. Immunol. , vol.130 , pp. 2316-2323
    • Bender, J.G.1    McPhail, L.C.2    Van Epps, D.E.3
  • 14
    • 44449124774 scopus 로고    scopus 로고
    • Pre-B cell colony-enhancing factor (PBEF)/visfatin: A novel mediator of innate immunity
    • Luk, T., Z. Malam, and J. C. Marshall. 2008. Pre-B cell colony-enhancing factor (PBEF)/visfatin: a novel mediator of innate immunity. J. Leukoc. Biol. 83: 804-816.
    • (2008) J. Leukoc. Biol. , vol.83 , pp. 804-816
    • Luk, T.1    Malam, Z.2    Marshall, J.C.3
  • 15
    • 0035145516 scopus 로고    scopus 로고
    • Identification of a plasmid-encoded gene from Haemophilus ducreyi which confers NAD independence
    • Martin, P. R., R. J. Shea, and M. H. Mulks. 2001. Identification of a plasmid-encoded gene from Haemophilus ducreyi which confers NAD independence. J. Bacteriol. 183: 1168-1174.
    • (2001) J. Bacteriol. , vol.183 , pp. 1168-1174
    • Martin, P.R.1    Shea, R.J.2    Mulks, M.H.3
  • 16
    • 0036856578 scopus 로고    scopus 로고
    • Pre-B-cell colony-enhancing factor, whose expression is upregulated in activated lymphocytes, is a nicotinamide phosphoribosyltransferase, a cytosolic enzyme involved in NAD biosynthesis
    • Rongvaux, A., R. J. Shea, M. H. Mulks, D. Gigot, J. Urbain, O. Leo, and F. Andris. 2002. Pre-B-cell colony-enhancing factor, whose expression is upregulated in activated lymphocytes, is a nicotinamide phosphoribosyltransferase, a cytosolic enzyme involved in NAD biosynthesis. Eur. J. Immunol. 32: 3225-3234.
    • (2002) Eur. J. Immunol. , vol.32 , pp. 3225-3234
    • Rongvaux, A.1    Shea, R.J.2    Mulks, M.H.3    Gigot, D.4    Urbain, J.5    Leo, O.6    Andris, F.7
  • 18
    • 85047693796 scopus 로고    scopus 로고
    • Pre-B cell colony-enhancing factor inhibits neutrophil apoptosis in experimental inflammation and clinical sepsis
    • Jia, S. H., Y. Li, J. Parodo, A. Kapus, L. Fan, O. D. Rotstein, and J. C. Marshall. 2004. Pre-B cell colony-enhancing factor inhibits neutrophil apoptosis in experimental inflammation and clinical sepsis. J. Clin. Invest. 113: 1318-1327.
    • (2004) J. Clin. Invest. , vol.113 , pp. 1318-1327
    • Jia, S.H.1    Li, Y.2    Parodo, J.3    Kapus, A.4    Fan, L.5    Rotstein, O.D.6    Marshall, J.C.7
  • 19
    • 0032528510 scopus 로고    scopus 로고
    • The IL-1β-converting enzyme (caspase-1) inhibits apoptosis of inflammatory neutrophils through activation of IL-1b
    • Watson, R. W., O. D. Rotstein, J. Parodo, R. Bitar, and J. C. Marshall. 1998. The IL-1β-converting enzyme (caspase-1) inhibits apoptosis of inflammatory neutrophils through activation of IL-1b. J. Immunol. 161: 957-962.
    • (1998) J. Immunol. , vol.161 , pp. 957-962
    • Watson, R.W.1    Rotstein, O.D.2    Parodo, J.3    Bitar, R.4    Marshall, J.C.5
  • 20
    • 0027314958 scopus 로고
    • Further characterization of the neutrophil oxidative burst by flow cytometry
    • Smith, J. A., and M. J. Weidemann. 1993. Further characterization of the neutrophil oxidative burst by flow cytometry. J. Immunol. Methods 162: 261-268.
