메뉴 건너뛰기




Volumn 4, Issue 189, 2011, Pages

Small molecule-mediated activation of the integrin CD11b/CD18 reduces inflammatory disease

Author keywords

[No Author keywords available]

Indexed keywords

ANTIINFLAMMATORY AGENT; CD11B ANTIGEN; CD18 ANTIGEN; LEUKADHERIN 1; LEUKADHERIN 2; LEUKADHERIN 3; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY M1 70; UNCLASSIFIED DRUG; CALCIUM; MAGNESIUM; MANGANESE;

EID: 80052573917     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.2001811     Document Type: Article
Times cited : (104)

References (83)
  • 1
    • 0025255615 scopus 로고
    • Structure and function of the leukocyte adhesion molecules CD11/CD18
    • M. A. Arnaout, Structure and function of the leukocyte adhesion molecules CD11/CD18. Blood 75, 1037-1050 (1990).
    • (1990) Blood , vol.75 , pp. 1037-1050
    • Arnaout, M.A.1
  • 2
    • 34548230927 scopus 로고    scopus 로고
    • Getting to the site of inflammation: The leukocyte adhesion cascade updated
    • K. Ley, C. Laudanna, M. I. Cybulsky, S. Nourshargh, Getting to the site of inflammation: The leukocyte adhesion cascade updated. Nat. Rev. Immunol. 7, 678-689 (2007).
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 678-689
    • Ley, K.1    Laudanna, C.2    Cybulsky, M.I.3    Nourshargh, S.4
  • 4
    • 0023891934 scopus 로고
    • The saturable high affinity association of factor X to ADP-stimulated monocytes defines a novel function of the Mac-1 receptor
    • D. C. Altieri, T. S. Edgington, The saturable high affinity association of factor X to ADP-stimulated monocytes defines a novel function of the Mac-1 receptor. J. Biol. Chem. 263, 7007-7015 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 7007-7015
    • Altieri, D.C.1    Edgington, T.S.2
  • 6
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • R. O. Hynes, Integrins: Bidirectional, allosteric signaling machines. Cell 110, 673-687 (2002).
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 7
    • 0027156112 scopus 로고
    • Functional inactivation of neutrophils with a Mac-1 (CD11b/CD18) monoclonal antibody protects against ischemia-reperfusion injury in rat liver
    • H. Jaeschke, A. Farhood, A. P. Bautista, Z. Spolarics, J. J. Spitzer, C. W. Smith, Functional inactivation of neutrophils with a Mac-1 (CD11b/CD18) monoclonal antibody protects against ischemia-reperfusion injury in rat liver. Hepatology 17, 915-923 (1993).
    • (1993) Hepatology , vol.17 , pp. 915-923
    • Jaeschke, H.1    Farhood, A.2    Bautista, A.P.3    Spolarics, Z.4    Spitzer, J.J.5    Smith, C.W.6
  • 8
    • 0032543958 scopus 로고    scopus 로고
    • 2-leukocyte integrin Mac-1 (CD11b/CD18) reduces intimal thickening after angioplasty or stent implantation in rabbits
    • 2- leukocyte integrin Mac-1 (CD11b/CD18) reduces intimal thickening after angioplasty or stent implantation in rabbits. Proc. Natl. Acad. Sci. U.S.A. 95, 10134-10139 (1998).
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 10134-10139
    • Rogers, C.1    Edelman, E.R.2    Simon, D.I.3
  • 11
    • 0033869420 scopus 로고    scopus 로고
    • CD18 trials disappoint again
    • A. Dove, CD18 trials disappoint again. Nat. Biotechnol. 18, 817-818 (2000).
    • (2000) Nat. Biotechnol. , vol.18 , pp. 817-818
    • Dove, A.1
  • 12
    • 0036254688 scopus 로고    scopus 로고
    • Leukocyte-endothelial interactions: Clinical trials of antiadhesion therapy
    • J. M. Harlan, R. K. Winn, Leukocyte-endothelial interactions: Clinical trials of antiadhesion therapy. Crit. Care Med. 30, S214-S219 (2002).
    • (2002) Crit. Care Med. , vol.30
    • Harlan, J.M.1    Winn, R.K.2
  • 14
    • 0026438977 scopus 로고
    • Recruitment of CD11b/CD18 to the neutrophil surface and adherence-dependent cell locomotion
    • B. J. Hughes, J. C. Hollers, E. Crockett-Torabi, C.W. Smith, Recruitment of CD11b/CD18 to the neutrophil surface and adherence-dependent cell locomotion. J. Clin. Invest. 90, 1687-1696 (1992).
