메뉴 건너뛰기




Volumn 189, Issue 4, 2012, Pages 2017-2022

Identification of hemopexin as an anti-inflammatory factor that inhibits synergy of hemoglobin with HMGB1 in sterile and infectious inflammation

Author keywords

[No Author keywords available]

Indexed keywords

ADVANCED GLYCATION END PRODUCT RECEPTOR; HEMOGLOBIN; HEMOPEXIN; HIGH MOBILITY GROUP B1 PROTEIN; INTERLEUKIN 6; MYELOID DIFFERENTIATION FACTOR 88; PROTEIN KINASE SYK; REACTIVE OXYGEN METABOLITE; TOLL LIKE RECEPTOR 2; TOLL LIKE RECEPTOR 4; TOLL LIKE RECEPTOR ADAPTOR MOLECULE 1; TUMOR NECROSIS FACTOR;

EID: 84864809340     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1103623     Document Type: Article
Times cited : (81)

References (40)
  • 1
    • 0028690483 scopus 로고
    • Hemoglobin: A newly recognized binding protein for bacterial endotoxins (LPS)
    • Roth, R. I., W. Kaca, and J. Levin. 1994. Hemoglobin: a newly recognized binding protein for bacterial endotoxins (LPS). Prog. Clin. Biol. Res. 388: 161-172.
    • (1994) Prog. Clin. Biol. Res. , vol.388 , pp. 161-172
    • Roth, R.I.1    Kaca, W.2    Levin, J.3
  • 2
    • 0030984960 scopus 로고    scopus 로고
    • Hemoglobin increases mortality from bacterial endotoxin
    • Su, D., R. I. Roth, M. Yoshida, and J. Levin. 1997. Hemoglobin increases mortality from bacterial endotoxin. Infect. Immun. 65: 1258-1266. (Pubitemid 27146611)
    • (1997) Infection and Immunity , vol.65 , Issue.4 , pp. 1258-1266
    • Su, D.1    Roth, R.I.2    Yoshida, M.3    Levin, J.4
  • 3
    • 0028131671 scopus 로고
    • Hemoglobin, a newly recognized lipopolysaccharide (LPS)-binding protein that enhances LPS biological activity
    • Kaca, W., R. I. Roth, and J. Levin. 1994. Hemoglobin, a newly recognized lipopolysaccharide (LPS)-binding protein that enhances LPS biological activity. J. Biol. Chem. 269: 25078-25084. (Pubitemid 24311778)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.40 , pp. 25078-25084
    • Kaca, W.1    Roth, R.I.2    Levin, J.3
  • 4
    • 34548763155 scopus 로고    scopus 로고
    • Hemoglobin and LPS act in synergy to amplify the inflammatory response
    • Bodet, C., F. Chandad, and D. Grenier. 2007. Hemoglobin and LPS act in synergy to amplify the inflammatory response. J. Dent. Res. 86: 878-882.
    • (2007) J. Dent. Res. , vol.86 , pp. 878-882
    • Bodet, C.1    Chandad, F.2    Grenier, D.3
  • 8
    • 77954699484 scopus 로고    scopus 로고
    • Synergistic inflammation is induced by blood degradation products with microbial Toll-like receptor agonists and is blocked by hemopexin
    • Lin, T., Y. H. Kwak, F. Sammy, P. He, S. Thundivalappil, G. Sun, W. Chao, and H. S. Warren. 2010. Synergistic inflammation is induced by blood degradation products with microbial Toll-like receptor agonists and is blocked by hemopexin. J. Infect. Dis. 202: 624-632.
    • (2010) J. Infect. Dis. , vol.202 , pp. 624-632
    • Lin, T.1    Kwak, Y.H.2    Sammy, F.3    He, P.4    Thundivalappil, S.5    Sun, G.6    Chao, W.7    Warren, H.S.8
  • 9
    • 0015980699 scopus 로고
    • Transfer of heme from ferrihemoglobin and ferrihemoglobin isolated chains to hemopexin
    • Hrkal, Z., Z. Vodrázka, and I. Kalousek. 1974. Transfer of heme from ferrihemoglobin and ferrihemoglobin isolated chains to hemopexin. Eur. J. Biochem. 43: 73-78.
