메뉴 건너뛰기




Volumn 28, Issue 3, 2007, Pages 371-382

The interrelated role of fibronectin and interleukin-1 in biomaterial-modulated macrophage function

Author keywords

Alveolar macrophage; Cytokine; Inflammation; Monocyte; PHSRN; RGD; Tyrosine phosphorylation

Indexed keywords

ALVEOLAR MACROPHAGE; CELLULAR ADHESION; CYTOKINE; EXTRACELLULAR MATRIX (ECM); FIBRONECTIN (FN); INFLAMMATION; MONOCYTE; TYROSINE PHOSPHORYLATION;

EID: 33750146181     PISSN: 01429612     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2006.08.041     Document Type: Review
Times cited : (58)

References (78)
  • 1
    • 0000228929 scopus 로고    scopus 로고
    • Inflammation, wound healing, and the foreign-body response
    • Ratner B.D., Hoffman A.S., Schoen F.J., and Lemons J.E. (Eds), Elsevier Academic Press, San Diego
    • Anderson J.M. Inflammation, wound healing, and the foreign-body response. In: Ratner B.D., Hoffman A.S., Schoen F.J., and Lemons J.E. (Eds). Biomaterials science. An introduction to materials in medicine (2004), Elsevier Academic Press, San Diego 296-304
    • (2004) Biomaterials science. An introduction to materials in medicine , pp. 296-304
    • Anderson, J.M.1
  • 2
    • 0034045243 scopus 로고    scopus 로고
    • Fibronectin peptides in cell migration and wound repair
    • Yamada, and Kenneth M. Fibronectin peptides in cell migration and wound repair. J Clin Invest 105 11 (2000) 1507-1509
    • (2000) J Clin Invest , vol.105 , Issue.11 , pp. 1507-1509
    • Yamada1    Kenneth, M.2
  • 3
    • 0035196741 scopus 로고    scopus 로고
    • Cutaneous wound healing: an update
    • Yamaguchi Y., and Kunihiko Y. Cutaneous wound healing: an update. J Dermatol 28 (2001) 521-534
    • (2001) J Dermatol , vol.28 , pp. 521-534
    • Yamaguchi, Y.1    Kunihiko, Y.2
  • 4
    • 33750189483 scopus 로고
    • Monocytes and macrophages
    • Graziano F.M., and Lemanske R.F. (Eds), Williams & Wilkins, Baltimore
    • Erickson C.M., and Albrecht R.M. Monocytes and macrophages. In: Graziano F.M., and Lemanske R.F. (Eds). Clinical immunology (1989), Williams & Wilkins, Baltimore 27-51
    • (1989) Clinical immunology , pp. 27-51
    • Erickson, C.M.1    Albrecht, R.M.2
  • 5
    • 0027525437 scopus 로고
    • Monocyte adherence to human vascular endothelium
    • Beekhuizen H., and van Furth R. Monocyte adherence to human vascular endothelium. J Leukoc Biol 54 (1993) 363-378
    • (1993) J Leukoc Biol , vol.54 , pp. 363-378
    • Beekhuizen, H.1    van Furth, R.2
  • 6
    • 84913893202 scopus 로고
    • Morphological identification of macrophages
    • Herscowitz H.B., Holden H.T., Bellanti J.A., and Ghaffar A. (Eds), Marcel Dekker, New York
    • Carr I. Morphological identification of macrophages. In: Herscowitz H.B., Holden H.T., Bellanti J.A., and Ghaffar A. (Eds). Manual of macrophage methodology (1981), Marcel Dekker, New York 187-198
    • (1981) Manual of macrophage methodology , pp. 187-198
    • Carr, I.1
  • 7
    • 0001294986 scopus 로고
    • Phagocytic cells: development and distribution of mononuclear phagocytes in normal steady state and inflammation
    • Gallin J.I., Goldstein I.M., and Snyderman R. (Eds), Raven Press, New York
    • Van Furth R. Phagocytic cells: development and distribution of mononuclear phagocytes in normal steady state and inflammation. In: Gallin J.I., Goldstein I.M., and Snyderman R. (Eds). Inflammation. Basic principles and clinical correlates (1988), Raven Press, New York 281-295
    • (1988) Inflammation. Basic principles and clinical correlates , pp. 281-295
    • Van Furth, R.1
  • 8
    • 0022468981 scopus 로고
    • Giant cell formation by peripheral human monocytes
    • Al-Sumidaie A.M. Giant cell formation by peripheral human monocytes. J Immunol Methods 91 (1986) 237-242
    • (1986) J Immunol Methods , vol.91 , pp. 237-242
    • Al-Sumidaie, A.M.1
  • 9
    • 0021243692 scopus 로고
    • Secretory products of macrophages and their physiological functions