    • (1992) J. Clin. Invest. , vol.90 , pp. 1687-1696
    • Hughes, B.J.1    Hollers, J.C.2    Crockett-Torabi, E.3    Smith, C.W.4
  • 15
    • 0037036421 scopus 로고    scopus 로고
    • Dynamic regulation of LFA-1 activation and neutrophil arrest on intercellular adhesion molecule 1 (ICAM-1) in shear flow
    • A. F. Lum, C. E. Green, G. R. Lee, D. E. Staunton, S. I. Simon, Dynamic regulation of LFA-1 activation and neutrophil arrest on intercellular adhesion molecule 1 (ICAM-1) in shear flow. J. Biol. Chem. 277, 20660-20670 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 20660-20670
    • Lum, A.F.1    Green, C.E.2    Lee, G.R.3    Staunton, D.E.4    Simon, S.I.5
  • 16
    • 70349172267 scopus 로고    scopus 로고
    • Therapy: Targeted but not trouble-free: Efalizumab and PML
    • E. S. Molloy, L. H. Calabrese, Therapy: Targeted but not trouble-free: Efalizumab and PML. Nat. Rev. Rheumatol. 5, 418-419 (2009).
    • (2009) Nat. Rev. Rheumatol. , vol.5 , pp. 418-419
    • Molloy, E.S.1    Calabrese, L.H.2
  • 19
    • 77949884325 scopus 로고    scopus 로고
    • Distinct roles for LFA-1 affinity regulation during T-cell adhesion, diapedesis, and interstitial migration in lymph nodes
    • E. J. Park, A. Peixoto, Y. Imai, A. Goodarzi, G. Cheng, C. V. Carman, U. H. von Andrian, M. Shimaoka, Distinct roles for LFA-1 affinity regulation during T-cell adhesion, diapedesis, and interstitial migration in lymph nodes. Blood 115, 1572-1581 (2010).
    • (2010) Blood , vol.115 , pp. 1572-1581
    • Park, E.J.1    Peixoto, A.2    Imai, Y.3    Goodarzi, A.4    Cheng, G.5    Carman, C.V.6    Von Andrian, U.H.7    Shimaoka, M.8
  • 21
    • 0027398448 scopus 로고
    • A subpopulation of Mac-1 (CD11b/CD18) molecules mediates neutrophil adhesion to ICAM-1 and fibrinogen
    • M. S. Diamond, T. A. Springer, A subpopulation of Mac-1 (CD11b/CD18) molecules mediates neutrophil adhesion to ICAM-1 and fibrinogen. J. Cell Biol. 120, 545-556 (1993).
    • (1993) J. Cell Biol. , vol.120 , pp. 545-556
    • Diamond, M.S.1    Springer, T.A.2
  • 22
    • 34047128107 scopus 로고    scopus 로고
    • A simple, no-wash cell adhesion-based high-throughput assay for the discovery of small-molecule regulators of the integrin CD11b/CD18
    • J. Y. Park, M. A. Arnaout, V. Gupta, A simple, no-wash cell adhesion-based high-throughput assay for the discovery of small-molecule regulators of the integrin CD11b/CD18. J. Biomol. Screen. 12, 406-417 (2007).
    • (2007) J. Biomol. Screen. , vol.12 , pp. 406-417
    • Park, J.Y.1    Arnaout, M.A.2    Gupta, V.3
  • 25
    • 2942532190 scopus 로고    scopus 로고
    • Binding affinity of metal ions to the CD11b A-domain is regulated by integrin activation and ligands
    • K. Ajroud, T. Sugimori, W. H. Goldmann, D. M. Fathallah, J. P. Xiong, M. A. Arnaout, Binding affinity of metal ions to the CD11b A-domain is regulated by integrin activation and ligands. J. Biol. Chem. 279, 25483-25488 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 25483-25488
    • Ajroud, K.1    Sugimori, T.2    Goldmann, W.H.3    Fathallah, D.M.4    Xiong, J.P.5    Arnaout, M.A.6
  • 26
    • 0027483226 scopus 로고
    • 2 integrin CR3 (CD11b/CD18) is essential for ligand binding
    • 2 integrin CR3 (CD11b/CD18) is essential for ligand binding. Cell 72, 857-867 (1993).
