메뉴 건너뛰기




Volumn 86, Issue 7, 2008, Pages 598-607

Biological implications of glycosaminoglycan interactions with haemopoietic cytokines

Author keywords

Cytokine; Glycosaminoglycan; Haemopoiesis; Heparan sulphate; Heparin; Interleukin

Indexed keywords

CYTOKINE; FIBROBLAST GROWTH FACTOR; GLYCOSAMINOGLYCAN; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; HEPARAN SULFATE; HEPARIN; INTERLEUKIN 2; INTERLEUKIN 3; INTERLEUKIN 4; INTERLEUKIN 5; INTERLEUKIN 6;

EID: 53249151669     PISSN: 08189641     EISSN: 14401711     Source Type: Journal    
DOI: 10.1038/icb.2008.49     Document Type: Review
Times cited : (64)

References (72)
  • 1
    • 15244364003 scopus 로고    scopus 로고
    • Heparan sulfate-protein interactions: Therapeutic potential through structure-function insights
    • Coombe DR, Kett WC. Heparan sulfate-protein interactions: therapeutic potential through structure-function insights. Cell Mol Life Sci 2005; 62: 410-424.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 410-424
    • Coombe, D.R.1    Kett, W.C.2
  • 2
    • 0038792320 scopus 로고    scopus 로고
    • Hudson award address in carbohydrate chemistry. Heparin: Structure and activity
    • Linhardt RJ. Claude S. Hudson award address in carbohydrate chemistry. Heparin: structure and activity. J Med Chem 2003; 46: 2551-2564.
    • (2003) J Med Chem , vol.46 , pp. 2551-2564
    • Linhardt, R.J.1    Claude, S.2
  • 3
    • 0035903106 scopus 로고    scopus 로고
    • Sequence analysis of heparan sulfate epitopes with graded affinities for fibroblast growth factors 1 and 2
    • Kreuger J, Salmivirta M, Sturiale L, Gimenez-Gallego G, Lindahl U. Sequence analysis of heparan sulfate epitopes with graded affinities for fibroblast growth factors 1 and 2. J Biol Chem 2001; 276: 30744-30752.
    • (2001) J Biol Chem , vol.276 , pp. 30744-30752
    • Kreuger, J.1    Salmivirta, M.2    Sturiale, L.3    Gimenez-Gallego, G.4    Lindahl, U.5
  • 4
    • 0035956435 scopus 로고    scopus 로고
    • Role of heparan sulfate as a tissue-specific regulator of FGF-4 and FGF receptor recognition
    • Allen BL, Filla MS, Rapraeger AC. Role of heparan sulfate as a tissue-specific regulator of FGF-4 and FGF receptor recognition. J Cell Biol 2001; 155: 845-858.
    • (2001) J Cell Biol , vol.155 , pp. 845-858
    • Allen, B.L.1    Filla, M.S.2    Rapraeger, A.C.3
  • 5
    • 0242677706 scopus 로고    scopus 로고
    • Spatial and temporal expression of heparan sulfate in mouse development regulates FGF and FGF receptor assembly
    • Allen BL, Rapraeger AC. Spatial and temporal expression of heparan sulfate in mouse development regulates FGF and FGF receptor assembly. J Cell Biol 2003; 163: 637-648.
    • (2003) J Cell Biol , vol.163 , pp. 637-648
    • Allen, B.L.1    Rapraeger, A.C.2
  • 6
    • 33746614761 scopus 로고    scopus 로고
    • Interactions between heparan sulfate and proteins: The concept of specificity
    • Kreuger J, Spillmann D, Li JP, Lindahl U. Interactions between heparan sulfate and proteins: the concept of specificity. J Cell Biol 2006; 174: 323-327.
    • (2006) J Cell Biol , vol.174 , pp. 323-327
    • Kreuger, J.1    Spillmann, D.2    Li, J.P.3    Lindahl, U.4
  • 7
    • 46049094815 scopus 로고    scopus 로고
    • Application of drug discovery software to the identification of heparin-binding sites on protein surfaces: A computational survey of the 4-helix cytokines
    • Mulloy B, Forster MJ. Application of drug discovery software to the identification of heparin-binding sites on protein surfaces: A computational survey of the 4-helix cytokines. Mol Sim 2008; 34: 481-489.
    • (2008) Mol Sim , vol.34 , pp. 481-489
    • Mulloy, B.1    Forster, M.J.2
  • 8
    • 33745478458 scopus 로고    scopus 로고
    • Cytokines and proteoglycans: An introductory overview
    • Mulloy B, Rider CC. Cytokines and proteoglycans: an introductory overview. Biochem Soc Trans 2006; 34: 409-413.
    • (2006) Biochem Soc Trans , vol.34 , pp. 409-413
    • Mulloy, B.1    Rider, C.C.2
  • 9
    • 0034718796 scopus 로고    scopus 로고
    • Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin
    • Pellegrini L, Burke DF, von Delft F, Mulloy B, Blundell TL. Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin. Nature 2000; 407: 1029-1034.