    • Takemura R., and Werb Z. Secretory products of macrophages and their physiological functions. Am Physiol Soc (1984) C1-C9
    • (1984) Am Physiol Soc
    • Takemura, R.1    Werb, Z.2
  • 11
    • 0029979369 scopus 로고    scopus 로고
    • Biologic basis for interleukin-1 in disease
    • Dinarello C.A. Biologic basis for interleukin-1 in disease. Blood 87 6 (1996) 2095-2147
    • (1996) Blood , vol.87 , Issue.6 , pp. 2095-2147
    • Dinarello, C.A.1
  • 12
    • 0036694645 scopus 로고    scopus 로고
    • The balance between IL-1 and IL-1ra in disease
    • Arend W.P. The balance between IL-1 and IL-1ra in disease. Cytokine Growth Factor Rev 13 (2002) 323-340
    • (2002) Cytokine Growth Factor Rev , vol.13 , pp. 323-340
    • Arend, W.P.1
  • 15
    • 2942598764 scopus 로고    scopus 로고
    • Interleukin-1beta and interleukin-18: regulation and activity in local inflammation
    • Delaleu N., and Bickel M. Interleukin-1beta and interleukin-18: regulation and activity in local inflammation. Periodontol 2000 35 (2004) 42-52
    • (2004) Periodontol 2000 , vol.35 , pp. 42-52
    • Delaleu, N.1    Bickel, M.2
  • 16
    • 0023951485 scopus 로고
    • The kinetics of interleukin 1 secretion from activated monocytes. Differences between interleukin 1 alpha and interleukin 1 beta
    • Hazuda D.J., Lee J.C., and Young P.R. The kinetics of interleukin 1 secretion from activated monocytes. Differences between interleukin 1 alpha and interleukin 1 beta. J Biol Chem 263 17 (1988) 8473-8479
    • (1988) J Biol Chem , vol.263 , Issue.17 , pp. 8473-8479
    • Hazuda, D.J.1    Lee, J.C.2    Young, P.R.3
  • 17
    • 0033952161 scopus 로고    scopus 로고
    • Fibronectin fragments and their role in inflammatory arthritis
    • Barilla M.L., and Carsons S.E. Fibronectin fragments and their role in inflammatory arthritis. Semin Arthritis Rheum 29 4 (2000) 252-265
    • (2000) Semin Arthritis Rheum , vol.29 , Issue.4 , pp. 252-265
    • Barilla, M.L.1    Carsons, S.E.2
  • 18
    • 0042887252 scopus 로고    scopus 로고
    • The ins and outs of fibronectin matrix assembly
    • Wierzbicka-Patynowski I., and Schwarzbauer J.E. The ins and outs of fibronectin matrix assembly. J Cell Sci 116 (2003) 3269-3276
    • (2003) J Cell Sci , vol.116 , pp. 3269-3276
    • Wierzbicka-Patynowski, I.1    Schwarzbauer, J.E.2
  • 19
    • 0037107551 scopus 로고    scopus 로고
    • Fibronectin at a glance
    • Pankov R., and Yamada K.M. Fibronectin at a glance. J Cell Sci 115 (2002) 3861-3863
    • (2002) J Cell Sci , vol.115 , pp. 3861-3863
    • Pankov, R.1    Yamada, K.M.2
  • 20
    • 0030723421 scopus 로고    scopus 로고
    • Molecules in focus-fibronectin
    • Romberger D.J. Molecules in focus-fibronectin. Int J Biochem Cell Biol 29 7 (1997) 939-943
    • (1997) Int J Biochem Cell Biol , vol.29 , Issue.7 , pp. 939-943
    • Romberger, D.J.1
  • 21
    • 0028875886 scopus 로고
    • Alternative splicing of fibronectin-many different proteins but few different functions
    • Ffrench-Constant C. Alternative splicing of fibronectin-many different proteins but few different functions. Exp Cell Res 221 (1995) 261-271
    • (1995) Exp Cell Res , vol.221 , pp. 261-271
    • Ffrench-Constant, C.1
  • 22
    • 0029729982 scopus 로고    scopus 로고
    • Molecular variants of fibronectin and laminin: structure, physiological occurrence and histopathological aspects
    • Kosmehl H., Berndt A., and Katenkamp D. Molecular variants of fibronectin and laminin: structure, physiological occurrence and histopathological aspects. Virchows Arch 429 (1996) 311-322
    • (1996) Virchows Arch , vol.429 , pp. 311-322
    • Kosmehl, H.1    Berndt, A.2    Katenkamp, D.3
  • 23
    • 0033017948 scopus 로고    scopus 로고
    • The dynamic dialogue between cells and matrices: implications of fibronectin's elasticity
    • Hynes R.O. The dynamic dialogue between cells and matrices: implications of fibronectin's elasticity. Proc Natl Acad Sci USA 96 (1999) 2588-2590
