메뉴 건너뛰기




Volumn 95, Issue 1, 2000, Pages 147-155

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

Author keywords

[No Author keywords available]

Indexed keywords

HEPARAN SULFATE; INTERLEUKIN 3; MATRIX PROTEIN;

EID: 0033957697     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v95.1.147.001k28_147_155     Document Type: Article
Times cited : (76)

References (65)
  • 1
    • 0026715931 scopus 로고
    • Stem cell factor induction of in vitro murine hematopoietic colony formation by "subliminal" cytokine combinations: The role of "anchor factors."
    • Lowry PA, Deacon D, Whitefield P, McGrath HE, Quesenberry PJ. Stem cell factor induction of in vitro murine hematopoietic colony formation by "subliminal" cytokine combinations: the role of "anchor factors." Blood. 1992;80:663-669.
    • (1992) Blood , vol.80 , pp. 663-669
    • Lowry, P.A.1    Deacon, D.2    Whitefield, P.3    McGrath, H.E.4    Quesenberry, P.J.5
  • 2
    • 0030722695 scopus 로고    scopus 로고
    • Microenvironmental regulation of hematopoietic stem cells
    • Lemischka IR. Microenvironmental regulation of hematopoietic stem cells. Stem Cells. 1997;15: 63-68.
    • (1997) Stem Cells , vol.15 , pp. 63-68
    • Lemischka, I.R.1
  • 3
    • 0030936580 scopus 로고    scopus 로고
    • Hematopoietic activity of a stromal cell transmembrane protein containing epidermal growth factor-like repeat motifs
    • Moore KA, Pytowski B, Witte L, Hicklin D, Lemischka IR. Hematopoietic activity of a stromal cell transmembrane protein containing epidermal growth factor-like repeat motifs. Proc Natl Acad Sci U S A. 1997;94:4011-4016.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 4011-4016
    • Moore, K.A.1    Pytowski, B.2    Witte, L.3    Hicklin, D.4    Lemischka, I.R.5
  • 4
    • 0031008521 scopus 로고    scopus 로고
    • In vitro maintenance of highly purified, transplantable hematopoietic stem cells
    • Moore KA, Ema H, Lemischka IR. In vitro maintenance of highly purified, transplantable hematopoietic stem cells. Blood. 1997;89:4337-4347.
    • (1997) Blood , vol.89 , pp. 4337-4347
    • Moore, K.A.1    Ema, H.2    Lemischka, I.R.3
  • 5
    • 0026661357 scopus 로고
    • Human hematopoietic stem cell adherence to cytokines and matrix molecules
    • Long MW, Briddell R, Walter AW, Bruno E, Hoffman R. Human hematopoietic stem cell adherence to cytokines and matrix molecules. J Clin Invest. 1992;90:251-255.
    • (1992) J Clin Invest , vol.90 , pp. 251-255
    • Long, M.W.1    Briddell, R.2    Walter, A.W.3    Bruno, E.4    Hoffman, R.5
  • 6
    • 0028346380 scopus 로고
    • Interaction of hepatocyte growth factor with heparan sulfate: Elucidation of the major heparan sulfate structural determinants
    • Lyon M, Deakin JA, Mizuno K, Nakamura T, Gallagher JT. Interaction of hepatocyte growth factor with heparan sulfate: elucidation of the major heparan sulfate structural determinants. J Biol Chem. 1994;269:11,216-11,223.
    • (1994) J Biol Chem , vol.269 , pp. 11216-11223
    • Lyon, M.1    Deakin, J.A.2    Mizuno, K.3    Nakamura, T.4    Gallagher, J.T.5
  • 7
    • 0027257980 scopus 로고
    • Mode of interaction between platelet factor 4 and heparin
    • Maccarana M, Lindahl U. Mode of interaction between platelet factor 4 and heparin. Glycobiology. 1993;3:271-277.
    • (1993) Glycobiology , vol.3 , pp. 271-277
    • Maccarana, M.1    Lindahl, U.2
  • 8
    • 0029024317 scopus 로고
    • FGF binding and FGF receptor activation by synthetic heparan-derived di- and trisaccharides
    • Ornitz DM, Herr AB, Nilsson M, Westman J, Svahn C-M, Waksman G. FGF binding and FGF receptor activation by synthetic heparan-derived di- and trisaccharides. Science. 1995;268:432-436.