    • (1993) J. Immunol. Methods , vol.162 , pp. 261-268
    • Smith, J.A.1    Weidemann, M.J.2
  • 21
    • 0029863313 scopus 로고    scopus 로고
    • Isoluminol-enhanced chemiluminescence: A sensitive method to study the release of superoxide anion from human neutrophils
    • Lundqvist, H., and C. Dahlgren. 1996. Isoluminol-enhanced chemiluminescence: a sensitive method to study the release of superoxide anion from human neutrophils. Free Radic. Biol. Med. 20: 785-792.
    • (1996) Free Radic. Biol. Med. , vol.20 , pp. 785-792
    • Lundqvist, H.1    Dahlgren, C.2
  • 22
    • 0036083848 scopus 로고    scopus 로고
    • Osmotic stress activates Rac and Cdc42 in neutrophils: Role in hypertonicity-induced actin polymerization
    • Lewis, A., C. Di Ciano, O. D. Rotstein, and A. Kapus. 2002. Osmotic stress activates Rac and Cdc42 in neutrophils: role in hypertonicity-induced actin polymerization. Am. J. Physiol. Cell Physiol. 282: C271-C279.
    • (2002) Am. J. Physiol. Cell Physiol. , vol.282
    • Lewis, A.1    Di Ciano, C.2    Rotstein, O.D.3    Kapus, A.4
  • 23
    • 27644514297 scopus 로고    scopus 로고
    • Structural organization of the neutrophil NADPH oxidase: Phosphorylation and translocation during priming and activation
    • Sheppard, F. R., M. R. Kelher, E. E. Moore, N. J. McLaughlin, A. Banerjee, and C. C. Silliman. 2005. Structural organization of the neutrophil NADPH oxidase: phosphorylation and translocation during priming and activation. J. Leukoc. Biol. 78: 1025-1042.
    • (2005) J. Leukoc. Biol. , vol.78 , pp. 1025-1042
    • Sheppard, F.R.1    Kelher, M.R.2    Moore, E.E.3    McLaughlin, N.J.4    Banerjee, A.5    Silliman, C.C.6
  • 25
    • 3042695344 scopus 로고    scopus 로고
    • Distinct ligand-dependent roles for p38 MAPK in priming and activation of the neutrophil NADPH oxidase
    • Brown, G. E., M. Q. Stewart, S. A. Bissonnette, A. E. Elia, E. Wilker, and M. B. Yaffe. 2004. Distinct ligand-dependent roles for p38 MAPK in priming and activation of the neutrophil NADPH oxidase. J. Biol. Chem. 279: 27059-27068.
    • (2004) J. Biol. Chem. , vol.279 , pp. 27059-27068
    • Brown, G.E.1    Stewart, M.Q.2    Bissonnette, S.A.3    Elia, A.E.4    Wilker, E.5    Yaffe, M.B.6
  • 26
    • 17844378221 scopus 로고    scopus 로고
    • Clinically relevant osmolar stress inhibits priming-induced PMN NADPH oxidase subunit translocation
    • discussion 757
    • Sheppard, F. R., E. E. Moore, N. McLaughlin, M. Kelher, J. L. Johnson, and C. C. Silliman. 2005. Clinically relevant osmolar stress inhibits priming-induced PMN NADPH oxidase subunit translocation. J. Trauma 58: 752-757, discussion 757.
    • (2005) J. Trauma , vol.58 , pp. 752-757
    • Sheppard, F.R.1    Moore, E.E.2    McLaughlin, N.3    Kelher, M.4    Johnson, J.L.5    Silliman, C.C.6
  • 28
    • 0026335622 scopus 로고
    • Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac 2
    • Knaus, U. G., P. G. Heyworth, T. Evans, J. T. Curnutte, and G. M. Bokoch. 1991. Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac 2. Science 254: 1512-1515.
