메뉴 건너뛰기




Volumn 162, Issue 2, 1999, Pages 1064-1070

IL-12 is a heparin-binding cytokine

Author keywords

[No Author keywords available]

Indexed keywords

FIBROBLAST GROWTH FACTOR 2; GLYCOSAMINOGLYCAN; HEPARIN; HEPARIN LYASE; INTERLEUKIN 12;

EID: 0033555412     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (95)

References (39)
  • 1
    • 0025875022 scopus 로고
    • Cloning of cDNA for natural killer cell stimulatory factor, a heterodimeric cytokine with multiple effects on T and natural killer cells
    • Wolf, S. F., P. A. Temple, M. Kobayashi, D. Young, M. Dicig, L. Lowe, R. Dzialo, L. Fitz, C. Ferenz, R. M. Hewiek, et al. 1991. Cloning of cDNA for natural killer cell stimulatory factor, a heterodimeric cytokine with multiple effects on T and natural killer cells. J. Immunol. 146:3074.
    • (1991) J. Immunol. , vol.146 , pp. 3074
    • Wolf, S.F.1    Temple, P.A.2    Kobayashi, M.3    Young, D.4    Dicig, M.5    Lowe, L.6    Dzialo, R.7    Fitz, L.8    Ferenz, C.9    Hewiek, R.M.10
  • 3
    • 0028970060 scopus 로고
    • Interleukin-12: A proinflammatory cytokine with immunoregulalory functions that bridge innate resistance and antigen-specific adaptive immunity
    • Trinchieri, G. 1995. Interleukin-12: a proinflammatory cytokine with immunoregulalory functions that bridge innate resistance and antigen-specific adaptive immunity. Annu. Rev. Immunol. 13:251.
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 251
    • Trinchieri, G.1
  • 4
    • 0028303170 scopus 로고
    • Interleukin 12 synergizes with B7/CD28 interaction in inducing efficient proliferation and cytokine production of human T cells
    • Kubin, M., M. Kamoun, and G. Trinchieri. 1994. Interleukin 12 synergizes with B7/CD28 interaction in inducing efficient proliferation and cytokine production of human T cells. J. Exp. Med. 180:211.
    • (1994) J. Exp. Med. , vol.180 , pp. 211
    • Kubin, M.1    Kamoun, M.2    Trinchieri, G.3
  • 7
    • 0030002111 scopus 로고    scopus 로고
    • Genetically resistant mice lacking interleukin-12 are susceptible to infection with Leishmania major and mount a polarized Th2 cell response
    • Mattner, F., J. Magram, J. Ferrante, P. Launios, K. Di Padova, R. Behin, M. K. Gately, J. A. Louis, and G. Alber. 1996. Genetically resistant mice lacking interleukin-12 are susceptible to infection with Leishmania major and mount a polarized Th2 cell response. Eur. J. Immunol. 26:1553.
    • (1996) Eur. J. Immunol. , vol.26 , pp. 1553
    • Mattner, F.1    Magram, J.2    Ferrante, J.3    Launios, P.4    Di Padova, K.5    Behin, R.6    Gately, M.K.7    Louis, J.A.8    Alber, G.9
  • 9
    • 0029946526 scopus 로고    scopus 로고
    • Potential clinical applications of interleukin-12
    • Chougent, C., and G. M. Shearer. 1996. Potential clinical applications of interleukin-12. Curr. Opin. Hematol. 3:216.
    • (1996) Curr. Opin. Hematol. , vol.3 , pp. 216
    • Chougent, C.1    Shearer, G.M.2
  • 10
    • 0030959049 scopus 로고    scopus 로고
    • Interleukin-12 induction of the Th1 cytokines is important for viral clearance in chronic hepatitis B
    • Rossol, S., G. Marinas, P. Carucci, M. V. Singer, R. Williams, and N. V. Naoumov. 1997. Interleukin-12 induction of the Th1 cytokines is important for viral clearance in chronic hepatitis B. J. Clin. Invest. 99:3025.
    • (1997) J. Clin. Invest. , vol.99 , pp. 3025
    • Rossol, S.1    Marinas, G.2    Carucci, P.3    Singer, M.V.4    Williams, R.5    Naoumov, N.V.6
  • 11
    • 0025976609 scopus 로고
    • Interferon-γ binds to heparan sulfate by a cluster of amino acids located in the C-terminal part of the molecule