    • (1974) Eur. J. Biochem. , vol.43 , pp. 73-78
    • Hrkal, Z.1    Vodrázka, Z.2    Kalousek, I.3
  • 10
    • 0036259938 scopus 로고    scopus 로고
    • Hemopexin: Structure, function, and regulation
    • DOI 10.1089/104454902753759717
    • Tolosano, E., and F. Altruda. 2002. Hemopexin: structure, function, and regulation. DNA Cell Biol. 21: 297-306. (Pubitemid 34594543)
    • (2002) DNA and Cell Biology , vol.21 , Issue.4 , pp. 297-306
    • Tolosano, E.1    Altruda, F.2
  • 11
    • 79953066407 scopus 로고    scopus 로고
    • HMGB1 is a therapeutic target for sterile inflammation and infection
    • Andersson, U., and K. J. Tracey. 2011. HMGB1 is a therapeutic target for sterile inflammation and infection. Annu. Rev. Immunol. 29: 139-162.
    • (2011) Annu. Rev. Immunol. , vol.29 , pp. 139-162
    • Andersson, U.1    Tracey, K.J.2
  • 15
    • 4544361769 scopus 로고    scopus 로고
    • Purification and characterization of human hemoglobin: Effect of the hemolysis conditions
    • DOI 10.1016/j.ijbiomac.2004.05.003, PII S0141813004000364
    • Andrade, C. T., L. A. Barros, M. C. Lima, and E. G. Azero. 2004. Purification and characterization of human hemoglobin: effect of the hemolysis conditions. Int. J. Biol. Macromol. 34: 233-240. (Pubitemid 39220858)
    • (2004) International Journal of Biological Macromolecules , vol.34 , Issue.4 , pp. 233-240
    • Andrade, C.T.1    Barros, L.A.M.2    Lima, M.C.P.3    Azero, E.G.4
  • 17
    • 0021940486 scopus 로고
    • Turbidimetric method for quantifying serum inhibition of Limulus amoebocyte lysate
    • Novitsky, T. J., P. F. Roslansky, G. R. Siber, and H. S. Warren. 1985. A turbidometric method for quantifying serum inhibition of limulus amoebocyte lysate response. J. Clin. Microbiol. 20: 211-216. (Pubitemid 15161115)
    • (1985) Journal of Clinical Microbiology , vol.21 , Issue.2 , pp. 211-216
    • Novitsky, T.J.1    Roslansky, P.F.2    Siber, G.R.3    Warren, H.S.4
  • 18
    • 0037111523 scopus 로고    scopus 로고
    • Toll-like receptor 4 and Toll-IL-1 receptor domain-containing adapter protein (TIRAP)/myeloid differentiation protein 88 adapter-like (Mal) contribute to maximal IL-6 expression in macrophages
    • Schilling, D., K. Thomas, K. Nixdorff, S. N. Vogel, and M. J. Fenton. 2002. Toll-like receptor 4 and Toll-IL-1 receptor domain-containing adapter protein (TIRAP)/myeloid differentiation protein 88 adapter-like (Mal) contribute to maximal IL-6 expression in macrophages. J. Immunol. 169: 5874-5880. (Pubitemid 35291692)
    • (2002) Journal of Immunology , vol.169 , Issue.10 , pp. 5874-5880
    • Schilling, D.1    Thomas, K.2    Nixdorff, K.3    Vogel, S.N.4    Fenton, M.J.5
  • 19
    • 33846207958 scopus 로고    scopus 로고
    • MyD88-dependent and MyD88-independent pathways in synergy, priming, and tolerance between TLR agonists
    • Bagchi, A., E. A. Herrup, H. S. Warren, J. Trigilio, H. S. Shin, C. Valentine, and J. Hellman. 2007. MyD88-dependent and MyD88-independent pathways in synergy, priming, and tolerance between TLR agonists. J. Immunol. 178: 1164-1171. (Pubitemid 46095190)