    • (1991) Science , vol.254 , pp. 1512-1515
    • Knaus, U.G.1    Heyworth, P.G.2    Evans, T.3    Curnutte, J.T.4    Bokoch, G.M.5
  • 29
    • 0027067903 scopus 로고
    • Purification and characterization of Rac 2: A cytosolic GTP-binding protein that regulates human neutrophil NADPH oxidase
    • Knaus, U. G., P. G. Heyworth, B. T. Kinsella, J. T. Curnutte, and G. M. Bokoch. 1992. Purification and characterization of Rac 2: a cytosolic GTP-binding protein that regulates human neutrophil NADPH oxidase. J. Biol. Chem. 267: 23575-23582.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23575-23582
    • Knaus, U.G.1    Heyworth, P.G.2    Kinsella, B.T.3    Curnutte, J.T.4    Bokoch, G.M.5
  • 30
    • 0030694534 scopus 로고    scopus 로고
    • The 40-kDa component of the phagocyte NADPH oxidase (p40phox) is phosphorylated during activation in differentiated HL60 cells
    • Fuchs, A., A. P. Bouin, T. Rabilloud, and P. V. Vignais. 1997. The 40-kDa component of the phagocyte NADPH oxidase (p40phox) is phosphorylated during activation in differentiated HL60 cells. Eur. J. Biochem. 249: 531-539.
    • (1997) Eur. J. Biochem. , vol.249 , pp. 531-539
    • Fuchs, A.1    Bouin, A.P.2    Rabilloud, T.3    Vignais, P.V.4
  • 31
    • 0032514915 scopus 로고    scopus 로고
    • p40phox is phosphorylated on threonine 154 and serine 315 during activation of the phagocyte NADPH oxidase: Implication of a protein kinase c-type kinase in the phosphorylation process
    • Bouin, A. P., N. Grandvaux, P. V. Vignais, and A. Fuchs. 1998. p40phox is phosphorylated on threonine 154 and serine 315 during activation of the phagocyte NADPH oxidase: implication of a protein kinase c-type kinase in the phosphorylation process. J. Biol. Chem. 273: 30097-30103.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30097-30103
    • Bouin, A.P.1    Grandvaux, N.2    Vignais, P.V.3    Fuchs, A.4
  • 33
    • 0034234752 scopus 로고    scopus 로고
    • phoxfor flavocytochrome b558
    • phox for flavocytochrome b558. Biochem. J. 349: 113-117.
    • (2000) Biochem. J. , vol.349 , pp. 113-117
    • Cross, A.R.1
  • 34
    • 70349567934 scopus 로고    scopus 로고
    • phoxin reactive oxygen species production in microvascular endothelial cells
    • phox in reactive oxygen species production in microvascular endothelial cells. Arterioscler. Thromb. Vasc. Biol. 29: 1651-1656.
    • (2009) Arterioscler. Thromb. Vasc. Biol. , vol.29 , pp. 1651-1656
    • Fan, L.M.1    Teng, L.2    Li, J.M.3
  • 37
    • 0037105528 scopus 로고    scopus 로고
    • Regulation of phosphatidylinositol 3- kinase activity and phosphatidylinositol 3,4,5-trisphosphate accumulation by neutrophil priming agents
    • Cadwallader, K. A., A. M. Condliffe, A. McGregor, T. R. Walker, J. F. White, L. R. Stephens, and E. R. Chilvers. 2002. Regulation of phosphatidylinositol 3- kinase activity and phosphatidylinositol 3,4,5-trisphosphate accumulation by neutrophil priming agents. J. Immunol. 169: 3336-3344.
    • (2002) J. Immunol. , vol.169 , pp. 3336-3344
    • Cadwallader, K.A.1    Condliffe, A.M.2    McGregor, A.3    Walker, T.R.4    White, J.F.5    Stephens, L.R.6    Chilvers, E.R.7
  • 38
    • 33747624726 scopus 로고    scopus 로고
    • Crystal structure of visfatin/pre-B cell colony-enhancing factor 1/nicotinamide phosphoribosyl-transferase, free and in complex with the anti-cancer agent FK-866
    • Kim, M. K., J. H. Lee, H. Kim, S. J. Park, S. H. Kim, G. B. Kang, Y. S. Lee, J. B. Kim, K. K. Kim, S. W. Suh, and S. H. Eom. 2006. Crystal structure of visfatin/pre-B cell colony-enhancing factor 1/nicotinamide phosphoribosyl- transferase, free and in complex with the anti-cancer agent FK-866. J. Mol. Biol. 362: 66-77.