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 2588-2590
    • Hynes, R.O.1
  • 24
    • 0036336106 scopus 로고    scopus 로고
    • Fibronectin in malignancy-effect of aging
    • Labat-Robert J. Fibronectin in malignancy-effect of aging. Semin Cancer Biol 12 (2002) 187-195
    • (2002) Semin Cancer Biol , vol.12 , pp. 187-195
    • Labat-Robert, J.1
  • 25
    • 0029775681 scopus 로고    scopus 로고
    • RGD and other recognition sequences for integrins
    • Ruoslahti E. RGD and other recognition sequences for integrins. Annu Rev Cell Dev Biol 12 (1996) 697-715
    • (1996) Annu Rev Cell Dev Biol , vol.12 , pp. 697-715
    • Ruoslahti, E.1
  • 26
    • 0035914421 scopus 로고    scopus 로고
    • The eighth FIII domain of human fibronectin promotes integrin α5β1 binding via stabilization of the ninth FIII domain
    • Altroff H., Van der Walle C.F., Asselin J., Fairless R., Campbell I.D., and Mardon H.J. The eighth FIII domain of human fibronectin promotes integrin α5β1 binding via stabilization of the ninth FIII domain. J Biol Chem 276 42 (2001) 38885-38892
    • (2001) J Biol Chem , vol.276 , Issue.42 , pp. 38885-38892
    • Altroff, H.1    Van der Walle, C.F.2    Asselin, J.3    Fairless, R.4    Campbell, I.D.5    Mardon, H.J.6
  • 27
    • 0034834329 scopus 로고    scopus 로고
    • Fibronectin, integrins, and growth control
    • Yamada K.M., and Danen E.H.J. Fibronectin, integrins, and growth control. J Cell Physiol 189 (2001) 1-13
    • (2001) J Cell Physiol , vol.189 , pp. 1-13
    • Yamada, K.M.1    Danen, E.H.J.2
  • 28
    • 0041559949 scopus 로고    scopus 로고
    • RGD modified polymers: biomaterials for stimulated cell adhesion and beyond
    • Hersel U., Dahmen C., and Kessle H. RGD modified polymers: biomaterials for stimulated cell adhesion and beyond. Biomaterials 24 (2003) 4385-4415
    • (2003) Biomaterials , vol.24 , pp. 4385-4415
    • Hersel, U.1    Dahmen, C.2    Kessle, H.3
  • 29
    • 84956680553 scopus 로고    scopus 로고
    • Tailoring biomaterials
    • Palsson B.O., and Bhata S.N. (Eds), Pearson Education, Inc., Upper Saddle River
    • Palsson B.O., and Bhata S.N. Tailoring biomaterials. In: Palsson B.O., and Bhata S.N. (Eds). Tissue Engineering (2004), Pearson Education, Inc., Upper Saddle River 270-287
    • (2004) Tissue Engineering , pp. 270-287
    • Palsson, B.O.1    Bhata, S.N.2
  • 30
    • 0029934877 scopus 로고    scopus 로고
    • Porphyomonas gingivalis Fimbrillin is one of the fibronectin-binding proteins
    • Murakami Y., et al. Porphyomonas gingivalis Fimbrillin is one of the fibronectin-binding proteins. Infect Immun 64 7 (1996) 2571-2576
    • (1996) Infect Immun , vol.64 , Issue.7 , pp. 2571-2576
    • Murakami, Y.1
  • 31
    • 0021564388 scopus 로고
    • The cell biology of macrophage activation
    • Adams D.O., and Hamilton T.A. The cell biology of macrophage activation. Annu Rev Immun 2 (1984) 283-318
    • (1984) Annu Rev Immun , vol.2 , pp. 283-318
    • Adams, D.O.1    Hamilton, T.A.2
  • 32
    • 0026786628 scopus 로고
    • Rebound elevation of fibronectin after tissue injury and ischemia: role of fibronectin synthesis
    • Thompson P.N., Cho E., Blumenstock F.A., Shah D.M., and Saba T.M. Rebound elevation of fibronectin after tissue injury and ischemia: role of fibronectin synthesis. Am J Physiol 263 26 (1992) G437-G445
    • (1992) Am J Physiol , vol.263 , Issue.26
    • Thompson, P.N.1    Cho, E.2    Blumenstock, F.A.3    Shah, D.M.4    Saba, T.M.5
  • 33
    • 0025729041 scopus 로고
    • Inhibition of in vitro differentiation of human monocytes to macrophages by lipopolysaccharides (LPS): phenotypic and functional analysis
    • Brugger W., Reinhardt D., Galanos C., and Andreesen R. Inhibition of in vitro differentiation of human monocytes to macrophages by lipopolysaccharides (LPS): phenotypic and functional analysis. Int Immunol 3 3 (1991) 221-227