    • (2000) Nature , vol.407 , pp. 1029-1034
    • Pellegrini, L.1    Burke, D.F.2    von Delft, F.3    Mulloy, B.4    Blundell, T.L.5
  • 10
    • 0033635299 scopus 로고    scopus 로고
    • Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization
    • Schlessinger J, Plotnikov AN, Ibrahimi OA, Eliseenkova AV, Yeh BK, Yayon A et al. Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization. Mol Cell 2000; 6: 743-750.
    • (2000) Mol Cell , vol.6 , pp. 743-750
    • Schlessinger, J.1    Plotnikov, A.N.2    Ibrahimi, O.A.3    Eliseenkova, A.V.4    Yeh, B.K.5    Yayon, A.6
  • 11
    • 33749412368 scopus 로고    scopus 로고
    • Solution NMR structure of a human FGF-1 monomer, activated by a hexasaccharide heparin-analogue
    • Canales A, Lozano R, Lopez-Mendez B, Angulo J, Ojeda R, Nieto PM et al. Solution NMR structure of a human FGF-1 monomer, activated by a hexasaccharide heparin-analogue. FEBS J 2006; 273: 4716-4727.
    • (2006) FEBS J , vol.273 , pp. 4716-4727
    • Canales, A.1    Lozano, R.2    Lopez-Mendez, B.3    Angulo, J.4    Ojeda, R.5    Nieto, P.M.6
  • 12
    • 31544445500 scopus 로고    scopus 로고
    • Multimers of the fibroblast growth factor (FGF)-FGF receptor-saccharide complex are formed on long oligomers of heparin
    • Harmer NJ, Robinson CJ, Adam LE, Ilag LL, Robinson CV, Gallagher JT et al. Multimers of the fibroblast growth factor (FGF)-FGF receptor-saccharide complex are formed on long oligomers of heparin. Biochem J 2006; 393: 741-748.
    • (2006) Biochem J , vol.393 , pp. 741-748
    • Harmer, N.J.1    Robinson, C.J.2    Adam, L.E.3    Ilag, L.L.4    Robinson, C.V.5    Gallagher, J.T.6
  • 13
    • 33746653467 scopus 로고    scopus 로고
    • Heparan sulfate-related oligosaccharides in ternary complex formation with fibroblast growth factors 1 and 2 and their receptors
    • Jastrebova N, Vanwildemeersch M, Rapraeger AC, Gimenez-Gallego G, Lindahl U, Spillmann D. Heparan sulfate-related oligosaccharides in ternary complex formation with fibroblast growth factors 1 and 2 and their receptors. J Biol Chem 2006; 281: 26884-26892.
    • (2006) J Biol Chem , vol.281 , pp. 26884-26892
    • Jastrebova, N.1    Vanwildemeersch, M.2    Rapraeger, A.C.3    Gimenez-Gallego, G.4    Lindahl, U.5    Spillmann, D.6
  • 14
    • 0037103725 scopus 로고    scopus 로고
    • Fibroblast growth factor-2 binds to small heparin-derived oligosaccharides and stimulates a sustained phosphorylation of p42/44 mitogen-activated protein kinase and proliferation of rat mammary fibroblasts
    • Delehedde M, Lyon M, Gallagher JT, Rudland PS, Fernig DG. Fibroblast growth factor-2 binds to small heparin-derived oligosaccharides and stimulates a sustained phosphorylation of p42/44 mitogen-activated protein kinase and proliferation of rat mammary fibroblasts. Biochem J 2002; 366: 235-244.
    • (2002) Biochem J , vol.366 , pp. 235-244
    • Delehedde, M.1    Lyon, M.2    Gallagher, J.T.3    Rudland, P.S.4    Fernig, D.G.5
  • 15
    • 25844440918 scopus 로고    scopus 로고
    • A protein canyon in the FGF-FGF receptor dimer selects from an a la carte menu of heparan sulfate motifs
    • Mohammadi M, Olsen SK, Goetz R. A protein canyon in the FGF-FGF receptor dimer selects from an a la carte menu of heparan sulfate motifs. Curr Opin Struct Biol 2005; 15: 506-516.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 506-516
    • Mohammadi, M.1    Olsen, S.K.2    Goetz, R.3
  • 16
    • 33745474608 scopus 로고    scopus 로고
    • Insights into the role of heparan sulphate in fibroblast growth factor signalling
    • Harmer NJ. Insights into the role of heparan sulphate in fibroblast growth factor signalling. Biochem Soc Trans 2006; 34: 442-445.
    • (2006) Biochem Soc Trans , vol.34 , pp. 442-445
    • Harmer, N.J.1
  • 17
    • 0023504771 scopus 로고
    • Growth and differentiation in the hemopoietic system
    • Dexter TM, Spooncer E. Growth and differentiation in the hemopoietic system. Annu Rev Cell Biol 1987; 3: 423-441.