    • Lortat Jacob, H., and J.-A. Grimaud. 1991. Interferon-γ binds to heparan sulfate by a cluster of amino acids located in the C-terminal part of the molecule. FEBS Letts. 280:152.
    • (1991) FEBS Letts. , vol.280 , pp. 152
    • Lortat Jacob, H.1    Grimaud, J.-A.2
  • 12
    • 0029051004 scopus 로고
    • Molecular organisation of the interferon γ-binding domain in heparan sulphate
    • Lortat-Jacob, H., J. E. Turnbull, and J.-A. Grimaud. 1995. Molecular organisation of the interferon γ-binding domain in heparan sulphate. Biochem. J. 310:497.
    • (1995) Biochem. J. , vol.310 , pp. 497
    • Lortat-Jacob, H.1    Turnbull, J.E.2    Grimaud, J.-A.3
  • 13
    • 0031441834 scopus 로고    scopus 로고
    • Characterization of human recombinant interleukin 2 binding to heparin and heparan sulfate using an ELISA approach
    • Najjam, S., R. V. Gibbs, M. Y. Gordon, and C. C. Rider. 1997. Characterization of human recombinant interleukin 2 binding to heparin and heparan sulfate using an ELISA approach. Cytokine 9:1013.
    • (1997) Cytokine , vol.9 , pp. 1013
    • Najjam, S.1    Gibbs, R.V.2    Gordon, M.Y.3    Rider, C.C.4
  • 14
    • 0031798591 scopus 로고    scopus 로고
    • Further characterization of the binding of human recombinant interleukin 2 to heparin and identification of putative binding sites
    • Najjam, S., B. Mulloy, J. Theze, M. Gordon, R. Gibbs, and C. C. Rider. 1998. Further characterization of the binding of human recombinant interleukin 2 to heparin and identification of putative binding sites. Glycobiology. 8:509.
    • (1998) Glycobiology , vol.8 , pp. 509
    • Najjam, S.1    Mulloy, B.2    Theze, J.3    Gordon, M.4    Gibbs, R.5    Rider, C.C.6
  • 15
    • 0021179878 scopus 로고
    • Heparan sulfates from porcine intestinal mucosa: Preparation and physicochemical properties
    • Johnson, E. A. 1984. Heparan sulfates from porcine intestinal mucosa: preparation and physicochemical properties. Thrombosis Res. 35:583.
    • (1984) Thrombosis Res. , vol.35 , pp. 583
    • Johnson, E.A.1
  • 17
    • 0031616475 scopus 로고    scopus 로고
    • Analysis of glycosaminoglycans and proteoglycans
    • E. F. Hounsell, ed. The Humana Press, Totowa, NJ
    • Rider, C. C. 1998. Analysis of glycosaminoglycans and proteoglycans. In Methods in Molecular Biology, Vol. 76. Glycoanalysis Protocols. E. F. Hounsell, ed. The Humana Press, Totowa, NJ, p. 131-144.
    • (1998) Methods in Molecular Biology, Vol. 76. Glycoanalysis Protocols , vol.76 , pp. 131-144
    • Rider, C.C.1
  • 18
    • 0017189425 scopus 로고
    • Formation of anhydrosugars in the chemical depolymerisation of heparin
    • Shively, J. E., and H. E. Conrad. 1976. Formation of anhydrosugars in the chemical depolymerisation of heparin. Biochemistry 15:3932.
    • (1976) Biochemistry , vol.15 , pp. 3932
    • Shively, J.E.1    Conrad, H.E.2
  • 19
    • 0024021040 scopus 로고
    • Conformational flexibility: A new concept for explaining binding and biological properties of iduronic acid-containing glycosaminoglycans
    • Casu, B., M. Petitou, M. Provasoli, and P. Sinay. 1988. Conformational flexibility: a new concept for explaining binding and biological properties of iduronic acid-containing glycosaminoglycans. Trends Biochem. Sci. 13:221.
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 221
    • Casu, B.1    Petitou, M.2    Provasoli, M.3    Sinay, P.4
  • 20
    • 0026744148 scopus 로고
    • Cell surface heparan sulfate proteoglycans
    • Yanagishita, M., and V. C. Hascall. 1992. Cell surface heparan sulfate proteoglycans. J. Biol. Chem. 267:9451.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9451
    • Yanagishita, M.1    Hascall, V.C.2