    • (1991) Int Immunol , vol.3 , Issue.3 , pp. 221-227
    • Brugger, W.1    Reinhardt, D.2    Galanos, C.3    Andreesen, R.4
  • 34
    • 0023472768 scopus 로고
    • Stimulation of rat macrophage interleukin-1 secretion by plasma fibronectin
    • Beezhold D.H., and Lause D.B. Stimulation of rat macrophage interleukin-1 secretion by plasma fibronectin. Immunol Invest 16 5 (1987) 437-449
    • (1987) Immunol Invest , vol.16 , Issue.5 , pp. 437-449
    • Beezhold, D.H.1    Lause, D.B.2
  • 35
    • 0343776166 scopus 로고    scopus 로고
    • The contact of human macrophages with extracellular matrix proteins selectively induces expression of proinflammatory cytokines
    • Schiffer R., Klein B., Klosterhalfen, and Zwadlo-Klarwassar G. The contact of human macrophages with extracellular matrix proteins selectively induces expression of proinflammatory cytokines. Pathobiology 67 (1999) 233-235
    • (1999) Pathobiology , vol.67 , pp. 233-235
    • Schiffer, R.1    Klein, B.2    Klosterhalfen3    Zwadlo-Klarwassar, G.4
  • 36
    • 33745420183 scopus 로고    scopus 로고
    • Fibronectin modulates expression of interleukin-1 beta and its receptor antagonist in human mononuclear cells
    • Graves K.L., and Roman J. Fibronectin modulates expression of interleukin-1 beta and its receptor antagonist in human mononuclear cells. Am J Physiol Lung Cell Mol Physiol 271 1 (1996) L61-L69
    • (1996) Am J Physiol Lung Cell Mol Physiol , vol.271 , Issue.1
    • Graves, K.L.1    Roman, J.2
  • 37
    • 0030587962 scopus 로고    scopus 로고
    • Regulation of polymorphonuclear leukocyte cytokine receptor expression
    • Simms H.H., and D'Amico. Regulation of polymorphonuclear leukocyte cytokine receptor expression. J Immunol 157 (1996) 3605-3616
    • (1996) J Immunol , vol.157 , pp. 3605-3616
    • Simms, H.H.1    D'Amico2
  • 38
    • 0343580525 scopus 로고    scopus 로고
    • Integrin stimulation regulates polymorphonuclear leukocytes inflammatory cytokine expression
    • Simms H.H., D'Amico R., and Bland K.I. Integrin stimulation regulates polymorphonuclear leukocytes inflammatory cytokine expression. Ann Surg 225 6 (1997) 757-765
    • (1997) Ann Surg , vol.225 , Issue.6 , pp. 757-765
    • Simms, H.H.1    D'Amico, R.2    Bland, K.I.3
  • 39
    • 0032030721 scopus 로고    scopus 로고
    • Regulation of interleukin 1 signaling through integrin binding and actin reorganization: disparate effects of NF-kB and stress kinase pathways
    • Zhu P., Xiong W., Rodgers G., and Qwarnstrom E.E. Regulation of interleukin 1 signaling through integrin binding and actin reorganization: disparate effects of NF-kB and stress kinase pathways. Biochem J 330 (1998) 975-981
    • (1998) Biochem J , vol.330 , pp. 975-981
    • Zhu, P.1    Xiong, W.2    Rodgers, G.3    Qwarnstrom, E.E.4
  • 40
    • 0026848944 scopus 로고
    • Protein adsorption of biomedical polymers influences activated monocytes to produce fibroblast stimulating factors
    • Bonfield T.L., Colton E., and Anderson J.M. Protein adsorption of biomedical polymers influences activated monocytes to produce fibroblast stimulating factors. J Biomed Mater Res 26 (1992) 457-465
    • (1992) J Biomed Mater Res , vol.26 , pp. 457-465
    • Bonfield, T.L.1    Colton, E.2    Anderson, J.M.3
  • 41
    • 0026898254 scopus 로고
    • Cytokine and growth factor production by monocyte/macrophages on protein preadsorbed polymers
    • Bonfield T.L., Colton E., Merchant R.E., and Anderson J.M. Cytokine and growth factor production by monocyte/macrophages on protein preadsorbed polymers. J Biomed Mater Res 26 (1992) 837-850
    • (1992) J Biomed Mater Res , vol.26 , pp. 837-850
    • Bonfield, T.L.1    Colton, E.2    Merchant, R.E.3    Anderson, J.M.4
  • 42
    • 0029188337 scopus 로고
    • Protein adsorption and macrophage activation on polydimethylsiloxane and silicone rubber