    • (2006) J. Mol. Biol. , vol.362 , pp. 66-77
    • Kim, M.K.1    Lee, J.H.2    Kim, H.3    Park, S.J.4    Kim, S.H.5    Kang, G.B.6    Lee, Y.S.7    Kim, J.B.8    Kim, K.K.9    Suh, S.W.10    Eom, S.H.11
  • 39
    • 0242460541 scopus 로고    scopus 로고
    • Regulation of the neutrophil-mediated inflammatory response to infection
    • Kobayashi, S. D., J. M. Voyich, and F. R. DeLeo. 2003. Regulation of the neutrophil-mediated inflammatory response to infection. Microbes Infect. 5: 1337-1344.
    • (2003) Microbes Infect. , vol.5 , pp. 1337-1344
    • Kobayashi, S.D.1    Voyich, J.M.2    DeLeo, F.R.3
  • 40
    • 0025907122 scopus 로고
    • Respiratory burst capability of polymorphonuclear neutrophils and TNF-α serum levels in relationship to the development of septic syndrome in critically ill patients
    • Trautinger, F., A. F. Hammerle, G. Pöschl, and M. Micksche. 1991. Respiratory burst capability of polymorphonuclear neutrophils and TNF-α serum levels in relationship to the development of septic syndrome in critically ill patients. J. Leukoc. Biol. 49: 449-454.
    • (1991) J. Leukoc. Biol. , vol.49 , pp. 449-454
    • Trautinger, F.1    Hammerle, A.F.2    Pöschl, G.3    Micksche, M.4
  • 41
    • 0141889087 scopus 로고    scopus 로고
    • phox is a common event of priming of human neutrophils by TNF-α and granulocyte-macrophage colony-stimulating factor
    • phox is a common event of priming of human neutrophils by TNF-α and granulocyte-macrophage colony-stimulating factor. J. Immunol. 171: 4392-4398.
    • (2003) J. Immunol. , vol.171 , pp. 4392-4398
    • Dewas, C.1    Dang, P.M.2    Gougerot-Pocidalo, M.A.3    El-Benna, J.4
  • 42
    • 0029859916 scopus 로고    scopus 로고
    • Demonstration of reversible priming of human neutrophils using platelet-activating factor
    • Kitchen, E., A. G. Rossi, A. M. Condliffe, C. Haslett, and E. R. Chilvers. 1996. Demonstration of reversible priming of human neutrophils using platelet-activating factor. Blood 88: 4330-4337.
    • (1996) Blood , vol.88 , pp. 4330-4337
    • Kitchen, E.1    Rossi, A.G.2    Condliffe, A.M.3    Haslett, C.4    Chilvers, E.R.5
  • 43
    • 0032733897 scopus 로고    scopus 로고
    • Phosphorylation of p40-phox during activation of neutrophil NADPH oxidase
    • Someya, A., H. Nunoi, T. Hasebe, and I. Nagaoka. 1999. Phosphorylation of p40-phox during activation of neutrophil NADPH oxidase. J. Leukoc. Biol. 66: 851-857.