    • (1993) Cell , vol.72 , pp. 857-867
    • Michishita, M.1    Videm, V.2    Arnaout, M.A.3
  • 28
    • 0026040946 scopus 로고
    • Occupancy of CD11b/CD18 (Mac-1) divalent ion binding site(s) induces leukocyte adhesion
    • D. C. Altieri, Occupancy of CD11b/CD18 (Mac-1) divalent ion binding site(s) induces leukocyte adhesion. J. Immunol. 147, 1891-1898 (1991).
    • (1991) J. Immunol. , vol.147 , pp. 1891-1898
    • Altieri, D.C.1
  • 30
    • 0020563394 scopus 로고
    • Inhibition of phagocytosis of complement C3- or immunoglobulin G-coated particles and of C3bi binding by monoclonal antibodies to a monocyte-granulocyte membrane glycoprotein (Mol)
    • M. A. Arnaout, R. F. Todd III, N. Dana, J. Melamed, S. F. Schlossman, H. R. Colten, Inhibition of phagocytosis of complement C3- or immunoglobulin G-coated particles and of C3bi binding by monoclonal antibodies to a monocyte-granulocyte membrane glycoprotein (Mol). J. Clin. Invest. 72, 171-179 (1983).
    • (1983) J. Clin. Invest. , vol.72 , pp. 171-179
    • Arnaout, M.A.1    Todd III, R.F.2    Dana, N.3    Melamed, J.4    Schlossman, S.F.5    Colten, H.R.6
  • 31
    • 34147153422 scopus 로고    scopus 로고
    • The β-tail domain (βTD) regulates physiologic ligand binding to integrin CD11b/CD18
    • V. Gupta, A. Gylling, J. L. Alonso, T. Sugimori, P. Ianakiev, J. P. Xiong, M. A. Arnaout, The β-tail domain (βTD) regulates physiologic ligand binding to integrin CD11b/CD18. Blood 109, 3513-3520 (2007).
    • (2007) Blood , vol.109 , pp. 3513-3520
    • Gupta, V.1    Gylling, A.2    Alonso, J.L.3    Sugimori, T.4    Ianakiev, P.5    Xiong, J.P.6    Arnaout, M.A.7
  • 34
    • 0037168524 scopus 로고    scopus 로고
    • Stabilizing the integrin αM inserted domain in alternative conformations with a range of engineered disulfide bonds
    • M. Shimaoka, C. Lu, A. Salas, T. Xiao, J. Takagi, T. A. Springer, Stabilizing the integrin αM inserted domain in alternative conformations with a range of engineered disulfide bonds. Proc. Natl. Acad. Sci. U.S.A. 99, 16737-16741 (2002).
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 16737-16741
    • Shimaoka, M.1    Lu, C.2    Salas, A.3    Xiao, T.4    Takagi, J.5    Springer, T.A.6
  • 36
    • 0034624058 scopus 로고    scopus 로고
    • An isoleucine-based allosteric switch controls affinity and shape shifting in integrin CD11b A-domain
    • J. P. Xiong, R. Li, M. Essafi, T. Stehle, M. A. Arnaout, An isoleucine-based allosteric switch controls affinity and shape shifting in integrin CD11b A-domain. J. Biol. Chem. 275, 38762-38767 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 38762-38767
    • Xiong, J.P.1    Li, R.2    Essafi, M.3    Stehle, T.4    Arnaout, M.A.5
  • 37
    • 0029646107 scopus 로고
    • Two conformations of the integrin A-domain (I-domain): A pathway for activation?
    • J. O. Lee, L. A. Bankston, M. A. Arnaout, R. C. Liddington, Two conformations of the integrin A-domain (I-domain): A pathway for activation? Structure 3, 1333-1340 (1995).
    • (1995) Structure , vol.3 , pp. 1333-1340
    • Lee, J.O.1    Bankston, L.A.2    Arnaout, M.A.3    Liddington, R.C.4
  • 38
    • 0028986196 scopus 로고
    • Crystal structure of the A domain from the α subunit of integrin CR3 (CD11b/CD18)
    • J. O. Lee, P. Rieu, M. A. Arnaout, R. Liddington, Crystal structure of the A domain from the α subunit of integrin CR3 (CD11b/CD18). Cell 80, 631-638 (1995).