    • Anderson J.M., et al. Protein adsorption and macrophage activation on polydimethylsiloxane and silicone rubber. J Biomater Sci Polym Ed 7 2 (1995) 159-169
    • (1995) J Biomater Sci Polym Ed , vol.7 , Issue.2 , pp. 159-169
    • Anderson, J.M.1
  • 43
    • 0030152637 scopus 로고    scopus 로고
    • Monocyte activation on titanium-sputtered polystyrene surfaces in vitro: the effect of culture conditions on interleukin-1 release
    • Gretzer C., Eriksson A.S., Alden B., Ericson L.E., and Thomsen P. Monocyte activation on titanium-sputtered polystyrene surfaces in vitro: the effect of culture conditions on interleukin-1 release. Biomaterials 17 (1996) 851-858
    • (1996) Biomaterials , vol.17 , pp. 851-858
    • Gretzer, C.1    Eriksson, A.S.2    Alden, B.3    Ericson, L.E.4    Thomsen, P.5
  • 44
    • 0031745848 scopus 로고    scopus 로고
    • Adhesion elicits an intrinsic defect in interleukin-1 expression by macrophages from autoimmune-prone MRL mice
    • Levine J.S., Koh J.S., Hartwell D., and Beller D.I. Adhesion elicits an intrinsic defect in interleukin-1 expression by macrophages from autoimmune-prone MRL mice. J Autoimmun 11 (1998) 141-150
    • (1998) J Autoimmun , vol.11 , pp. 141-150
    • Levine, J.S.1    Koh, J.S.2    Hartwell, D.3    Beller, D.I.4
  • 45
    • 0035075879 scopus 로고    scopus 로고
    • Fibronectin regulates the activation of THP-1 cells by TGF-β1
    • Wang A.C.C., and Fu L. Fibronectin regulates the activation of THP-1 cells by TGF-β1. Inflamm Res 50 (2001) 142-148
    • (2001) Inflamm Res , vol.50 , pp. 142-148
    • Wang, A.C.C.1    Fu, L.2
  • 47
    • 0028030408 scopus 로고
    • The role of protein tyrosine phosphorylation in integrin-mediated gene induction in monocytes
    • Lin T.H., Yurochko A., Kornberg L., Morris J., Walker J.J., Haskill S., et al. The role of protein tyrosine phosphorylation in integrin-mediated gene induction in monocytes. J Cell Biol 126 6 (1994) 1585-1593
    • (1994) J Cell Biol , vol.126 , Issue.6 , pp. 1585-1593
    • Lin, T.H.1    Yurochko, A.2    Kornberg, L.3    Morris, J.4    Walker, J.J.5    Haskill, S.6
  • 48
    • 0029005762 scopus 로고
    • Integrin-mediated tyrosine phosphorylation and cytokine message induction in monocytic cells-a possible signaling role for the syk tyrosine kinase
    • Lin T.H., Rosales C., Mondal K., Bolen J.B., Haskill S., and Juliano R.L. Integrin-mediated tyrosine phosphorylation and cytokine message induction in monocytic cells-a possible signaling role for the syk tyrosine kinase. J Biol Chem 270 27 (1995) 16179-16189
    • (1995) J Biol Chem , vol.270 , Issue.27 , pp. 16179-16189
    • Lin, T.H.1    Rosales, C.2    Mondal, K.3    Bolen, J.B.4    Haskill, S.5    Juliano, R.L.6
  • 49
    • 0026756730 scopus 로고
    • Integrins as a primary signal transduction molecule regulating monocyte intermediate-early gene induction
    • Yurochko A.D., Liu D.Y., Eierman D., and Haskill S. Integrins as a primary signal transduction molecule regulating monocyte intermediate-early gene induction. Proc Natl Acad Sci USA 89 19 (1992) 9034-9038
    • (1992) Proc Natl Acad Sci USA , vol.89 , Issue.19 , pp. 9034-9038
    • Yurochko, A.D.1    Liu, D.Y.2    Eierman, D.3    Haskill, S.4
  • 50
    • 33645960432 scopus 로고    scopus 로고
    • Effect of surface-adsorbed proteins and phosphorylation inhibitor AG18 on intracellular protein expression in adherent macrophages
    • Zuckerman S.T., and Kao W.J. Effect of surface-adsorbed proteins and phosphorylation inhibitor AG18 on intracellular protein expression in adherent macrophages. Biomaterials 27 (2006) 3745-3757
    • (2006) Biomaterials , vol.27 , pp. 3745-3757
    • Zuckerman, S.T.1    Kao, W.J.2
  • 51
    • 33750156917 scopus 로고    scopus 로고
    • Zuckerman ST, Kao WJ. LC/MS identification of 12 intracellular cytoskeletal and inflammatory proteins from monocytes adherent on surface-adsorbed fibronectin-derived peptides. Journal of Biomedical Materials Research 2006, submitted.