    • (1987) Annu Rev Cell Biol , vol.3 , pp. 423-441
    • Dexter, T.M.1    Spooncer, E.2
  • 18
    • 0023928595 scopus 로고
    • Heparan sulphate bound growth factors: A mechanism for stromal cell mediated haemopoiesis
    • Roberts R, Gallagher J, Spooncer E, Allen TD, Bloomfield F, Dexter TM. Heparan sulphate bound growth factors: a mechanism for stromal cell mediated haemopoiesis. Nature 1988; 332: 376-378.
    • (1988) Nature , vol.332 , pp. 376-378
    • Roberts, R.1    Gallagher, J.2    Spooncer, E.3    Allen, T.D.4    Bloomfield, F.5    Dexter, T.M.6
  • 19
    • 0027482760 scopus 로고
    • Localisation of granulocyte macrophage colony-stimulating factor in human long-term bone marrow cultures. Biological and immunocytochemical characterisation
    • de Wynter E, Allen T, Coutinho L, Flavell D, Flavell SU, Dexter TM. Localisation of granulocyte macrophage colony-stimulating factor in human long-term bone marrow cultures. Biological and immunocytochemical characterisation. J Cell Sci 1993; 106: 761-769.
    • (1993) J Cell Sci , vol.106 , pp. 761-769
    • de Wynter, E.1    Allen, T.2    Coutinho, L.3    Flavell, D.4    Flavell, S.U.5    Dexter, T.M.6
  • 20
    • 0029927427 scopus 로고    scopus 로고
    • The role of stromal cell heparan sulphate in regulating haemopoiesis
    • Coombe DR. The role of stromal cell heparan sulphate in regulating haemopoiesis. Leuk Lymphoma 1996; 21: 399-406.
    • (1996) Leuk Lymphoma , vol.21 , pp. 399-406
    • Coombe, D.R.1
  • 21
    • 0028784886 scopus 로고
    • Marrow-derived heparan sulfate proteoglycan mediates the adhesion of hematopoietic progenitor cells to cytokines
    • Bruno E, Luikart SD, Long MW, Hoffman R. Marrow-derived heparan sulfate proteoglycan mediates the adhesion of hematopoietic progenitor cells to cytokines. Exp Hematol 1995; 23: 1212-1217.
    • (1995) Exp Hematol , vol.23 , pp. 1212-1217
    • Bruno, E.1    Luikart, S.D.2    Long, M.W.3    Hoffman, R.4
  • 22
    • 0032535591 scopus 로고    scopus 로고
    • Structurally specific heparan sulfates support primitive human hematopoiesis by formation of a multimolecular stem cell niche
    • Gupta P, Oegema Jr TR, Brazil JJ, Dudek AZ, Slungaard A, Verfaillie CM. Structurally specific heparan sulfates support primitive human hematopoiesis by formation of a multimolecular stem cell niche. Blood 1998; 92: 4641-4651.
    • (1998) Blood , vol.92 , pp. 4641-4651
    • Gupta, P.1    Oegema Jr, T.R.2    Brazil, J.J.3    Dudek, A.Z.4    Slungaard, A.5    Verfaillie, C.M.6
  • 23
    • 0033957697 scopus 로고    scopus 로고
    • Human LTC-IC can be maintained for at least 5 weeks in vitro when interleukin-3 and a single chemokine are combined with O-sulfated heparan sulfates: Requirement for optimal binding interactions of heparan sulfate with early-acting cytokines and matrix proteins
    • Gupta P, Oegema Jr TR, Brazil JJ, Dudek AZ, Slungaard A, Verfaillie CM. Human LTC-IC can be maintained for at least 5 weeks in vitro when interleukin-3 and a single chemokine are combined with O-sulfated heparan sulfates: requirement for optimal binding interactions of heparan sulfate with early-acting cytokines and matrix proteins. Blood 2000; 95: 147-155.
    • (2000) Blood , vol.95 , pp. 147-155
    • Gupta, P.1    Oegema Jr, T.R.2    Brazil, J.J.3    Dudek, A.Z.4    Slungaard, A.5    Verfaillie, C.M.6
  • 24
    • 0344089342 scopus 로고    scopus 로고
    • Molecular assembly of the ternary granulocyte-macrophage colony-stimulating factor receptor complex
    • McClure BJ, Hercus TR, Cambareri BA, Woodcock JM, Bagley CJ, Howlett GJ et al. Molecular assembly of the ternary granulocyte-macrophage colony-stimulating factor receptor complex. Blood 2003; 101: 1308-1315.
    • (2003) Blood , vol.101 , pp. 1308-1315
    • McClure, B.J.1    Hercus, T.R.2    Cambareri, B.A.3    Woodcock, J.M.4    Bagley, C.J.5    Howlett, G.J.6
  • 25
    • 34347394325 scopus 로고    scopus 로고
    • Biology of umbilical cord blood progenitors in bone marrow niches
    • Dao MA, Creer MH, Nolta JA, Verfaillie CM. Biology of umbilical cord blood progenitors in bone marrow niches. Blood 2007; 110: 74-81.