    • (1995) Cell , vol.80 , pp. 631-638
    • Lee, J.O.1    Rieu, P.2    Arnaout, M.A.3    Liddington, R.4
  • 39
    • 0036721793 scopus 로고    scopus 로고
    • Requirement for RhoA kinase activation in leukocyte de-adhesion
    • L. Liu, B. R. Schwartz, N. Lin, R. K. Winn, J. M. Harlan, Requirement for RhoA kinase activation in leukocyte de-adhesion. J. Immunol. 169, 2330-2336 (2002).
    • (2002) J. Immunol. , vol.169 , pp. 2330-2336
    • Liu, L.1    Schwartz, B.R.2    Lin, N.3    Winn, R.K.4    Harlan, J.M.5
  • 40
    • 0029820264 scopus 로고    scopus 로고
    • Modulation of cell migration by integrin-mediated cytoskeletal linkages and ligand-binding affinity
    • A. Huttenlocher, M. H. Ginsberg, A. F. Horwitz, Modulation of cell migration by integrin-mediated cytoskeletal linkages and ligand-binding affinity. J. Cell Biol. 134, 1551-1562 (1996).
    • (1996) J. Cell Biol. , vol.134 , pp. 1551-1562
    • Huttenlocher, A.1    Ginsberg, M.H.2    Horwitz, A.F.3
  • 41
    • 0031034352 scopus 로고    scopus 로고
    • Integrin-ligand binding properties govern cell migration speed through cell-substratum adhesiveness
    • S. P. Palecek, J. C. Loftus, M. H. Ginsberg, D. A. Lauffenburger, A. F. Horwitz, Integrin-ligand binding properties govern cell migration speed through cell-substratum adhesiveness. Nature 385, 537-540 (1997).
    • (1997) Nature , vol.385 , pp. 537-540
    • Palecek, S.P.1    Loftus, J.C.2    Ginsberg, M.H.3    Lauffenburger, D.A.4    Horwitz, A.F.5
  • 42
    • 0024242694 scopus 로고
    • Orientation chamber in chemotaxis
    • S. H. Zigmond, Orientation chamber in chemotaxis. Methods Enzymol. 162, 65-72 (1988).
    • (1988) Methods Enzymol. , vol.162 , pp. 65-72
    • Zigmond, S.H.1
  • 44
    • 33748744871 scopus 로고    scopus 로고
    • Cost-effectiveness of coronary artery bypass grafts versus percutaneous coronary intervention for revascularization of high-risk patients
    • Investigators of Veterans Affairs Cooperative Studies Program #385 (AWESOME: Angina With Extremely Serious Operative Mortality Evaluation)
    • K. T. Stroupe, D. A. Morrison, M. A. Hlatky, P. G. Barnett, L. Cao, C. Lyttle, D. M. Hynes, W. G. Henderson; Investigators of Veterans Affairs Cooperative Studies Program #385 (AWESOME: Angina With Extremely Serious Operative Mortality Evaluation), Cost-effectiveness of coronary artery bypass grafts versus percutaneous coronary intervention for revascularization of high-risk patients. Circulation 114, 1251-1257 (2006).
    • (2006) Circulation , vol.114 , pp. 1251-1257
    • Stroupe, K.T.1    Morrison, D.A.2    Hlatky, M.A.3    Barnett, P.G.4    Cao, L.5    Lyttle, C.6    Hynes, D.M.7    Henderson, W.G.8
  • 45
    • 27744503901 scopus 로고    scopus 로고
    • Leukocyte engagement of platelet glycoprotein Ibα via the integrin Mac-1 is critical for the biological response to vascular injury
    • Y. Wang, M. Sakuma, Z. Chen, V. Ustinov, C. Shi, K. Croce, A. C. Zago, J. Lopez, P. Andre, E. Plow, D. I. Simon, Leukocyte engagement of platelet glycoprotein Ibα via the integrin Mac-1 is critical for the biological response to vascular injury. Circulation 112, 2993-3000 (2005).
    • (2005) Circulation , vol.112 , pp. 2993-3000
    • Wang, Y.1    Sakuma, M.2    Chen, Z.3    Ustinov, V.4    Shi, C.5    Croce, K.6    Zago, A.C.7    Lopez, J.8    Andre, P.9    Plow, E.10    Simon, D.I.11
  • 48
    • 0018758819 scopus 로고
    • Mac-1: A macrophage differentiation antigen identified by monoclonal antibody
    • T. Springer, G. Galfré, D. S. Secher, C. Milstein, Mac-1: A macrophage differentiation antigen identified by monoclonal antibody. Eur. J. Immunol. 9, 301-306 (1979).