  • 52
    • 0028903979 scopus 로고
    • Effects of fibronectin and group B streptococci on tumour necrosis factor-alpha production by human culture-derived macrophages
    • Peat E.B., Augustine N.H., Drummond W.K., and Bohnsack Hill H.R. Effects of fibronectin and group B streptococci on tumour necrosis factor-alpha production by human culture-derived macrophages. Immunology 84 (1995) 440-445
    • (1995) Immunology , vol.84 , pp. 440-445
    • Peat, E.B.1    Augustine, N.H.2    Drummond, W.K.3    Bohnsack Hill, H.R.4
  • 53
    • 0026006260 scopus 로고
    • The proinflammatory cytokines interleukin-1 and tumor necrosis factor and the treatment of septic shock syndrome
    • Dinarello C.A. The proinflammatory cytokines interleukin-1 and tumor necrosis factor and the treatment of septic shock syndrome. J Infect Dis 163 (1991) 1177-1184
    • (1991) J Infect Dis , vol.163 , pp. 1177-1184
    • Dinarello, C.A.1
  • 55
    • 0029745365 scopus 로고    scopus 로고
    • Interleukin-4-induced macrophage fusion is prevented by inhibitors of mannose receptor activity
    • McNally A.K., DeFife K.M., and Anderson J.M. Interleukin-4-induced macrophage fusion is prevented by inhibitors of mannose receptor activity. Am J Pathol 149 3 (1996) 975-985
    • (1996) Am J Pathol , vol.149 , Issue.3 , pp. 975-985
    • McNally, A.K.1    DeFife, K.M.2    Anderson, J.M.3
  • 56
    • 0026717870 scopus 로고
    • Human neutrophils produce high levels of the interleukin-1 receptor antagonist in response to granulocyte/macrophage colony-stimulating factor and tumor necrosis factor alpha
    • McColl S.R., Paquin R., Menard C., and Beaulieu A.D. Human neutrophils produce high levels of the interleukin-1 receptor antagonist in response to granulocyte/macrophage colony-stimulating factor and tumor necrosis factor alpha. J Exp Med 176 (1992) 593-598
    • (1992) J Exp Med , vol.176 , pp. 593-598
    • McColl, S.R.1    Paquin, R.2    Menard, C.3    Beaulieu, A.D.4
  • 57
    • 0027971378 scopus 로고
    • The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell-adhesive function
    • Aota S., Nomizu M., and Yamada K.M. The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell-adhesive function. J Biol Chem 269 (1994) 24756-24761
    • (1994) J Biol Chem , vol.269 , pp. 24756-24761
    • Aota, S.1    Nomizu, M.2    Yamada, K.M.3
  • 58
    • 0035806227 scopus 로고    scopus 로고
    • Amino acids and peptides. Part 39: a bivalent poly(ethylene glycol) hybrid containing an active site (RGD) and its synergistic site (PHSRN) of fibronectin
    • Hojo K., Sususki Y., Maeda M., Okazaki I., Nomizu M., Kamada H., et al. Amino acids and peptides. Part 39: a bivalent poly(ethylene glycol) hybrid containing an active site (RGD) and its synergistic site (PHSRN) of fibronectin. Bioorg Med Chem Lett 11 2001 (2001) 1429-1432
    • (2001) Bioorg Med Chem Lett , vol.11 , Issue.2001 , pp. 1429-1432
    • Hojo, K.1    Sususki, Y.2    Maeda, M.3    Okazaki, I.4    Nomizu, M.5    Kamada, H.6
  • 59
    • 15244349103 scopus 로고    scopus 로고
    • The effect on osteoblasts function of colocalized RGD and PHSRN epitopes on PEG surfaces
    • Benoit D.S.W., and Anseth K.S. The effect on osteoblasts function of colocalized RGD and PHSRN epitopes on PEG surfaces. Biomaterials 26 (2005) 5209-5220
    • (2005) Biomaterials , vol.26 , pp. 5209-5220
    • Benoit, D.S.W.1    Anseth, K.S.2
  • 60
    • 0028953177 scopus 로고
    • Activation of human lymphomononuclear cells by peptides derived from extracellular matrix proteins