    • (1995) Science , vol.268 , pp. 432-436
    • Ornitz, D.M.1    Herr, A.B.2    Nilsson, M.3    Westman, J.4    Svahn, C.-M.5    Waksman, G.6
  • 9
    • 0023928595 scopus 로고    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 RM. Heparan sulphate bound growth factors: a mechanism for stromal cell mediated haemopoiesis. Nature. 1998;332: 376-378.
    • (1998) Nature , vol.332 , pp. 376-378
    • Roberts, R.1    Gallagher, J.2    Spooncer, E.3    Allen, T.D.4    Bloomfield, F.5    Dexter, R.M.6
  • 10
    • 0027053914 scopus 로고    scopus 로고
    • Cell-associated proteoheparan sulfate mediates binding and uptake of thrombospondin in cultured porcine vascular endothelial cells
    • Schon P, Vischer P, Volker W, Schmidt A, Faber V. Cell-associated proteoheparan sulfate mediates binding and uptake of thrombospondin in cultured porcine vascular endothelial cells. Eur J Cell Biol. 59:329-339.
    • Eur J Cell Biol , vol.59 , pp. 329-339
    • Schon, P.1    Vischer, P.2    Volker, W.3    Schmidt, A.4    Faber, V.5
  • 11
    • 0026653353 scopus 로고
    • Effects of sized heparin oligosaccharides on the interactions of Chinese hamster ovary cells with thrombospondin
    • Sun X, Kaesberg PR, Choay J, Harenberg J, Ershler WB, Mosher DF. Effects of sized heparin oligosaccharides on the interactions of Chinese hamster ovary cells with thrombospondin. Semin Thromb Hemost. 1992;18:243-251.
    • (1992) Semin Thromb Hemost , vol.18 , pp. 243-251
    • Sun, X.1    Kaesberg, P.R.2    Choay, J.3    Harenberg, J.4    Ershler, W.B.5    Mosher, D.F.6
  • 12
    • 0026724478 scopus 로고
    • Colocalization of thrombospondin and syndecan during murine development
    • Corless CL, Mendoza A, Collins T, Lawler J. Colocalization of thrombospondin and syndecan during murine development. Dev Dyn. 1992;193: 346-358.
    • (1992) Dev Dyn , vol.193 , pp. 346-358
    • Corless, C.L.1    Mendoza, A.2    Collins, T.3    Lawler, J.4
  • 13
    • 0025953905 scopus 로고
    • Phospholipase C release of basic fibroblast growth factor from human bone marrow cultures as a biologically active complex with a phosphatidylinositol-anchored heparan sulfate proteoglycan
    • Brunner G, Gabrilove J, Rifkin DB, Wilson EL. Phospholipase C release of basic fibroblast growth factor from human bone marrow cultures as a biologically active complex with a phosphatidylinositol-anchored heparan sulfate proteoglycan. J Cell Biol. 1991;114:1275-1283.
    • (1991) J Cell Biol , vol.114 , pp. 1275-1283
    • Brunner, G.1    Gabrilove, J.2    Rifkin, D.B.3    Wilson, E.L.4
  • 14
    • 0027258527 scopus 로고
    • Specificity in the interactions of extracellular matrix proteins with subpopulations of the glycosaminoglycan heparin
    • San Antonio JD, Slover J, Lawler J, Karnovsky MJ, Lander AD. Specificity in the interactions of extracellular matrix proteins with subpopulations of the glycosaminoglycan heparin. Biochemistry. 1993;32:4746-4755.
    • (1993) Biochemistry , vol.32 , pp. 4746-4755
    • San Antonio, J.D.1    Slover, J.2    Lawler, J.3    Karnovsky, M.J.4    Lander, A.D.5
  • 15
    • 0026188978 scopus 로고
    • A new method for sequencing linear oligosaccharides on gels using charged, fluorescent conjugates
    • Lee KB, al-Hakim A, Loganathan D, Linhardt RJ. A new method for sequencing linear oligosaccharides on gels using charged, fluorescent conjugates. Carbohydr Res. 1991;214:155-168.