    • (1979) Eur. J. Immunol. , vol.9 , pp. 301-306
    • Springer, T.1    Galfré, G.2    Secher, D.S.3    Milstein, C.4
  • 49
    • 0030784483 scopus 로고    scopus 로고
    • A role for Mac-1 (CDIIb/CD18) in immune complex-stimulated neutrophil function in vivo: Mac-1 deficiency abrogates sustained Fcg receptor-dependent neutrophil adhesion and complement-dependent proteinuria in acute glomerulonephritis
    • T. Tang, A. Rosenkranz, K. J. Assmann, M. J. Goodman, J. C. Gutierrez-Ramos, M. C. Carroll, R. S. Cotran, T. N. Mayadas, A role for Mac-1 (CDIIb/CD18) in immune complex-stimulated neutrophil function in vivo: Mac-1 deficiency abrogates sustained Fcg receptor-dependent neutrophil adhesion and complement-dependent proteinuria in acute glomerulonephritis. J. Exp. Med. 186, 1853-1863 (1997).
    • (1997) J. Exp. Med. , vol.186 , pp. 1853-1863
    • Tang, T.1    Rosenkranz, A.2    Assmann, K.J.3    Goodman, M.J.4    Gutierrez-Ramos, J.C.5    Carroll, M.C.6    Cotran, R.S.7    Mayadas, T.N.8
  • 52
    • 0345447594 scopus 로고    scopus 로고
    • Mac-1, but not LFA-1, uses intercellular adhesion molecule-1 to mediate slow leukocyte rolling in TNF-α-induced inflammation
    • J. L. Dunne, R. G. Collins, A. L. Beaudet, C. M. Ballantyne, K. Ley, Mac-1, but not LFA-1, uses intercellular adhesion molecule-1 to mediate slow leukocyte rolling in TNF-α-induced inflammation. J. Immunol. 171, 6105-6111 (2003).
    • (2003) J. Immunol. , vol.171 , pp. 6105-6111
    • Dunne, J.L.1    Collins, R.G.2    Beaudet, A.L.3    Ballantyne, C.M.4    Ley, K.5
  • 53
    • 14644391560 scopus 로고    scopus 로고
    • Targeting leukocyte integrins in human diseases
    • K. Yonekawa, J. M. Harlan, Targeting leukocyte integrins in human diseases. J. Leukoc. Biol. 77, 129-140 (2005).
    • (2005) J. Leukoc. Biol. , vol.77 , pp. 129-140
    • Yonekawa, K.1    Harlan, J.M.2
  • 54
    • 77957363101 scopus 로고    scopus 로고
    • Integrins as therapeutic targets: Lessons and opportunities
    • D. Cox, M. Brennan, N. Moran, Integrins as therapeutic targets: Lessons and opportunities. Nat. Rev. Drug Discov. 9, 804-820 (2010).
    • (2010) Nat. Rev. Drug Discov. , vol.9 , pp. 804-820
    • Cox, D.1    Brennan, M.2    Moran, N.3
  • 55
    • 76349084909 scopus 로고    scopus 로고
    • PML problems loom for Rituxan
    • M. Allison, PML problems loom for Rituxan. Nat. Biotechnol. 28, 105-106 (2010).
    • (2010) Nat. Biotechnol. , vol.28 , pp. 105-106
    • Allison, M.1
  • 59
    • 0024814732 scopus 로고
    • 2+ binding epitope on leukocyte integrin α subunits
    • 2+ binding epitope on leukocyte integrin α subunits. EMBO J. 8, 3759-3765 (1989).
    • (1989) EMBO J. , vol.8 , pp. 3759-3765
    • Dransfield, I.1    Hogg, N.2
  • 60
    • 0034662159 scopus 로고    scopus 로고
    • Insertion of enhanced green fluorescent protein into the lysozyme gene creates mice with green fluorescent granulocytes and macrophages
    • N. Faust, F. Varas, L. M. Kelly, S. Heck, T. Graf, Insertion of enhanced green fluorescent protein into the lysozyme gene creates mice with green fluorescent granulocytes and macrophages. Blood 96, 719-726 (2000).