    • (2007) Journal of Immunology , vol.178 , Issue.2 , pp. 1164-1171
    • Bagchi, A.1    Herrup, E.A.2    Warren, H.S.3    Trigilio, J.4    Shin, H.-S.5    Valentine, C.6    Hellman, J.7
  • 20
    • 0032825215 scopus 로고    scopus 로고
    • Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two beta-propeller domains
    • DOI 10.1038/13294
    • Paoli, M., B. F. Anderson, H. M. Baker, W. T. Morgan, A. Smith, and E. N. Baker. 1999. Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two beta-propeller domains. Nat. Struct. Biol. 6: 926-931. (Pubitemid 29463305)
    • (1999) Nature Structural Biology , vol.6 , Issue.10 , pp. 926-931
    • Paoli, M.1    Anderson, B.F.2    Baker, H.M.3    Morgan, W.T.4    Smith, A.5    Baker, E.N.6
  • 21
    • 67650563915 scopus 로고    scopus 로고
    • Hemoglobin and its scavenger protein haptoglobin associate with apoA-1-containing particles and influence the inflammatory properties and function of high density lipoprotein
    • Watanabe, J., V. Grijalva, S. Hama, K. Barbour, F. G. Berger, M. Navab, A. M. Fogelman, and S. T. Reddy. 2009. Hemoglobin and its scavenger protein haptoglobin associate with apoA-1-containing particles and influence the inflammatory properties and function of high density lipoprotein. J. Biol. Chem. 284: 18292-18301.
    • (2009) J. Biol. Chem. , vol.284 , pp. 18292-18301
    • Watanabe, J.1    Grijalva, V.2    Hama, S.3    Barbour, K.4    Berger, F.G.5    Navab, M.6    Fogelman, A.M.7    Reddy, S.T.8
  • 23
    • 80054799282 scopus 로고    scopus 로고
    • Delineation of lipopolysaccharide (LPS)-binding sites on hemoglobin: From in silico predictions to biophysical characterization
    • Bahl, N., R. Du, I. Winarsih, B. Ho, L. Tucker-Kellogg, B. Tidor, and J. L. Ding. 2011. Delineation of lipopolysaccharide (LPS)-binding sites on hemoglobin: from in silico predictions to biophysical characterization. J. Biol. Chem. 286: 37793-37803.
    • (2011) J. Biol. Chem. , vol.286 , pp. 37793-37803
    • Bahl, N.1    Du, R.2    Winarsih, I.3    Ho, B.4    Tucker-Kellogg, L.5    Tidor, B.6    Ding, J.L.7
  • 24
    • 28944452535 scopus 로고    scopus 로고
    • Toll-like receptors
    • DOI 10.1097/01.CCM.0000185504.39347.5D
    • Warren, H. S. 2005. Toll-like receptors. Crit. Care Med. 33(Suppl. 12): S457-S459. (Pubitemid 41785987)
    • (2005) Critical Care Medicine , vol.33 , Issue.12 SUPPL.
    • Warren, H.S.1
  • 26
    • 70149090632 scopus 로고    scopus 로고
    • CC chemokine ligand-2 synergizes with the nonchemokine G protein-coupled receptor ligand fMLP in monocyte chemotaxis, and it cooperates with the TLR ligand LPS via induction of CXCL8
    • Gouwy, M., S. Struyf, H. Verbeke, W. Put, P. Proost, G. Opdenakker, and J. Van Damme. 2009. CC chemokine ligand-2 synergizes with the nonchemokine G protein-coupled receptor ligand fMLP in monocyte chemotaxis, and it cooperates with the TLR ligand LPS via induction of CXCL8. J. Leukoc. Biol. 86: 671-680.