    • (1991) Carbohydr Res , vol.214 , pp. 155-168
    • Lee, K.B.1    Al-Hakim, A.2    Loganathan, D.3    Linhardt, R.J.4
  • 16
    • 0025355270 scopus 로고
    • Identification and characterization of an inhibitor of haemopoietic stem cell proliferation
    • Graham GJ, Wright EG, Hewick R, et al. Identification and characterization of an inhibitor of haemopoietic stem cell proliferation. Nature. 1990; 344:442-444.
    • (1990) Nature , vol.344 , pp. 442-444
    • Graham, G.J.1    Wright, E.G.2    Hewick, R.3
  • 17
    • 0030942527 scopus 로고    scopus 로고
    • A common precursor for primitive erythropoiesis and definitive haematopoiesis
    • Kennedy M, Firpo M, Choi K, et al. A common precursor for primitive erythropoiesis and definitive haematopoiesis. Nature. 1997;386:488-493.
    • (1997) Nature , vol.386 , pp. 488-493
    • Kennedy, M.1    Firpo, M.2    Choi, K.3
  • 18
    • 0027533021 scopus 로고
    • Synthesis and assembly of functionally active human vascular endothelial growth factor homodimers in insect cells
    • Fiebich BL, Jager B, Schollmann C, et al. Synthesis and assembly of functionally active human vascular endothelial growth factor homodimers in insect cells. Eur J Biochem. 1993;211:19-26.
    • (1993) Eur J Biochem , vol.211 , pp. 19-26
    • Fiebich, B.L.1    Jager, B.2    Schollmann, C.3
  • 19
    • 0026723142 scopus 로고
    • The binding of vascular endothelial growth factor to its receptors is dependent on cell surface-associated heparin-like molecules
    • Gitay-Goren H, Soker S, Vlodavsky I, Neufeld G. The binding of vascular endothelial growth factor to its receptors is dependent on cell surface-associated heparin-like molecules. J Biol Chem. 1992;267:6093-6098.
    • (1992) J Biol Chem , vol.267 , pp. 6093-6098
    • Gitay-Goren, H.1    Soker, S.2    Vlodavsky, I.3    Neufeld, G.4
  • 20
    • 0032055461 scopus 로고    scopus 로고
    • Natural killer and B-lymphoid potential in CD34+ cells derived from embryonic stem cells differentiated in the presence of vascular endothelial growth factor
    • Nakayama N, Fang I, Elliott G. Natural killer and B-lymphoid potential in CD34+ cells derived from embryonic stem cells differentiated in the presence of vascular endothelial growth factor. Blood. 1998;91:2283-2295.
    • (1998) Blood , vol.91 , pp. 2283-2295
    • Nakayama, N.1    Fang, I.2    Elliott, G.3
  • 21
    • 0029866647 scopus 로고    scopus 로고
    • Heparin structure and interactions with basic fibroblast growth factor
    • Faham S, Hileman RE, Fromm JR, Linhardt RJ, Rees DC. Heparin structure and interactions with basic fibroblast growth factor. Science. 1996;271: 1116-1120.
    • (1996) Science , vol.271 , pp. 1116-1120
    • Faham, S.1    Hileman, R.E.2    Fromm, J.R.3    Linhardt, R.J.4    Rees, D.C.5
  • 22
    • 0031749471 scopus 로고    scopus 로고
    • Physiological degradation converts the soluble syndecan-1 ectodomain from an inhibitor to a potent activator of FGF-2
    • Kato M, Wang H, Kainulainen V, et al. Physiological degradation converts the soluble syndecan-1 ectodomain from an inhibitor to a potent activator of FGF-2. Nature Med. 1998;4:691-697.
    • (1998) Nature Med , vol.4 , pp. 691-697
    • Kato, M.1    Wang, H.2    Kainulainen, V.3
  • 23
    • 0032574688 scopus 로고    scopus 로고
    • Hepatocyte growth factor/scatter factor has distinct classes of binding site in heparan sulfate from mammary cells
    • Rahmoune H, Rudland PS, Gallagher JT, Fernig DG. Hepatocyte growth factor/scatter factor has distinct classes of binding site in heparan sulfate from mammary cells. Biochemistry. 1998;37: 6003-6008.