    • Lopez-Moratalla N., et al. Activation of human lymphomononuclear cells by peptides derived from extracellular matrix proteins. Biochim Biophys Acta 1265 (1995) 181-188
    • (1995) Biochim Biophys Acta , vol.1265 , pp. 181-188
    • Lopez-Moratalla, N.1
  • 61
    • 0032486576 scopus 로고    scopus 로고
    • Murine macrophage behavior on peptide-grafted polyethyleneglycol-containing networks
    • Kao W.J., and Hubbell J.A. Murine macrophage behavior on peptide-grafted polyethyleneglycol-containing networks. Biotechnol Bioeng 59 1 (1998)
    • (1998) Biotechnol Bioeng , vol.59 , Issue.1
    • Kao, W.J.1    Hubbell, J.A.2
  • 62
    • 17744412490 scopus 로고    scopus 로고
    • Utilizing biomimetic oligopeptides to probe fibronectin-integrin binding and signaling in regulating macrophage function in vitro and in vivo
    • Kao W.J., and Liu Y. Utilizing biomimetic oligopeptides to probe fibronectin-integrin binding and signaling in regulating macrophage function in vitro and in vivo. Front Biosci 6 (2001) d992-d999
    • (2001) Front Biosci , vol.6
    • Kao, W.J.1    Liu, Y.2
  • 63
    • 0036141244 scopus 로고    scopus 로고
    • Human macrophage adhesion on fibronectin: the role of substratum and intracellular signaling kinases
    • Liu Y., and Kao W.J. Human macrophage adhesion on fibronectin: the role of substratum and intracellular signaling kinases. Cell Signal 14 (2002) 145-152
    • (2002) Cell Signal , vol.14 , pp. 145-152
    • Liu, Y.1    Kao, W.J.2
  • 64
    • 33750196434 scopus 로고    scopus 로고
    • Chung A, Gao Q, Kao WJ. Integrin-mediated macrophage adhesion, gene, and protein expression to multifunctional matrices containing ECM-derived molecules. Biomaterials 2006, in press.
  • 65
    • 33750147491 scopus 로고    scopus 로고
    • Gao Q, Chung A, Kao WJ. Monocytic U937 adhesion, TNF-α and IL-1β expression in response to gelatin-based networks grafted with RGD and PHSRN oligopeptides. Tissue Eng 2006, in press.
  • 66
    • 0025431082 scopus 로고
    • Alveolar macrophage: origin, kinetics and relationship with cells of the alveolo-interstitial region
    • Perez-Arellano J.L., Alcazar-Montero M.C., and Jimenez-Lopez A. Alveolar macrophage: origin, kinetics and relationship with cells of the alveolo-interstitial region. Allergol Immunopathol 18 3 (1990) 175-183
    • (1990) Allergol Immunopathol , vol.18 , Issue.3 , pp. 175-183
    • Perez-Arellano, J.L.1    Alcazar-Montero, M.C.2    Jimenez-Lopez, A.3
  • 67
    • 0026279296 scopus 로고
    • Interleukin-8 gene expression from human alveolar macrophages: the role of adherence
    • Standiford T.J., Kunkel S.L., Kasahara K., et al. Interleukin-8 gene expression from human alveolar macrophages: the role of adherence. Am J Respir Cell Mol Biol 5 (1991) 579-585
    • (1991) Am J Respir Cell Mol Biol , vol.5 , pp. 579-585
    • Standiford, T.J.1    Kunkel, S.L.2    Kasahara, K.3
  • 68
    • 30344449735 scopus 로고    scopus 로고
    • Respiratory burst: role in signal transduction in alveolar macrophages
    • Gwinn M.R., and Vallyathan V. Respiratory burst: role in signal transduction in alveolar macrophages. J Toxicol Environ Health B 9 1 (2006) 27-39
    • (2006) J Toxicol Environ Health B , vol.9 , Issue.1 , pp. 27-39
    • Gwinn, M.R.1    Vallyathan, V.2
  • 69
    • 21744448376 scopus 로고    scopus 로고
    • Alveolar macrophages in chronic obstructive pulmonary disease (COPD)
    • Barnes P.J. Alveolar macrophages in chronic obstructive pulmonary disease (COPD). Cell Mol Biol 50 (2004) OL627-OL637
    • (2004) Cell Mol Biol , vol.50
    • Barnes, P.J.1
  • 71
    • 0028201058 scopus 로고