    • (2000) Blood , vol.96 , pp. 719-726
    • Faust, N.1    Varas, F.2    Kelly, L.M.3    Heck, S.4    Graf, T.5
  • 61
    • 80052588781 scopus 로고    scopus 로고
    • HTS identification of compounds that enhance the binding of CD11b/CD18 to fibrinogen via a luminescence assay
    • V. Gupta, HTS identification of compounds that enhance the binding of CD11b/CD18 to fibrinogen via a luminescence assay. PubChem BioAssay AID 1499 (2009).
    • (2009) PubChem BioAssay AID , pp. 1499
    • Gupta, V.1
  • 64
    • 33845511326 scopus 로고    scopus 로고
    • Rho GTPase CDC42 regulates directionality and random movement via distinct MAPK pathways in neutrophils
    • K. Szczur, H. Xu, S. Atkinson, Y. Zheng, M. D. Filippi, Rho GTPase CDC42 regulates directionality and random movement via distinct MAPK pathways in neutrophils. Blood 108, 4205-4213 (2006).
    • (2006) Blood , vol.108 , pp. 4205-4213
    • Szczur, K.1    Xu, H.2    Atkinson, S.3    Zheng, Y.4    Filippi, M.D.5
  • 65
    • 2142847315 scopus 로고    scopus 로고
    • Reconstructing leukocyte migration in 3D extracellular matrix by time-lapse videomicroscopy and computer-assisted tracking
    • P. Friedl, E. B. Bröcker, Reconstructing leukocyte migration in 3D extracellular matrix by time-lapse videomicroscopy and computer-assisted tracking. Methods Mol. Biol. 239, 77-90 (2004).
    • (2004) Methods Mol. Biol. , vol.239 , pp. 77-90
    • Friedl, P.1    Bröcker, E.B.2
  • 66
    • 24944526542 scopus 로고    scopus 로고
    • Synergistic neovascularization by mixed transplantation of early endothelial progenitor cells and late outgrowth endothelial cells: The role of angiogenic cytokines and matrix metalloproteinases
    • C. H. Yoon, J. Hur, K. W. Park, J. H. Kim, C. S. Lee, I. Y. Oh, T. Y. Kim, H. J. Cho, H. J. Kang, I. H. Chae, H. K. Yang, B. H. Oh, Y. B. Park, H. S. Kim, Synergistic neovascularization by mixed transplantation of early endothelial progenitor cells and late outgrowth endothelial cells: The role of angiogenic cytokines and matrix metalloproteinases. Circulation 112, 1618-1627 (2005).
    • (2005) Circulation , vol.112 , pp. 1618-1627
    • Yoon, C.H.1    Hur, J.2    Park, K.W.3    Kim, J.H.4    Lee, C.S.5    Oh, I.Y.6    Kim, T.Y.7    Cho, H.J.8    Kang, H.J.9    Chae, I.H.10    Yang, H.K.11    Oh, B.H.12    Park, Y.B.13    Kim, H.S.14
  • 68
    • 0032610425 scopus 로고    scopus 로고
    • Functional analysis of the β2 integrins
    • R. Li, M. A. Arnaout, Functional analysis of the β2 integrins. Methods Mol. Biol. 129, 105-124 (1999).
    • (1999) Methods Mol. Biol. , vol.129 , pp. 105-124
    • Li, R.1    Arnaout, M.A.2
  • 69
    • 0035341132 scopus 로고    scopus 로고
    • 2 subunit reveals regions that become exposed upon receptor activation
    • 2 subunit reveals regions that become exposed upon receptor activation. J. Immunol. 166, 5629-5637 (2001).
    • (2001) J. Immunol. , vol.166 , pp. 5629-5637
    • Lu, C.1    Ferzly, M.2    Takagi, J.3    Springer, T.A.4
  • 70
    • 0042739086 scopus 로고    scopus 로고
    • New insights into the structural basis of integrin activation
    • J. P. Xiong, T. Stehle, S. L. Goodman, M. A. Arnaout, New insights into the structural basis of integrin activation. Blood 102, 1155-1159 (2003).
    • (2003) Blood , vol.102 , pp. 1155-1159
    • Xiong, J.P.1    Stehle, T.2    Goodman, S.L.3    Arnaout, M.A.4
  • 72
    • 0024411402 scopus 로고
    • Cooperative interactions of LFA-1 and Mac-1 with intercellular adhesion molecule-1 in facilitating adherence and transendothelial migration of human neutrophils in vitro
    • C. W. Smith, S. D. Marlin, R. Rothlein, C. Toman, D. C. Anderson, Cooperative interactions of LFA-1 and Mac-1 with intercellular adhesion molecule-1 in facilitating adherence and transendothelial migration of human neutrophils in vitro. J. Clin. Invest. 83, 2008-2017 (1989).