    • (1998) Biochemistry , vol.37 , pp. 6003-6008
    • Rahmoune, H.1    Rudland, P.S.2    Gallagher, J.T.3    Fernig, D.G.4
  • 24
    • 0030796217 scopus 로고    scopus 로고
    • Specific binding of the chemokine platelet factor 4 to heparan sulfate
    • Stringer SE, Gallagher JT. Specific binding of the chemokine platelet factor 4 to heparan sulfate. J Biol Chem. 1997;272:20,508-20,514.
    • (1997) J Biol Chem , vol.272 , pp. 20508-20514
    • Stringer, S.E.1    Gallagher, J.T.2
  • 25
    • 0032577484 scopus 로고    scopus 로고
    • Age-dependent modulation of heparan sulfate structure and function
    • Feyzi E, Saldeen T, Larsson E, Lindahl U, Salmivirta M. Age-dependent modulation of heparan sulfate structure and function. J Biol Chem. 1998; 273:13,395-13,398.
    • (1998) J Biol Chem , vol.273 , pp. 13395-13398
    • Feyzi, E.1    Saldeen, T.2    Larsson, E.3    Lindahl, U.4    Salmivirta, M.5
  • 26
    • 0032535591 scopus 로고    scopus 로고
    • Structurally specific heparan sulfates support primitive human hematopoiesis by formation of a multimolecular stem cell niche
    • Gupta P, Oegema 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, T.R.2    Brazil, J.J.3    Dudek, A.Z.4    Slungaard, A.5    Verfaillie, C.M.6
  • 27
    • 0027366275 scopus 로고
    • Soluble factor(s) produced by human bone marrow stroma increase cytokine-induced proliferation and maturation of primitive hematopoietic progenitors while preventing their terminal differentiation
    • Verfaillie CM. Soluble factor(s) produced by human bone marrow stroma increase cytokine-induced proliferation and maturation of primitive hematopoietic progenitors while preventing their terminal differentiation. Blood. 1993;82:2045-2053.
    • (1993) Blood , vol.82 , pp. 2045-2053
    • Verfaillie, C.M.1
  • 28
    • 0026650764 scopus 로고
    • Direct contact between human primitive hematopoietic progenitors and bone marrow stroma is not required for long-term in vitro hematopoiesis
    • Verfaillie CM. Direct contact between human primitive hematopoietic progenitors and bone marrow stroma is not required for long-term in vitro hematopoiesis. Blood. 1992;79:2821-2826.
    • (1992) Blood , vol.79 , pp. 2821-2826
    • Verfaillie, C.M.1
  • 29
    • 0028058157 scopus 로고
    • Macrophage inflammatory protein-1α, interleukin 3 and diffusible marrow stromal factors maintain human hematopoietic stem cells for at least eight weeks in vitro
    • Verfaillie CM, Catanzarro PM, Li W. Macrophage inflammatory protein-1α, interleukin 3 and diffusible marrow stromal factors maintain human hematopoietic stem cells for at least eight weeks in vitro. J Exp Med. 1994;179:643-649.
    • (1994) J Exp Med , vol.179 , pp. 643-649
    • Verfaillie, C.M.1    Catanzarro, P.M.2    Li, W.3
  • 30
    • 0030849526 scopus 로고    scopus 로고
    • A clinically suitable ex vivo expansion culture system for LTC-IC and CFC using stroma-conditioned medium
    • Bhatia R, McGlave PB, Miller JS, Wissink S, Lin WN, Verfaillie CM. A clinically suitable ex vivo expansion culture system for LTC-IC and CFC using stroma-conditioned medium. Exp Hematol. 1997; 25:980-991.
    • (1997) Exp Hematol , vol.25 , pp. 980-991
    • Bhatia, R.1    McGlave, P.B.2    Miller, J.S.3    Wissink, S.4    Lin, W.N.5    Verfaillie, C.M.6
  • 31
    • 0027300330 scopus 로고
    • Comparative analysis of the human macrophage inflammatory protein family of cytokines (chemokines) on proliferation of human myeloid progenitor cells: Interacting effects involving suppression, synergistic suppression, and blocking of suppression
    • Broxmeyer HE, Sherry B, Cooper S, et al. Comparative analysis of the human macrophage inflammatory protein family of cytokines (chemokines) on proliferation of human myeloid progenitor cells: interacting effects involving suppression, synergistic suppression, and blocking of suppression. J Immunol. 1993;150:3448-3458.