    • Ozone-induced release of cytokines and firbonectin by alveolar macrophages and airway epithelial cells
    • Devlin R.B., McKinnon K.P., Noah T., Becker S., and Koren S.H. Ozone-induced release of cytokines and firbonectin by alveolar macrophages and airway epithelial cells. Am J Physiol 266 1 (1994) L612-L619
    • (1994) Am J Physiol , vol.266 , Issue.1
    • Devlin, R.B.1    McKinnon, K.P.2    Noah, T.3    Becker, S.4    Koren, S.H.5
  • 72
    • 0028503301 scopus 로고
    • Enhanced production of interleukin-1, tumor-necrosis-factor-alpha, and fibronectin by rat lung phagocytes following inhalation of a pulmonary irritant
    • Pendrino K.J., Shuler R.L., Laskin J.D., and Laskin D.L. Enhanced production of interleukin-1, tumor-necrosis-factor-alpha, and fibronectin by rat lung phagocytes following inhalation of a pulmonary irritant. Am J Respir Cell Mol Biol 11 3 (1994) 279-286
    • (1994) Am J Respir Cell Mol Biol , vol.11 , Issue.3 , pp. 279-286
    • Pendrino, K.J.1    Shuler, R.L.2    Laskin, J.D.3    Laskin, D.L.4
  • 73
    • 21244506485 scopus 로고    scopus 로고
    • Use of bronchoalveolar lavage to detect repiratory tract toxicity of inhaled material
    • Henderson R.F. Use of bronchoalveolar lavage to detect repiratory tract toxicity of inhaled material. Exp Toxicol Pathol 57 (2005) 155-159
    • (2005) Exp Toxicol Pathol , vol.57 , pp. 155-159
    • Henderson, R.F.1
  • 74
    • 0027212844 scopus 로고
    • Enhanced IL-1β and tumor necrosis factor-α release and messenger RNA expression in macrophages from idiopathic pulmonary fibrosis or after asbestos exposure
    • Zhang Y., Lee T.C., Guillemin B., Yu M- C., and Rom W.N. Enhanced IL-1β and tumor necrosis factor-α release and messenger RNA expression in macrophages from idiopathic pulmonary fibrosis or after asbestos exposure. J Immunol 150 9 (1993) 4188-4196
    • (1993) J Immunol , vol.150 , Issue.9 , pp. 4188-4196
    • Zhang, Y.1    Lee, T.C.2    Guillemin, B.3    Yu M-, C.4    Rom, W.N.5
  • 75
    • 0028869226 scopus 로고
    • Alveolar macrophage cytokine and growth-factor production in a rat model of crocidolite-induced pulmonary inflammation and fibrosis
    • Driscoll K.E., Maurer J.K., Higgins J., and Poynter J. Alveolar macrophage cytokine and growth-factor production in a rat model of crocidolite-induced pulmonary inflammation and fibrosis. J Toxicol Environ Health 46 2 (1995) 155-169
    • (1995) J Toxicol Environ Health , vol.46 , Issue.2 , pp. 155-169
    • Driscoll, K.E.1    Maurer, J.K.2    Higgins, J.3    Poynter, J.4
  • 76
    • 0026323213 scopus 로고
    • Cytokine and growth factor release by alveolar macrophages: potential biomarkers of pulmonary toxicity
    • Driscoll K.E., and Maurer J.K. Cytokine and growth factor release by alveolar macrophages: potential biomarkers of pulmonary toxicity. Toxicol Pathol 19 4 (1991) 398-405
    • (1991) Toxicol Pathol , vol.19 , Issue.4 , pp. 398-405
    • Driscoll, K.E.1    Maurer, J.K.2
  • 78
    • 0029075346 scopus 로고
    • Lung toxicity of hard metal particles and production of interleukin-1, tumor necrosis factor-α, fibronectin, and cystatin-c by lung phagocytes
    • Huaux F., Lasfargues G., Lauwerys R., and Lison D. Lung toxicity of hard metal particles and production of interleukin-1, tumor necrosis factor-α, fibronectin, and cystatin-c by lung phagocytes. Toxicol Appl Pharmacol 132 (1995) 53-62
    • (1995) Toxicol Appl Pharmacol , vol.132 , pp. 53-62
    • Huaux, F.1    Lasfargues, G.2    Lauwerys, R.3    Lison, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.