    • (2009) J. Leukoc. Biol. , vol.86 , pp. 671-680
    • Gouwy, M.1    Struyf, S.2    Verbeke, H.3    Put, W.4    Proost, P.5    Opdenakker, G.6    Van Damme, J.7
  • 27
    • 65449133935 scopus 로고    scopus 로고
    • Human dendritic cells stimulated via TLR7 and/or TLR8 induce the sequential production of Il-10, IFN-gamma, and IL-17A by naive CD4+ T cells
    • Lombardi, V., L. Van Overtvelt, S. Horiot, and P. Moingeon. 2009. Human dendritic cells stimulated via TLR7 and/or TLR8 induce the sequential production of Il-10, IFN-gamma, and IL-17A by naive CD4+ T cells. J. Immunol. 182: 3372-3379.
    • (2009) J. Immunol. , vol.182 , pp. 3372-3379
    • Lombardi, V.1    Van Overtvelt, L.2    Horiot, S.3    Moingeon, P.4
  • 28
    • 48649107478 scopus 로고    scopus 로고
    • Doublestranded RNA- and CpG DNA-induced immune responses in Atlantic salmon: Comparison and synergies
    • Strandskog, G., I. Skjaeveland, T. Ellingsen, and J. B. Jørgensen. 2008. Doublestranded RNA- and CpG DNA-induced immune responses in Atlantic salmon: comparison and synergies. Vaccine 26: 4704-4715.
    • (2008) Vaccine , vol.26 , pp. 4704-4715
    • Strandskog, G.1    Skjaeveland, I.2    Ellingsen, T.3    Jørgensen, J.B.4
  • 30
    • 34247179499 scopus 로고    scopus 로고
    • Synergy of CpG oligodeoxynucleotide and double-stranded RNA (poly I:C) on nitric oxide induction in chicken peripheral blood monocytes
    • DOI 10.1016/j.molimm.2007.01.034, PII S0161589007000533
    • He, H., K. J. Genovese, D. J. Nisbet, and M. H. Kogut. 2007. Synergy of CpG oligodeoxynucleotide and double-stranded RNA (poly I:C) on nitric oxide induction in chicken peripheral blood monocytes. Mol. Immunol. 44: 3234-3242. (Pubitemid 46610502)
    • (2007) Molecular Immunology , vol.44 , Issue.12 , pp. 3234-3242
    • He, H.1    Genovese, K.J.2    Nisbet, D.J.3    Kogut, M.H.4
  • 31
    • 23644449245 scopus 로고    scopus 로고
    • The expression of Toll-like receptors 3 and 7 in rheumatoid arthritis synovium is increased and costimulation of Toll-like receptors 3, 4, and 7/8 results in synergistic cytokine production by dendritic cells
    • DOI 10.1002/art.21278
    • Roelofs, M. F., L. A. Joosten, S. Abdollahi-Roodsaz, A. W. van Lieshout, T. Sprong, F. H. van den Hoogen, W. B. van den Berg, and T. R. Radstake. 2005. The expression of toll-like receptors 3 and 7 in rheumatoid arthritis synovium is increased and costimulation of toll-like receptors 3, 4, and 7/8 results in synergistic cytokine production by dendritic cells. Arthritis Rheum. 52: 2313-2322. (Pubitemid 41117415)
    • (2005) Arthritis and Rheumatism , vol.52 , Issue.8 , pp. 2313-2322
    • Roelofs, M.F.1    Joosten, L.A.B.2    Abdollahi-Roodsaz, S.3    Van Lieshout, A.W.T.4    Sprong, T.5    Van Den, H.F.H.6    Van Den, B.W.B.7    Radstake, T.R.D.J.8
  • 32
    • 23944489407 scopus 로고    scopus 로고
    • Selected Toll-like receptor agonist combinations synergistically trigger a T helper type 1 -polarizing program in dendritic cells
    • DOI 10.1038/ni1223, PII N1223
    • Napolitani, G., A. Rinaldi, F. Bertoni, F. Sallusto, and A. Lanzavecchia. 2005. Selected Toll-like receptor agonist combinations synergistically trigger a T helper type 1-polarizing program in dendritic cells. Nat. Immunol. 6: 769-776. (Pubitemid 43090462)