    • (1993) J Immunol , vol.150 , pp. 3448-3458
    • Broxmeyer, H.E.1    Sherry, B.2    Cooper, S.3
  • 32
    • 0031810567 scopus 로고    scopus 로고
    • Ex vivo culture of CD34+/Lin-/DR-cells in stroma-derived soluble factors, interleukin-3, and macrophage inflammatory protein-1 alpha maintains not only myeloid but also lymphoid progenitors in a novel switch culture assay
    • Miller JS, McCullar V, Verfaillie CM. Ex vivo culture of CD34+/Lin-/DR-cells in stroma-derived soluble factors, interleukin-3, and macrophage inflammatory protein-1 alpha maintains not only myeloid but also lymphoid progenitors in a novel switch culture assay. Blood. 1998;91:4516-4522.
    • (1998) Blood , vol.91 , pp. 4516-4522
    • Miller, J.S.1    McCullar, V.2    Verfaillie, C.M.3
  • 34
    • 0029915836 scopus 로고    scopus 로고
    • Stromal fibroblast heparan sulfate is required for cytokine-mediated ex vivo maintenance of human long-term culture-initiating cells
    • Gupta P, McCarthy JB, Verfaillie CM. Stromal fibroblast heparan sulfate is required for cytokine-mediated ex vivo maintenance of human long-term culture-initiating cells. Blood. 1996;87:3229-3236.
    • (1996) Blood , vol.87 , pp. 3229-3236
    • Gupta, P.1    McCarthy, J.B.2    Verfaillie, C.M.3
  • 35
    • 0023105108 scopus 로고
    • Compartmentalization of a haematopoietic growth factor (GM-CSF) by glycosaminoglycans in the bone marrow microenvironment
    • Gordon MY, Riley GP, Watt SM, Greaves MF. Compartmentalization of a haematopoietic growth factor (GM-CSF) by glycosaminoglycans in the bone marrow microenvironment. Nature. 1987;326:403-405.
    • (1987) Nature , vol.326 , pp. 403-405
    • Gordon, M.Y.1    Riley, G.P.2    Watt, S.M.3    Greaves, M.F.4
  • 36
    • 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
  • 37
    • 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
  • 38
    • 0025337660 scopus 로고
    • Thrombospondin functions as a cytoadhesion molecule for human hematopoietic progenitor cells
    • Long MW, Dixit VM. Thrombospondin functions as a cytoadhesion molecule for human hematopoietic progenitor cells. Blood. 1990;75:2311-2318.
    • (1990) Blood , vol.75 , pp. 2311-2318
    • Long, M.W.1    Dixit, V.M.2
  • 40
    • 0020773654 scopus 로고
    • Very-high-field nmr studies of bovine lung heparan sulfate oligosaccharides produced by nitrous acid deaminative cleavage
    • Sanderson PN, Nieduszynski IA, Huckerby TN. Very-high-field nmr studies of bovine lung heparan sulfate oligosaccharides produced by nitrous acid deaminative cleavage. Biochem J. 1983;211: 677-682.
    • (1983) Biochem J , vol.211 , pp. 677-682
    • Sanderson, P.N.1    Nieduszynski, I.A.2    Huckerby, T.N.3
  • 42
    • 0017285685 scopus 로고
    • Synthesis of heparin-sepharoses and their binding with thrombin and antithrombin-heparin cofactor
    • Danishefsky I, Tzeng F, Ahrens M, Klein S. Synthesis of heparin-sepharoses and their binding with thrombin and antithrombin-heparin cofactor. Thromb Res. 1976;8:131-140.
    • (1976) Thromb Res , vol.8 , pp. 131-140
    • Danishefsky, I.1    Tzeng, F.2    Ahrens, M.3    Klein, S.4
  • 43
    • 0025030585 scopus 로고
    • Purified primitive human hematopoietic progenitor cells with long-term in vitro repopulating capacity adhere selectively to irradiated bone marrow stroma
    • Verfaillie CM, Blakolmer K, McGlave P. Purified primitive human hematopoietic progenitor cells with long-term in vitro repopulating capacity adhere selectively to irradiated bone marrow stroma. J Exp Med. 1990;172:509-512.