  • 21
    • 0027494436 scopus 로고
    • A revised structure for fucoidan may explain some of its biological activities
    • Patankar, M. S., S. Oehninger, T. Barnett, R. L. Williams, and G. F. Clark. 1993. A revised structure for fucoidan may explain some of its biological activities. J. Biol. Chem. 268:21770.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21770
    • Patankar, M.S.1    Oehninger, S.2    Barnett, T.3    Williams, R.L.4    Clark, G.F.5
  • 23
    • 0027480740 scopus 로고
    • Structure and biological activities of a heparin-derived hexasaccharide with high affinity for basic fibroblast growth factor
    • Tyrell, D. J., M. Ishihara, R. Narasinga, A. Horne, M. C. Kiefer, G. B. Stauber, L. H. Lam, and R. J. Stack. 1993. Structure and biological activities of a heparin-derived hexasaccharide with high affinity for basic fibroblast growth factor. J. Biol. Chem. 268:4684.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4684
    • Tyrell, D.J.1    Ishihara, M.2    Narasinga, R.3    Horne, A.4    Kiefer, M.C.5    Stauber, G.B.6    Lam, L.H.7    Stack, R.J.8
  • 24
    • 0027448951 scopus 로고
    • Minimal sequence in heparin/heparan sulfate required for binding of basic fibroblast growth factor
    • Maccarana, M., B. Casu, and U. Lindahl. 1993. Minimal sequence in heparin/heparan sulfate required for binding of basic fibroblast growth factor. J. Biol. Chem. 268:23898.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23898
    • Maccarana, M.1    Casu, B.2    Lindahl, U.3
  • 25
    • 0026727774 scopus 로고
    • Identification of the basic fibroblast growth factor binding sequence in fibroblast heparan sulfate
    • Tumbull, J. E., D. G. Fernig, Y. Ke, M. C. Wilkinson, and J. T. Gallagher. 1992. Identification of the basic fibroblast growth factor binding sequence in fibroblast heparan sulfate. J. Biol. Chem. 267:10337.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10337
    • Tumbull, J.E.1    Fernig, D.G.2    Ke, Y.3    Wilkinson, M.C.4    Gallagher, J.T.5
  • 26
    • 0031051151 scopus 로고    scopus 로고
    • Structural differences and the presence of unsubstituted amino groups in heparan sulfates from different tissues and species
    • Toida, T., H. Yoshida, H. Toyoda, I. Koshiishi, T. Imanari, R. E. Hileman, J. R. Fromm, and R. J. Linhardt. 1997. Structural differences and the presence of unsubstituted amino groups in heparan sulfates from different tissues and species. Biochem. J. 322:499.
    • (1997) Biochem. J. , vol.322 , pp. 499
    • Toida, T.1    Yoshida, H.2    Toyoda, H.3    Koshiishi, I.4    Imanari, T.5    Hileman, R.E.6    Fromm, J.R.7    Linhardt, R.J.8
  • 28
    • 0030796217 scopus 로고    scopus 로고
    • Specific binding of the chemokine platelet factor 4 to heparan sulfate
    • Stringer, S. E., and J. T. Gallagher. 1997. Specific binding of the chemokine platelet factor 4 to heparan sulfate. J. Biol. Chem. 272:20508.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20508
    • Stringer, S.E.1    Gallagher, J.T.2
  • 29
    • 0026567028 scopus 로고
    • Sequence similarity between NSKSF and the IL-6/G-CSF family
    • Merberg, D. M., S. F. Wolf, and S.C. Clark. 1992. Sequence similarity between NSKSF and the IL-6/G-CSF family. Immunol. Today 13:77-78.
    • (1992) Immunol. Today , vol.13 , pp. 77-78
    • Merberg, D.M.1    Wolf, S.F.2    Clark, S.C.3
  • 30
    • 0025783528 scopus 로고
    • Homology of the p40 subunit of natural killer stimulatory factor (NKSF) with the extracellular domain of the interleukin-6 receptor
    • Gearing, D. P., and D. Cosman. 1991. Homology of the p40 subunit of natural killer stimulatory factor (NKSF) with the extracellular domain of the interleukin-6 receptor. Cell 66:9.