    • (2007) Blood , vol.110 , pp. 74-81
    • Dao, M.A.1    Creer, M.H.2    Nolta, J.A.3    Verfaillie, C.M.4
  • 26
    • 0042090059 scopus 로고    scopus 로고
    • Stroma-mediated granulocyte-macrophage colony-stimulating factor (GM-CSF) control of myelopoiesis: Spatial organisation of intercellular interactions
    • Borojevic R, Carvalho MA, Correa-Junior JD, Arcanjo K, Gomes L, Joazeiro PP et al. Stroma-mediated granulocyte-macrophage colony-stimulating factor (GM-CSF) control of myelopoiesis: spatial organisation of intercellular interactions. Cell Tissue Res 2003; 313: 55-62.
    • (2003) Cell Tissue Res , vol.313 , pp. 55-62
    • Borojevic, R.1    Carvalho, M.A.2    Correa-Junior, J.D.3    Arcanjo, K.4    Gomes, L.5    Joazeiro, P.P.6
  • 27
    • 42449150821 scopus 로고    scopus 로고
    • Platelet endothelial cell adhesion molecule 1 (PECAM-1) and its interactions with glycosaminoglycans: 2. biochemical analyses
    • Coombe DR, Stevenson SM, Kinnear BF, Gandhi NS, Mancera RL, Osmond RI et al. Platelet endothelial cell adhesion molecule 1 (PECAM-1) and its interactions with glycosaminoglycans: 2. biochemical analyses. Biochemistry 2008; 47: 4863-4875.
    • (2008) Biochemistry , vol.47 , pp. 4863-4875
    • Coombe, D.R.1    Stevenson, S.M.2    Kinnear, B.F.3    Gandhi, N.S.4    Mancera, R.L.5    Osmond, R.I.6
  • 28
    • 0033615689 scopus 로고    scopus 로고
    • Acidic pH modulates the interaction between human granulocyte-macrophage colony-stimulating factor and glycosaminoglycans
    • Wettreich A, Sebollela A, Carvalho MA, Azevedo SP, Borojevic R, Ferreira ST et al. Acidic pH modulates the interaction between human granulocyte-macrophage colony-stimulating factor and glycosaminoglycans. J Biol Chem 1999; 274: 31468-31475.
    • (1999) J Biol Chem , vol.274 , pp. 31468-31475
    • Wettreich, A.1    Sebollela, A.2    Carvalho, M.A.3    Azevedo, S.P.4    Borojevic, R.5    Ferreira, S.T.6
  • 29
    • 24744447215 scopus 로고    scopus 로고
    • Heparin-binding sites in granulocyte-macrophage colony-stimulating factor. Localization and regulation by histidine ionization
    • Sebollela A, Cagliari TC, Limaverde GS, Chapeaurouge A, Sorgine MH, Coelho-Sampaio T et al. Heparin-binding sites in granulocyte-macrophage colony-stimulating factor. Localization and regulation by histidine ionization. J Biol Chem 2005; 280: 31949-31956.
    • (2005) J Biol Chem , vol.280 , pp. 31949-31956
    • Sebollela, A.1    Cagliari, T.C.2    Limaverde, G.S.3    Chapeaurouge, A.4    Sorgine, M.H.5    Coelho-Sampaio, T.6
  • 30
    • 0028233122 scopus 로고
    • Identification of residues in the first and fourth helices of human granulocyte-macrophage colony-stimulating factor involved in biologic activity and in binding to the alpha- and beta-chains of its receptor
    • Hercus TR, Cambareri B, Dottore M, Woodcock J, Bagley CJ, Vadas MA et al. Identification of residues in the first and fourth helices of human granulocyte-macrophage colony-stimulating factor involved in biologic activity and in binding to the alpha- and beta-chains of its receptor. Blood 1994; 83: 3500-3508.
    • (1994) Blood , vol.83 , pp. 3500-3508
    • Hercus, T.R.1    Cambareri, B.2    Dottore, M.3    Woodcock, J.4    Bagley, C.J.5    Vadas, M.A.6
  • 31
    • 0031595659 scopus 로고    scopus 로고
    • Glycosaminoglycans bind granulocyte-macrophage colony-stimulating factor and modulate its mitogenic activity and signaling in human osteoblastic cells
    • Modrowski D, Lomri A, Marie PJ. Glycosaminoglycans bind granulocyte-macrophage colony-stimulating factor and modulate its mitogenic activity and signaling in human osteoblastic cells. J Cell Physiol 1998; 177: 187-195.
    • (1998) J Cell Physiol , vol.177 , pp. 187-195
    • Modrowski, D.1    Lomri, A.2    Marie, P.J.3
  • 32
    • 0034737470 scopus 로고    scopus 로고
    • Syndecan-2 is involved in the mitogenic activity and signaling of granulocyte-macrophage colony-stimulating factor in osteoblasts
    • Modrowski D, Basle M, Lomri A, Marie PJ. Syndecan-2 is involved in the mitogenic activity and signaling of granulocyte-macrophage colony-stimulating factor in osteoblasts. J Biol Chem 2000; 275: 9178-9185.