    • (2005) Nature Immunology , vol.6 , Issue.8 , pp. 769-776
    • Napolitani, G.1    Rinaldi, A.2    Bertoni, F.3    Sallusto, F.4    Lanzavecchia, A.5
  • 33
    • 0343360868 scopus 로고    scopus 로고
    • A multicenter, randomized, controlled clinical trial of transfusion requirements in critical care
    • DOI 10.1056/NEJM199902113400601
    • Hébert, P. C., G. Wells, M. A. Blajchman, J. Marshall, C. Martin, G. Pagliarello, M. Tweeddale, I. Schweitzer, and E. Yetisir. 1999. A multicenter, randomized, controlled clinical trial of transfusion requirements in critical care. Transfusion Requirements in Critical Care Investigators, Canadian Critical Care Trials Group. N. Engl. J. Med. 340: 409-417. (Pubitemid 29084771)
    • (1999) New England Journal of Medicine , vol.340 , Issue.6 , pp. 409-417
    • Hebert, P.C.1    Wells, G.2    Blajchman, M.A.3    Marshall, J.4    Martin, C.5    Pagliarello, G.6    Tweeddale, M.7    Schweitzer, I.8    Yetisir, E.9
  • 35
    • 84055177595 scopus 로고    scopus 로고
    • Transfusion of human volunteers with older, stored red blood cells produces extravascular hemolysis and circulating non-transferrin-bound iron
    • Hod, E. A., G. M. Brittenham, G. B. Billote, R. O. Francis, Y. Z. Ginzburg, J. E. Hendrickson, J. Jhang, J. Schwartz, S. Sharma, S. Sheth, et al. 2011. Transfusion of human volunteers with older, stored red blood cells produces extravascular hemolysis and circulating non-transferrin-bound iron. Blood 118: 6675-6682.
    • (2011) Blood , vol.118 , pp. 6675-6682
    • Hod, E.A.1    Brittenham, G.M.2    Billote, G.B.3    Francis, R.O.4    Ginzburg, Y.Z.5    Hendrickson, J.E.6    Jhang, J.7    Schwartz, J.8    Sharma, S.9    Sheth, S.10
  • 37
    • 79952316970 scopus 로고    scopus 로고
    • Red blood cell transfusion, feeding and necrotizing enterocolitis in preterm infants
    • El-Dib, M., S. Narang, E. Lee, A. N. Massaro, and H. Aly. 2011. Red blood cell transfusion, feeding and necrotizing enterocolitis in preterm infants. J. Perinatol. 31: 183-187.
    • (2011) J. Perinatol. , vol.31 , pp. 183-187
    • El-Dib, M.1    Narang, S.2    Lee, E.3    Massaro, A.N.4    Aly, H.5
  • 38
    • 0043268709 scopus 로고    scopus 로고
    • Heme oxygenase-1: Unleashing the protective properties of heme
    • DOI 10.1016/S1471-4906(03)00181-9
    • Otterbein, L. E., M. P. Soares, K. Yamashita, and F. H. Bach. 2003. Heme oxygenase-1: unleashing the protective properties of heme. Trends Immunol. 24: 449-455. (Pubitemid 36928103)
    • (2003) Trends in Immunology , vol.24 , Issue.8 , pp. 449-455
    • Otterbein, L.E.1    Soares, M.P.2    Yamashita, K.3    Bach, F.H.4
  • 39
    • 0014360531 scopus 로고
    • Plasma concentrations of hemopexin, haptoglobin and heme in patients with various hemolytic diseases
    • Muller-Eberhard, U., J. Javid, H. H. Liem, A. Hanstein, and M. Hanna. 1968. Plasma concentrations of hemopexin, haptoglobin and heme in patients with various hemolytic diseases. Blood 32: 811-815.
    • (1968) Blood , vol.32 , pp. 811-815
    • Muller-Eberhard, U.1    Javid, J.2    Liem, H.H.3    Hanstein, A.4    Hanna, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.