    • (1989) J. Clin. Invest. , vol.83 , pp. 2008-2017
    • Smith, C.W.1    Marlin, S.D.2    Rothlein, R.3    Toman, C.4    Anderson, D.C.5
  • 73
    • 0025025904 scopus 로고
    • Granulocyte-macrophage colony-stimulating factor and other cytokines regulate surface expression of the leukocyte adhesion molecule-1 on human neutrophils, monocytes, and their precursors
    • J. D. Griffin, O. Spertini, T. J. Ernst, M. P. Belvin, H. B. Levine, Y. Kanakura, T. F. Tedder, Granulocyte-macrophage colony-stimulating factor and other cytokines regulate surface expression of the leukocyte adhesion molecule-1 on human neutrophils, monocytes, and their precursors. J. Immunol. 145, 576-584 (1990).
    • (1990) J. Immunol. , vol.145 , pp. 576-584
    • Griffin, J.D.1    Spertini, O.2    Ernst, T.J.3    Belvin, M.P.4    Levine, H.B.5    Kanakura, Y.6    Tedder, T.F.7
  • 76
    • 77952389941 scopus 로고    scopus 로고
    • Inhibition of Mac-1 (CD11b/CD18) enhances tumor response to radiation by reducing myeloid cell recruitment
    • G. O. Ahn, D. Tseng, C. H. Liao, M. J. Dorie, A. Czechowicz, J. M. Brown, Inhibition of Mac-1 (CD11b/CD18) enhances tumor response to radiation by reducing myeloid cell recruitment. Proc. Natl. Acad. Sci. U.S.A. 107, 8363-8368 (2010).
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 8363-8368
    • Ahn, G.O.1    Tseng, D.2    Liao, C.H.3    Dorie, M.J.4    Czechowicz, A.5    Brown, J.M.6
  • 80
    • 12144273121 scopus 로고    scopus 로고
    • In vivo drug discovery in the zebrafish
    • L. I. Zon, R. T. Peterson, In vivo drug discovery in the zebrafish. Nat. Rev. Drug Discov. 4, 35-44 (2005).
    • (2005) Nat. Rev. Drug Discov. , vol.4 , pp. 35-44
    • Zon, L.I.1    Peterson, R.T.2
  • 83
    • 80052566429 scopus 로고    scopus 로고
    • note
    • Acknowledgments: We thank H. Tannoury, J. Y. Park, and J. Rosa for their generous help and discussions with the cell-based assays; T. D. Y. Chung, S. Vasile, E. Sergienko, and the staff of Conrad Prebys Center for Chemical Genomics at the Burnham Institute for Medical Research; and C. Shamu and the staff of the Institute for Chemistry and Chemical Biology at Harvard Medical School for their generous support in the implementation of the HTS assay. We thank S. Shankland and J. Pippin for the gift of sheep antibody against rabbit GBM. We thank M. A. Arnaout, P. Mundel, and D. Stoub for helpful discussions. We also thank Y. Wei and D. Mateu for help with the rat balloon injury model and immunostaining procedures. Funding: This work was supported in part by K01-HL096413 (to R.I.V.-P.) and with resources from the Miller School of Medicine, the Katz Family Fund, and the Center for Computational Science at the University of Miami. Author contributions: D.M. and M.H.F. contributed equally to this work and performed most of the experiments in this study, with technical assistance from C.J.B. and M.D. C.W. performed the anti-GBM nephritis experiment; Y.K. performed the intravital microscopy experiment; K.M.B. and G.L. performed the zebrafish experiments; D.H., A.N., and P.R. conducted the histological analyses; R.I.V.-P. conducted the balloon injury experiment; L.F.M., S.S., D.T., R.I.V.-P., K.L., J.R., and V.G. designed the experiments; L.F.M., D.T., K.L., and J.R. provided input in the preparation of the manuscript; and D.M., M.H.F., J.R., and V.G. co-wrote the paper. Competing interests: V.G. is an inventor of pending patents related to the study, and V.G. and the University of Miami have the potential for financial benefit from their future commercialization. The pending patents have been licensed to Adhaere Pharmaceuticals Inc., a company cofounded by V.G. The authors have no additional financial interests.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.