    • (2000) J Biol Chem , vol.275 , pp. 9178-9185
    • Modrowski, D.1    Basle, M.2    Lomri, A.3    Marie, P.J.4
  • 33
    • 0029938639 scopus 로고    scopus 로고
    • Three-dimensional solution structure and backbone dynamics of a variant of human interleukin-3
    • Feng Y, Klein BK, McWherter CA. Three-dimensional solution structure and backbone dynamics of a variant of human interleukin-3. J Mol Biol 1996; 259: 524-541.
    • (1996) J Mol Biol , vol.259 , pp. 524-541
    • Feng, Y.1    Klein, B.K.2    McWherter, C.A.3
  • 34
    • 0029657911 scopus 로고    scopus 로고
    • A discontinuous eight-amino acid epitope in human interleukin-3 binds the alpha-chain of its receptor
    • Bagley CJ, Phillips J, Cambareri B, Vadas MA, Lopez AF. A discontinuous eight-amino acid epitope in human interleukin-3 binds the alpha-chain of its receptor. J Biol Chem 1996; 271: 31922-31928.
    • (1996) J Biol Chem , vol.271 , pp. 31922-31928
    • Bagley, C.J.1    Phillips, J.2    Cambareri, B.3    Vadas, M.A.4    Lopez, A.F.5
  • 35
    • 0029996266 scopus 로고    scopus 로고
    • GM-CSF and IL-3 activities in schistosomal liver granulomas are controlled by stroma-associated heparan sulfate proteoglycans
    • Alvarez-Silva M, Borojevic R. GM-CSF and IL-3 activities in schistosomal liver granulomas are controlled by stroma-associated heparan sulfate proteoglycans. J Leukoc Biol 1996; 59: 435-441.
    • (1996) J Leukoc Biol , vol.59 , pp. 435-441
    • Alvarez-Silva, M.1    Borojevic, R.2
  • 36
    • 0025825585 scopus 로고
    • Role of glycosaminoglycans in the regulation of T cell proliferation induced by thymic stroma-derived T cell growth factor
    • Kimura K, Matsubara H, Sogoh S, Kita Y, Sakata T, Nishitani Y et al. Role of glycosaminoglycans in the regulation of T cell proliferation induced by thymic stroma-derived T cell growth factor. J Immunol 1991; 146: 2618-2624.
    • (1991) J Immunol , vol.146 , pp. 2618-2624
    • Kimura, K.1    Matsubara, H.2    Sogoh, S.3    Kita, Y.4    Sakata, T.5    Nishitani, Y.6
  • 37
    • 0028981023 scopus 로고
    • Detailed analysis of the IL-5-IL-5R alpha interaction: Characterization of crucial residues on the ligand and the receptor
    • Cornelis S, Plaetinck G, Devos R, Van der Heyden J, Tavernier J, Sanderson CJ et al. Detailed analysis of the IL-5-IL-5R alpha interaction: characterization of crucial residues on the ligand and the receptor. EMBO J 1995; 14: 3395-3402.
    • (1995) EMBO J , vol.14 , pp. 3395-3402
    • Cornelis, S.1    Plaetinck, G.2    Devos, R.3    Van der Heyden, J.4    Tavernier, J.5    Sanderson, C.J.6
  • 38
    • 0029077810 scopus 로고
    • Identification of key charged residues of human interleukin-5 in receptor binding and cellular activation
    • Graber P, Proudfoot AE, Talabot F, Bernard A, McKinnon M, Banks M et al. Identification of key charged residues of human interleukin-5 in receptor binding and cellular activation. J Biol Chem 1995; 270: 15762-15769.
    • (1995) J Biol Chem , vol.270 , pp. 15762-15769
    • Graber, P.1    Proudfoot, A.E.2    Talabot, F.3    Bernard, A.4    McKinnon, M.5    Banks, M.6
  • 39
    • 0029000927 scopus 로고
    • Identification of receptor-binding domains on human interleukin 5 and design of an interleukin 5-derived receptor antagonist
    • Tavernier J, Tuypens T, Verhee A, Plaetinck G, Devos R, Van der Heyden J et al. Identification of receptor-binding domains on human interleukin 5 and design of an interleukin 5-derived receptor antagonist. Proc Natl Acad Sci USA 1995; 92: 5194-5198.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5194-5198
    • Tavernier, J.1    Tuypens, T.2    Verhee, A.3    Plaetinck, G.4    Devos, R.5    Van der Heyden, J.6
  • 40
    • 0034536831 scopus 로고    scopus 로고
    • Interleukin-5: A drug target for allergic diseases
    • Sanderson CJ, Urwin D. Interleukin-5: a drug target for allergic diseases. Curr Opin Investig Drugs 2000; 1: 435-441.
    • (2000) Curr Opin Investig Drugs , vol.1 , pp. 435-441
    • Sanderson, C.J.1    Urwin, D.2
  • 41
    • 0031906297 scopus 로고    scopus 로고
    • Interleukin-5 binds to heparin/heparan sulfate. A model for an interaction with extracellular matrix
    • Lipscombe RJ, Nakhoul AM, Sanderson CJ, Coombe DR. Interleukin-5 binds to heparin/heparan sulfate. A model for an interaction with extracellular matrix. J Leukoc Biol 1998; 63: 342-350.