    • (1990) J Exp Med , vol.172 , pp. 509-512
    • Verfaillie, C.M.1    Blakolmer, K.2    McGlave, P.3
  • 44
    • 0019468220 scopus 로고
    • Limiting dilution assays for the determination of immunocompetent cell frequencies. I. Data analysis
    • Taswell C. Limiting dilution assays for the determination of immunocompetent cell frequencies. I. Data analysis. J Immunol. 1981;126:1614-1619.
    • (1981) J Immunol , vol.126 , pp. 1614-1619
    • Taswell, C.1
  • 45
    • 0025862954 scopus 로고
    • Analysis of affinity and structural selectivity in the binding of proteins to glycosaminoglycans: Development of a sensitive electrophoretic approach
    • Lee MK, Lander AD. Analysis of affinity and structural selectivity in the binding of proteins to glycosaminoglycans: development of a sensitive electrophoretic approach. Proc Natl Acad Sci U S A. 1991;88:2768-2772.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 2768-2772
    • Lee, M.K.1    Lander, A.D.2
  • 46
    • 0027158136 scopus 로고
    • Nature of the interaction of heparin with acidic fibroblast growth factor
    • Mach H, Volkin DB, Burke CJ, et al. Nature of the interaction of heparin with acidic fibroblast growth factor. Biochemistry. 1993;32:5480-5489.
    • (1993) Biochemistry , vol.32 , pp. 5480-5489
    • Mach, H.1    Volkin, D.B.2    Burke, C.J.3
  • 47
    • 0028065020 scopus 로고
    • Surface plasmon resonance based methods for measuring the kinetics and binding affinities of biomolecular interactions
    • Fisher RJ, Fivash M. Surface plasmon resonance based methods for measuring the kinetics and binding affinities of biomolecular interactions. Curr Opin Biotechnol. 1994;5:389-395.
    • (1994) Curr Opin Biotechnol , vol.5 , pp. 389-395
    • Fisher, R.J.1    Fivash, M.2
  • 48
    • 0029670002 scopus 로고    scopus 로고
    • Selective binding of VEGF121 to one of the three vascular endothelial growth factor receptors of vascular endothelial cells
    • Gitay-Goren H, Cohen T, Tessler S, et al. Selective binding of VEGF121 to one of the three vascular endothelial growth factor receptors of vascular endothelial cells. J Biol Chem. 1996;271: 5519-5523.
    • (1996) J Biol Chem , vol.271 , pp. 5519-5523
    • Gitay-Goren, H.1    Cohen, T.2    Tessler, S.3
  • 49
    • 0027751890 scopus 로고
    • The vascular endothelial growth factor (VEGF) isoforms: Differential deposition into the subepithelial extracellular matrix and bioactivity of extracellular matrix-bound VEGF
    • Park JE, Keller GA, Ferrara N. The vascular endothelial growth factor (VEGF) isoforms: differential deposition into the subepithelial extracellular matrix and bioactivity of extracellular matrix-bound VEGF. Mol Biol Cell. 1993;4:1317-1326.
    • (1993) Mol Biol Cell , vol.4 , pp. 1317-1326
    • Park, J.E.1    Keller, G.A.2    Ferrara, N.3
  • 50
    • 0032571310 scopus 로고    scopus 로고
    • Interaction of heparan sulfate from mammary cells with acidic fibroblast growth factor (FGF) and basic FGF. Regulation of the activity of basic FGF by high and low affinity binding sites in heparan sulfate
    • Rahmoune H, Chen HL, Gallagher JT, Rudland PS, Fernig DG. Interaction of heparan sulfate from mammary cells with acidic fibroblast growth factor (FGF) and basic FGF. Regulation of the activity of basic FGF by high and low affinity binding sites in heparan sulfate. J Biol Chem. 1998; 273:7303-7310.
    • (1998) J Biol Chem , vol.273 , pp. 7303-7310
    • Rahmoune, H.1    Chen, H.L.2    Gallagher, J.T.3    Rudland, P.S.4    Fernig, D.G.5
  • 51
    • 85084727031 scopus 로고    scopus 로고
    • Culture of human CD34+/HLA-DR-/LIN-cells for 4 weeks on the AFT024 stromal cell line results in extensive amplification of CD34+ cells with 3-100 fold expansion of LTC-IC, CFC and primitive lymphoid progenitors
    • Punzel M, Miller JS, Moore KA, Lemischka IR, Verfaillie CM. Culture of human CD34+/HLA-DR-/LIN-cells for 4 weeks on the AFT024 stromal cell line results in extensive amplification of CD34+ cells with 3-100 fold expansion of LTC-IC, CFC and primitive lymphoid progenitors [abstract]. Blood. 1997;90(10 suppl 1):161a.