    • (1999) J. Leukoc. Biol. , vol.66 , pp. 851-857
    • Someya, A.1    Nunoi, H.2    Hasebe, T.3    Nagaoka, I.4
  • 44
    • 1642619114 scopus 로고    scopus 로고
    • Increased gene expression of a cytokine-related molecule and profilin after activation of Suberites domuncula cells with xenogeneic sponge molecule(s)
    • DOI 10.1089/104454999314746
    • Müller, W. E., S. Perovic, J. Wilkesman, M. Kruse, I. M. Müller, and R. Batel. 1999. Increased gene expression of a cytokine-related molecule and profilin after activation of Suberites domuncula cells with xenogeneic sponge molecule(s). DNA Cell Biol. 18: 885-893. (Pubitemid 30013441)
    • (1999) DNA and Cell Biology , vol.18 , Issue.12 , pp. 885-893
    • Muller, W.E.G.1    Perovic, S.2    Wilkesman, J.3    Kruse, M.4    Muller, I.M.5    Batel, R.6
  • 46
    • 0027958452 scopus 로고
    • Cloning and characterization of the cDNA encoding a novel human pre-B-cell colony-enhancing factor
    • Samal, B., Y. Sun, G. Stearns, C. Xie, S. Suggs, and I. McNiece. 1994. Cloning and characterization of the cDNA encoding a novel human pre-B-cell colony-enhancing factor. Mol. Cell. Biol. 14: 1431-1437.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1431-1437
    • Samal, B.1    Sun, Y.2    Stearns, G.3    Xie, C.4    Suggs, S.5    McNiece, I.6
  • 48
    • 60749115555 scopus 로고    scopus 로고
    • Circulating visfatin in chronic obstructive pulmonary disease
    • Liu, X., Y. Ji, J. Chen, S. Li, and F. Luo. 2009. Circulating visfatin in chronic obstructive pulmonary disease. Nutrition 25: 373-378.
    • (2009) Nutrition , vol.25 , pp. 373-378
    • Liu, X.1    Ji, Y.2    Chen, J.3    Li, S.4    Luo, F.5
  • 49
    • 55749103395 scopus 로고    scopus 로고
    • Visfatin/pre- B cell colony-enhancing factor in amniotic fluid in normal pregnancy, spontaneous labor at term, preterm labor and prelabor rupture of membranes: An association with subclinical intrauterine infection in preterm parturition
    • Mazaki-Tovi, S., R. Romero, J. P. Kusanovic, O. Erez, F. Gotsch, P. Mittal, N. G. Than, C. L. Nhan-Chang, N. Hamill, E. Vaisbuch, et al. 2008. Visfatin/pre- B cell colony-enhancing factor in amniotic fluid in normal pregnancy, spontaneous labor at term, preterm labor and prelabor rupture of membranes: an association with subclinical intrauterine infection in preterm parturition. J. Perinat. Med. 36: 485-496.
    • (2008) J. Perinat. Med. , vol.36 , pp. 485-496
    • Mazaki-Tovi, S.1    Romero, R.2    Kusanovic, J.P.3    Erez, O.4    Gotsch, F.5    Mittal, P.6    Than, N.G.7    Nhan-Chang, C.L.8    Hamill, N.9    Vaisbuch, E.10
  • 50
    • 33747786726 scopus 로고    scopus 로고
    • Changes in plasma levels of fat-derived hormones adiponectin, leptin, resistin and visfatin in patients with rheumatoid arthritis
    • Otero, M., R. Lago, R. Gomez, F. Lago, C. Dieguez, J. J. Gómez-Reino, and O. Gualillo. 2006. Changes in plasma levels of fat-derived hormones adiponectin, leptin, resistin and visfatin in patients with rheumatoid arthritis. Ann. Rheum. Dis. 65: 1198-1201.
    • (2006) Ann. Rheum. Dis. , vol.65 , pp. 1198-1201
    • Otero, M.1    Lago, R.2    Gomez, R.3    Lago, F.4    Dieguez, C.5    Gómez-Reino, J.J.6    Gualillo, O.7
  • 51
    • 65649107670 scopus 로고    scopus 로고
    • Visfatin stimulates production of monocyte chemotactic protein-1 and interleukin-6 in human vein umbilical endothelial cells
    • Liu, S. W., S. B. Qiao, J. S. Yuan, and D. Q. Liu. 2009. Visfatin stimulates production of monocyte chemotactic protein-1 and interleukin-6 in human vein umbilical endothelial cells. Horm. Metab. Res. 41: 281-286.
    • (2009) Horm. Metab. Res. , vol.41 , pp. 281-286
    • Liu, S.W.1    Qiao, S.B.2    Yuan, J.S.3    Liu, D.Q.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.