    • (1998) J Leukoc Biol , vol.63 , pp. 342-350
    • Lipscombe, R.J.1    Nakhoul, A.M.2    Sanderson, C.J.3    Coombe, D.R.4
  • 43
    • 0027480765 scopus 로고
    • Recombinant soluble human interleukin-5 (hIL-5) receptor molecules. Cross-linking and stoichiometry of binding to IL-5
    • Devos R, Guisez Y, Cornelis S, Verhee A, Van der Heyden J, Manneberg M et al. Recombinant soluble human interleukin-5 (hIL-5) receptor molecules. Cross-linking and stoichiometry of binding to IL-5. J Biol Chem 1993; 268: 6581-6587.
    • (1993) J Biol Chem , vol.268 , pp. 6581-6587
    • Devos, R.1    Guisez, Y.2    Cornelis, S.3    Verhee, A.4    Van der Heyden, J.5    Manneberg, M.6
  • 44
    • 17744386517 scopus 로고    scopus 로고
    • Structure of the complete extracellular domain of the common beta subunit of the human GM-CSF, IL-3, and IL-5 receptors reveals a novel dimer configuration
    • Carr PD, Gustin SE, Church AP, Murphy JM, Ford SC, Mann DA et al. Structure of the complete extracellular domain of the common beta subunit of the human GM-CSF, IL-3, and IL-5 receptors reveals a novel dimer configuration. Cell 2001; 104: 291-300.
    • (2001) Cell , vol.104 , pp. 291-300
    • Carr, P.D.1    Gustin, S.E.2    Church, A.P.3    Murphy, J.M.4    Ford, S.C.5    Mann, D.A.6
  • 45
    • 0037102095 scopus 로고    scopus 로고
    • Biosensor analysis of dynamics of interleukin 5 receptor subunit beta(c) interaction with IL5:IL5R(alpha) complexes
    • Scibek JJ, Evergren E, Zahn S, Canziani GA, Van Ryk D, Chaiken IM. Biosensor analysis of dynamics of interleukin 5 receptor subunit beta(c) interaction with IL5:IL5R(alpha) complexes. Anal Biochem 2002; 307: 258-265.
    • (2002) Anal Biochem , vol.307 , pp. 258-265
    • Scibek, J.J.1    Evergren, E.2    Zahn, S.3    Canziani, G.A.4    Van Ryk, D.5    Chaiken, I.M.6
  • 46
    • 9644281044 scopus 로고    scopus 로고
    • Interleukin-13 in asthma pathogenesis
    • Wills-Karp M. Interleukin-13 in asthma pathogenesis. Immunol Rev 2004; 202: 175-190.
    • (2004) Immunol Rev , vol.202 , pp. 175-190
    • Wills-Karp, M.1
  • 47
    • 0035967886 scopus 로고    scopus 로고
    • Solution structure of human IL-13 and implication for receptor binding
    • Moy FJ, Diblasio E, Wilhelm J, Powers R. Solution structure of human IL-13 and implication for receptor binding. J Mol Biol 2001; 310: 219-230.
    • (2001) J Mol Biol , vol.310 , pp. 219-230
    • Moy, F.J.1    Diblasio, E.2    Wilhelm, J.3    Powers, R.4
  • 49
    • 0030068217 scopus 로고    scopus 로고
    • Cloning and characterization of a binding subunit of the interleukin 13 receptor that is also a component of the interleukin 4 receptor
    • Hilton DJ, Zhang JG, Metcalf D, Alexander WS, Nicola NA, Willson TA. Cloning and characterization of a binding subunit of the interleukin 13 receptor that is also a component of the interleukin 4 receptor. Proc Natl Acad Sci USA 1996; 93: 497-501.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 497-501
    • Hilton, D.J.1    Zhang, J.G.2    Metcalf, D.3    Alexander, W.S.4    Nicola, N.A.5    Willson, T.A.6
  • 50
    • 0037064548 scopus 로고    scopus 로고
    • Structure, binding, and antagonists in the IL-4/IL-13 receptor system
    • Mueller TD, Zhang JL, Sebald W, Duschl A. Structure, binding, and antagonists in the IL-4/IL-13 receptor system. Biochim Biophys Acta 2002; 1592: 237-250.
    • (2002) Biochim Biophys Acta , vol.1592 , pp. 237-250
    • Mueller, T.D.1    Zhang, J.L.2    Sebald, W.3    Duschl, A.4
  • 51
    • 38649137731 scopus 로고    scopus 로고
    • Molecular and structural basis of cytokine receptor pleiotropy in the interleukin-4/13 system
    • LaPorte SL, Juo ZS, Vaclavikova J, Colf LA, Qi X, Heller NM et al. Molecular and structural basis of cytokine receptor pleiotropy in the interleukin-4/13 system. Cell 2008; 132: 259-272.