    • (1997) Blood , vol.90 , Issue.10 SUPPL. 1
    • Punzel, M.1    Miller, J.S.2    Moore, K.A.3    Lemischka, I.R.4    Verfaillie, C.M.5
  • 52
    • 0342538323 scopus 로고    scopus 로고
    • Development of an in vitro assay that can enumerate generative multilineage-initiating cells (ML-IC) in adult human BM
    • Punzel M, Wissink S, Asleson K, et al. Development of an in vitro assay that can enumerate generative multilineage-initiating cells (ML-IC) in adult human BM [abstract]. Exp Hematol. 1998; 26:693.
    • (1998) Exp Hematol , vol.26 , pp. 693
    • Punzel, M.1    Wissink, S.2    Asleson, K.3
  • 53
    • 0031748725 scopus 로고    scopus 로고
    • The murine stromal cell line AFT024 acts specifically on human CD34+CD38- progenitors to maintain primitive function and immunophenotype in vitro
    • Thiemann FT, Moore KA, Smogorzewska EM, Lemischka IR, Crooks GM. The murine stromal cell line AFT024 acts specifically on human CD34+CD38-progenitors to maintain primitive function and immunophenotype in vitro. Exp Hematol. 1998;26:612-619.
    • (1998) Exp Hematol , vol.26 , pp. 612-619
    • Thiemann, F.T.1    Moore, K.A.2    Smogorzewska Em, L.I.R.3    Crooks, G.M.4
  • 54
    • 0032776874 scopus 로고    scopus 로고
    • Factor(s) secreted by AFT024 fetal liver cells following stimulation with human cytokines, are important for human LTC-IC growth
    • Punzel M, Gupta P, Roodell M, Mortari F, Verfaillie CM. Factor(s) secreted by AFT024 fetal liver cells following stimulation with human cytokines, are important for human LTC-IC growth. Leukemia 1999;7:1079-1084.
    • (1999) Leukemia , vol.7 , pp. 1079-1084
    • Punzel, M.1    Gupta, P.2    Roodell, M.3    Mortari, F.4    Verfaillie, C.M.5
  • 55
    • 0032147193 scopus 로고    scopus 로고
    • Negative regulation by interleukin-3 (IL-3) of mouse early B-cell progenitors and stem cells in culture: Transduction of the negative signals by betac and betaIL-3 proteins of IL-3 receptor and absence of negative regulation by granulocyte-macrophage colony-stimulating factor
    • Matsunaga T, Hirayama F, Yonemura Y, Murray R, Ogawa M. Negative regulation by interleukin-3 (IL-3) of mouse early B-cell progenitors and stem cells in culture: transduction of the negative signals by betac and betaIL-3 proteins of IL-3 receptor and absence of negative regulation by granulocyte-macrophage colony-stimulating factor. Blood. 1998;92:901-907.
    • (1998) Blood , vol.92 , pp. 901-907
    • Matsunaga, T.1    Hirayama, F.2    Yonemura, Y.3    Murray, R.4    Ogawa, M.5
  • 56
    • 0029923437 scopus 로고    scopus 로고
    • Interleukin 3 or interleukin 1 abrogates the reconstituting ability of hematopoietic stem cells
    • Yonemura Y, Ku H, Hirayama F, Souza LM, Ogawa M. Interleukin 3 or interleukin 1 abrogates the reconstituting ability of hematopoietic stem cells. Proc Natl Acad Sci U S A. 1996;93:4040-4044.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 4040-4044
    • Yonemura, Y.1    Ku, H.2    Hirayama, F.3    Souza, L.M.4    Ogawa, M.5
  • 57
    • 0025771278 scopus 로고
    • Differential effects of microenvironmentally presented interleukin 3 versus soluble growth factor on primitive human hematopoietic cells
    • Otsuka T, Thacker JD, Eaves CJ, Hogge DE. Differential effects of microenvironmentally presented interleukin 3 versus soluble growth factor on primitive human hematopoietic cells. J Clin Invest. 1991;88:417-422.