    • (1991) Cell , vol.66 , pp. 9
    • Gearing, D.P.1    Cosman, D.2
  • 31
    • 0028004630 scopus 로고
    • Glycosaminoglycan-protein interactions: A question of specificity
    • Spillman, D., and U. Lindahl. 1994. Glycosaminoglycan-protein interactions: a question of specificity. Curr. Opin. Struct. Biol. 4:677.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 677
    • Spillman, D.1    Lindahl, U.2
  • 34
    • 0028429960 scopus 로고
    • Differential binding of chemokines to glycosaminoglycan subpopulations
    • Witt, D.P., and A. Lander. 1994. Differential binding of chemokines to glycosaminoglycan subpopulations. Curr. Biol. 4:394.
    • (1994) Curr. Biol. , vol.4 , pp. 394
    • Witt, D.P.1    Lander, A.2
  • 35
    • 0027270899 scopus 로고
    • Heparin binding affinity of normal and genetically modified antithrombin III measured using a monoclonal antibody to the heparin binding site of antithrombin III
    • Watton, J., C. Longstaff, D. A. Lane, and T. W. Barrowcliffe. 1993. Heparin binding affinity of normal and genetically modified antithrombin III measured using a monoclonal antibody to the heparin binding site of antithrombin III. Biochemistry 32:7286.
    • (1993) Biochemistry , vol.32 , pp. 7286
    • Watton, J.1    Longstaff, C.2    Lane, D.A.3    Barrowcliffe, T.W.4
  • 36
    • 0025862954 scopus 로고
    • Analysis of affinity and structural selectivity in the binding of proteins to glycosaminoglycans: Development of a sensitive electrophoretic technique
    • Lee, M. K., and A. D. Lander. 1991. Analysis of affinity and structural selectivity in the binding of proteins to glycosaminoglycans: development of a sensitive electrophoretic technique. Proc. Natl. Acad. Sci. USA 88:2768.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2768
    • Lee, M.K.1    Lander, A.D.2
  • 37
    • 0002685325 scopus 로고
    • Intracellular proteoglycans of the immune system
    • T. N. Wight and R. P. Mehan, eds. Academic Press, Orlando, FL
    • Stevens, R.L. 1987. Intracellular proteoglycans of the immune system. In Biology of Proteoglycans. T. N. Wight and R. P. Mehan, eds. Academic Press, Orlando, FL. p. 367-387.
    • (1987) Biology of Proteoglycans , pp. 367-387
    • Stevens, R.L.1
  • 38
    • 0000060327 scopus 로고    scopus 로고
    • In vivo microbial stimulation induces rapid CD40 ligand independent production of interleukin 12 by dendritic cells and their redistribution to T cell areas
    • Reis e Sousa, C., S. Heiny, T. Scharton-Kersten, D. Jankovic, H. Charest, R. N. Germain, and A. Sher. 1997. In vivo microbial stimulation induces rapid CD40 ligand independent production of interleukin 12 by dendritic cells and their redistribution to T cell areas. J. Exp. Med. 186:1819.
    • (1997) J. Exp. Med. , vol.186 , pp. 1819
    • Reis E Sousa, C.1    Heiny, S.2    Scharton-Kersten, T.3    Jankovic, D.4    Charest, H.5    Germain, R.N.6    Sher, A.7
  • 39
    • 0028957492 scopus 로고
    • Mechanism of interleukin 12-mediated toxicities during experimental viral infections: Role of tumor necrosis factor and glucocorticoids
    • Orange, J. S., T. P. Salazar-Mather, S. M. Opal, R. L. Spencer, A. H. Miller, B. S. McEwen, and C. A. Biron. 1995. Mechanism of interleukin 12-mediated toxicities during experimental viral infections: role of tumor necrosis factor and glucocorticoids. J. Exp. Med. 181:901.
    • (1995) J. Exp. Med. , vol.181 , pp. 901
    • Orange, J.S.1    Salazar-Mather, T.P.2    Opal, S.M.3    Spencer, R.L.4    Miller, A.H.5    McEwen, B.S.6    Biron, C.A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.