    • (2008) Cell , vol.132 , pp. 259-272
    • LaPorte, S.L.1    Juo, Z.S.2    Vaclavikova, J.3    Colf, L.A.4    Qi, X.5    Heller, N.M.6
  • 52
    • 0028922284 scopus 로고
    • Interleukin 4 production by human amnion epithelial cells and regulation of its activity by glycosaminoglycan binding
    • Jones CA, Williams KA, Finlay-Jones JJ, Hart PH. Interleukin 4 production by human amnion epithelial cells and regulation of its activity by glycosaminoglycan binding. Biol Reprod 1995; 52: 839-847.
    • (1995) Biol Reprod , vol.52 , pp. 839-847
    • Jones, C.A.1    Williams, K.A.2    Finlay-Jones, J.J.3    Hart, P.H.4
  • 54
    • 44849134171 scopus 로고    scopus 로고
    • Monocyte cell surface glycosaminoglycans positively modulate IL-4-induced differentiation toward dendritic cells
    • den Dekker E, Grefte S, Huijs T, ten Dam GB, Versteeg EM, van den Berk LC et al. Monocyte cell surface glycosaminoglycans positively modulate IL-4-induced differentiation toward dendritic cells. J Immunol 2008; 180: 3680-3688.
    • (2008) J Immunol , vol.180 , pp. 3680-3688
    • den Dekker, E.1    Grefte, S.2    Huijs, T.3    ten Dam, G.B.4    Versteeg, E.M.5    van den Berk, L.C.6
  • 55
    • 0036786477 scopus 로고    scopus 로고
    • Differential functions of IL-4 receptor types I and II for dendritic cell maturation and IL-12 production and their dependency on GM-CSF
    • Lutz MB, Schnare M, Menges M, Rossner S, Rollinghoff M, Schuler G et al. Differential functions of IL-4 receptor types I and II for dendritic cell maturation and IL-12 production and their dependency on GM-CSF. J Immunol 2002; 169: 3574-3580.
    • (2002) J Immunol , vol.169 , pp. 3574-3580
    • Lutz, M.B.1    Schnare, M.2    Menges, M.3    Rossner, S.4    Rollinghoff, M.5    Schuler, G.6
  • 56
    • 0026475049 scopus 로고
    • Selective and differential binding of interleukin (IL)-1 alpha, IL-1 beta, IL-2 and IL-6 to glycosaminoglycans
    • Ramsden L, Rider CC. Selective and differential binding of interleukin (IL)-1 alpha, IL-1 beta, IL-2 and IL-6 to glycosaminoglycans. Eur J Immunol 1992; 22: 3027-3031.
    • (1992) Eur J Immunol , vol.22 , pp. 3027-3031
    • Ramsden, L.1    Rider, C.C.2
  • 57
    • 0031441834 scopus 로고    scopus 로고
    • Characterization of human recombinant interleukin 2 binding to heparin and heparan sulfate using an ELISA approach
    • Najjam S, Gibbs RV, Gordon MY, Rider CC. Characterization of human recombinant interleukin 2 binding to heparin and heparan sulfate using an ELISA approach. Cytokine 1997; 9: 1013-1022.
    • (1997) Cytokine , vol.9 , pp. 1013-1022
    • Najjam, S.1    Gibbs, R.V.2    Gordon, M.Y.3    Rider, C.C.4
  • 58
    • 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, Mulloy B, Theze J, Gordon M, Gibbs R, Rider CC. Further characterization of the binding of human recombinant interleukin 2 to heparin and identification of putative binding sites. Glycobiology 1998; 8: 509-516.
    • (1998) Glycobiology , vol.8 , pp. 509-516
    • Najjam, S.1    Mulloy, B.2    Theze, J.3    Gordon, M.4    Gibbs, R.5    Rider, C.C.6
  • 59
    • 0035925887 scopus 로고    scopus 로고
    • Signaling domains of the interleukin 2 receptor
    • Gaffen SL. Signaling domains of the interleukin 2 receptor. Cytokine 2001; 14: 63-77.
    • (2001) Cytokine , vol.14 , pp. 63-77
    • Gaffen, S.L.1
  • 61
    • 27944505913 scopus 로고    scopus 로고
    • Structure of the quaternary complex of interleukin-2 with its alpha, beta, and gamma c receptors
    • Wang X, Rickert M, Garcia KC. Structure of the quaternary complex of interleukin-2 with its alpha, beta, and gamma c receptors. Science 2005; 310: 1159-1163.
    • (2005) Science , vol.310 , pp. 1159-1163
    • Wang, X.1    Rickert, M.2    Garcia, K.C.3
  • 63
    • 1542297244 scopus 로고    scopus 로고
    • IL-6 signal transduction and its physiological roles: The signal orchestration model
    • Kamimura D, Ishihara K, Hirano T. IL-6 signal transduction and its physiological roles: the signal orchestration model. Rev Physiol Biochem Pharmacol 2003; 149: 1-38.
    • (2003) Rev Physiol Biochem Pharmacol , vol.149 , pp. 1-38
    • Kamimura, D.1    Ishihara, K.2    Hirano, T.3
  • 64
    • 0034669968 scopus 로고    scopus 로고
    • Characterization of the heparin-binding properties of IL-6
    • Mummery RS, Rider CC. Characterization of the heparin-binding properties of IL-6. J Immunol 2000; 165: 5671-5679.