    • (1991) J Clin Invest , vol.88 , pp. 417-422
    • Otsuka, T.1    Thacker, J.D.2    Eaves, C.J.3    Hogge, D.E.4
  • 58
    • 0028062043 scopus 로고
    • Diffusible factors from the murine cell line M2-10B4 support human in vitro hematopoiesis
    • Burroughs J, Gupta P, Blazar BR, Verfaillie CM. Diffusible factors from the murine cell line M2-10B4 support human in vitro hematopoiesis. Exp Hematol. 1994;22:1095-1101.
    • (1994) Exp Hematol , vol.22 , pp. 1095-1101
    • Burroughs, J.1    Gupta, P.2    Blazar, B.R.3    Verfaillie, C.M.4
  • 59
    • 0026693272 scopus 로고
    • Biologic significance of constitutive and subliminal growth factor production by bone marrow stroma
    • Kittler EL, McGrath H, Temeles D, Crittenden RB, Kister VK, Quesenberry PJ. Biologic significance of constitutive and subliminal growth factor production by bone marrow stroma. Blood. 1992;79: 3168-3178.
    • (1992) Blood , vol.79 , pp. 3168-3178
    • Kittler, E.L.1    McGrath, H.2    Temeles, D.3    Crittenden, R.B.4    Kister, V.K.5    Quesenberry, P.J.6
  • 60
    • 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
  • 61
    • 0028608075 scopus 로고
    • Heparin-induced oligomerization of FGF molecules is responsible for FGF receptor dimerization, activation, and cell proliferation
    • Spivak-Kroizman T, Lemmon MA, Dikic I, et al. Heparin-induced oligomerization of FGF molecules is responsible for FGF receptor dimerization, activation, and cell proliferation. Cell. 1994; 79:1015-1024.
    • (1994) Cell , vol.79 , pp. 1015-1024
    • Spivak-Kroizman, T.1    Lemmon, M.A.2    Dikic, I.3
  • 62
    • 0027954917 scopus 로고
    • Homodimeric murine interleukin-3 agonists indicate that ligand dimerization is important for high-affinity receptor complex formation
    • Muther H, Kuhlcke K, Gessner A, Abdallah S, Lother H. Homodimeric murine interleukin-3 agonists indicate that ligand dimerization is important for high-affinity receptor complex formation. Growth Factors. 1994;10:17-27.
    • (1994) Growth Factors , vol.10 , pp. 17-27
    • Muther, H.1    Kuhlcke, K.2    Gessner, A.3    Abdallah, S.4    Lother, H.5
  • 63
    • 0029124099 scopus 로고
    • Heparin inhibits the expression of interleukin-11 and granulocyte-macrophage colony-stimulating factor in primate bone marrow stromal fibroblasts through mRNA destabilization
    • Yang L, Yang Y-C. Heparin inhibits the expression of interleukin-11 and granulocyte-macrophage colony-stimulating factor in primate bone marrow stromal fibroblasts through mRNA destabilization. Blood. 1995;86:2526-2533.
    • (1995) Blood , vol.86 , pp. 2526-2533
    • Yang, L.1    Yang, Y.-C.2
  • 64
    • 0029795565 scopus 로고    scopus 로고
    • Heparan sulfate: A piece of information
    • Salmivirta M, Lidholt K, Lindahl U. Heparan sulfate: a piece of information. FASEB J. 1996;10: 1270-1279.
    • (1996) FASEB J , vol.10 , pp. 1270-1279
    • Salmivirta, M.1    Lidholt, K.2    Lindahl, U.3
  • 65
    • 0031577166 scopus 로고    scopus 로고
    • Glycosaminoglycans can influence fibroblast growth factor-2 mitogenicity without significant growth factor binding
    • Wang H, Toida T, Kim YS, et al. Glycosaminoglycans can influence fibroblast growth factor-2 mitogenicity without significant growth factor binding. Biochem Biophys Res Commun. 1997;235: 369-373.
    • (1997) Biochem Biophys Res Commun , vol.235 , pp. 369-373
    • Wang, H.1    Toida, T.2    Kim, Y.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.