    • (2000) J Immunol , vol.165 , pp. 5671-5679
    • Mummery, R.S.1    Rider, C.C.2
  • 65
    • 0038609651 scopus 로고    scopus 로고
    • Hexameric structure and assembly of the interleukin-6/IL-6 alpha-receptor/gp130 complex
    • Boulanger MJ, Chow DC, Brevnova EE, Garcia KC. Hexameric structure and assembly of the interleukin-6/IL-6 alpha-receptor/gp130 complex. Science 2003; 300: 2101-2104.
    • (2003) Science , vol.300 , pp. 2101-2104
    • Boulanger, M.J.1    Chow, D.C.2    Brevnova, E.E.3    Garcia, K.C.4
  • 66
    • 0842346188 scopus 로고    scopus 로고
    • Regulation of myeloid development and function by colony stimulating factors
    • Barreda DR, Hanington PC, Belosevic M. Regulation of myeloid development and function by colony stimulating factors. Dev Comp Immunol 2004; 28: 509-554.
    • (2004) Dev Comp Immunol , vol.28 , pp. 509-554
    • Barreda, D.R.1    Hanington, P.C.2    Belosevic, M.3
  • 67
    • 33644761881 scopus 로고    scopus 로고
    • Homodimeric cross-over structure of the human granulocyte colony-stimulating factor (GCSF) receptor signaling complex
    • Tamada T, Honjo E, Maeda Y, Okamoto T, Ishibashi M, Tokunaga M et al. Homodimeric cross-over structure of the human granulocyte colony-stimulating factor (GCSF) receptor signaling complex. Proc Natl Acad Sci USA 2006; 103: 3135-3140.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 3135-3140
    • Tamada, T.1    Honjo, E.2    Maeda, Y.3    Okamoto, T.4    Ishibashi, M.5    Tokunaga, M.6
  • 68
    • 1642485197 scopus 로고    scopus 로고
    • Capillary zone electrophoresis investigation of the interaction between heparin and granulocyte-colony stimulating factor
    • Liang A, He X, Du Y, Wang K, Fung Y, Lin B. Capillary zone electrophoresis investigation of the interaction between heparin and granulocyte-colony stimulating factor. Electrophoresis 2004; 25: 870-875.
    • (2004) Electrophoresis , vol.25 , pp. 870-875
    • Liang, A.1    He, X.2    Du, Y.3    Wang, K.4    Fung, Y.5    Lin, B.6
  • 69
    • 26244454789 scopus 로고    scopus 로고
    • Separation, identification, and interaction of heparin oligosaccharides with granulocyte-colony stimulating factor using capillary electrophoresis and mass spectrometry
    • Liang A, Chao Y, Liu X, Du Y, Wang K, Qian S et al. Separation, identification, and interaction of heparin oligosaccharides with granulocyte-colony stimulating factor using capillary electrophoresis and mass spectrometry. Electrophoresis 2005; 26: 3460-3467.
    • (2005) Electrophoresis , vol.26 , pp. 3460-3467
    • Liang, A.1    Chao, Y.2    Liu, X.3    Du, Y.4    Wang, K.5    Qian, S.6
  • 70
    • 33748365407 scopus 로고    scopus 로고
    • Interactions of dextran sulfates with granulocyte colony-stimulating factor and their effects on leukemia cells
    • Liang A, Zhou X, Wang Q, Liu X, Qin J, Du Y et al. Interactions of dextran sulfates with granulocyte colony-stimulating factor and their effects on leukemia cells. Electrophoresis 2006; 27: 3195-3201.
    • (2006) Electrophoresis , vol.27 , pp. 3195-3201
    • Liang, A.1    Zhou, X.2    Wang, Q.3    Liu, X.4    Qin, J.5    Du, Y.6
  • 71
    • 33749447284 scopus 로고    scopus 로고
    • Structural features in carrageenan that interact with a heparin-binding hematopoietic growth factor and modulate its biological activity
    • Liang A, Zhou X, Wang Q, Liu X, Du Y, Wang K et al. Structural features in carrageenan that interact with a heparin-binding hematopoietic growth factor and modulate its biological activity. J Chromatogr B Analyt Technol Biomed Life Sci 2006; 843: 114-119.
    • (2006) J Chromatogr B Analyt Technol Biomed Life Sci , vol.843 , pp. 114-119
    • Liang, A.1    Zhou, X.2    Wang, Q.3    Liu, X.4    Du, Y.5    Wang, K.6
  • 72
    • 0037112671 scopus 로고    scopus 로고
    • Protein-heparin interactions measured by BIAcore 2000 are affected by the method of heparin immobilization
    • Osmond RI, Kett WC, Skett SE, Coombe DR. Protein-heparin interactions measured by BIAcore 2000 are affected by the method of heparin immobilization. Anal Biochem 2002; 310: 199-207.
    • (2002) Anal Biochem , vol.310 , pp. 199-207
    • Osmond, R.I.1    Kett, W.C.2    Skett, S.E.3    Coombe, D.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.