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Volumn 121, Issue 5, 1997, Pages 914-921

Structural interlock between ligand-binding site and stalk-like region of β1 integrin revealed by a monoclonal antibody recognizing conformation-dependent epitope

Author keywords

Cell adhesion; Inside out signaling; Integrin; Ligand binding; Monoclonal antibody

Indexed keywords

CHIMERIC PROTEIN; EPITOPE; INTEGRIN; MANGANESE; MONOCLONAL ANTIBODY;

EID: 0030913268     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021673     Document Type: Article
Times cited : (32)

References (42)
  • 2
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes, R.O. (1992) Integrins: versatility, modulation, and signaling in cell adhesion. Cell 69, 11-25
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 3
    • 0025218924 scopus 로고
    • VLA proteins in the integrin family: Structures, functions, and their role on leukocytes
    • Hemler, M.E. (1990) VLA proteins in the integrin family: structures, functions, and their role on leukocytes. Annu. Rev. Immunol. 8, 365-400
    • (1990) Annu. Rev. Immunol. , vol.8 , pp. 365-400
    • Hemler, M.E.1
  • 5
    • 0026527577 scopus 로고
    • Integrin modulating factor-1: A lipid that alters the function of leukocyte integrins
    • Hermanowski-Vosatka, A., Van-Strijp, J.A., Swiggard, W.J., and Wright, S.D. (1992) Integrin modulating factor-1: a lipid that alters the function of leukocyte integrins. Cell 68, 341-352
    • (1992) Cell , vol.68 , pp. 341-352
    • Hermanowski-Vosatka, A.1    Van-Strijp, J.A.2    Swiggard, W.J.3    Wright, S.D.4
  • 6
    • 0025976515 scopus 로고
    • β1 integrin-mediated lymphocyte adherence to extracellular matrix is enhanced by phorbol ester treatment
    • Wilkins, J.A., Stupack, D., Stewart, S., and Caixia, S. (1991) β1 integrin-mediated lymphocyte adherence to extracellular matrix is enhanced by phorbol ester treatment. Eur. J. Immunol. 21, 517-522
    • (1991) Eur. J. Immunol. , vol.21 , pp. 517-522
    • Wilkins, J.A.1    Stupack, D.2    Stewart, S.3    Caixia, S.4
  • 7
    • 0027395041 scopus 로고
    • Affinity modulation of integrin α5β1: Regulation of the functional response by soluble fibronectin
    • Faull, R.J., Kovach, N.L., Harlan, J.M., and Ginsberg, M.H. (1993) Affinity modulation of integrin α5β1: regulation of the functional response by soluble fibronectin. J. Cell Biol. 121, 155-162
    • (1993) J. Cell Biol. , vol.121 , pp. 155-162
    • Faull, R.J.1    Kovach, N.L.2    Harlan, J.M.3    Ginsberg, M.H.4
  • 8
    • 0027243763 scopus 로고
    • A high affinity conformational state on VLA integrin heterodimers induced by an anti-β1 chain monoclonal antibody
    • Arroyo, A.G., Garcia-Pardo, A., and Sanchez-Madrid, F. (1993) A high affinity conformational state on VLA integrin heterodimers induced by an anti-β1 chain monoclonal antibody. J. Biol. Chem. 268, 9863-9868
    • (1993) J. Biol. Chem. , vol.268 , pp. 9863-9868
    • Arroyo, A.G.1    Garcia-Pardo, A.2    Sanchez-Madrid, F.3
  • 9
    • 0024109978 scopus 로고
    • Oligospecificity of the cellular adhesion receptor Mac-1 encompasses an inducible recognition specificity for fibrinogen
    • Altieli, D.C., Bader, R., Mannucci, P.M., and Edgington, T.S. (1988) Oligospecificity of the cellular adhesion receptor Mac-1 encompasses an inducible recognition specificity for fibrinogen. J. Cell Biol. 107, 1893-1900
    • (1988) J. Cell Biol. , vol.107 , pp. 1893-1900
    • Altieli, D.C.1    Bader, R.2    Mannucci, P.M.3    Edgington, T.S.4
  • 10
    • 0024443411 scopus 로고
    • T-cell receptor crosslinking transiently stimulates adhesiveness through LFA-1
    • Dustin, M.L. and Springer, T.A. (1989) T-cell receptor crosslinking transiently stimulates adhesiveness through LFA-1. Nature 341, 619-624
    • (1989) Nature , vol.341 , pp. 619-624
    • Dustin, M.L.1    Springer, T.A.2
  • 11
    • 0025363922 scopus 로고
    • Regulated expression and binding of three VLA (β1) integrin receptors on T cells
    • Shimizu, Y., Van-Seventer, G.A., Horgan, K.J., and Shaw, S. (1990) Regulated expression and binding of three VLA (β1) integrin receptors on T cells. Nature 345, 250-253
    • (1990) Nature , vol.345 , pp. 250-253
    • Shimizu, Y.1    Van-Seventer, G.A.2    Horgan, K.J.3    Shaw, S.4
  • 13
    • 0025781381 scopus 로고
    • Effect of platelet activation on the conformation of the plasma membrane glycoprotem IIb-IIIa complex
    • Sims, P.J., Ginsberg, M.H., Plow, E.F., and Shattil, S.J. (1991) Effect of platelet activation on the conformation of the plasma membrane glycoprotem IIb-IIIa complex. J. Biol. Chem. 266, 7345-7352
    • (1991) J. Biol. Chem. , vol.266 , pp. 7345-7352
    • Sims, P.J.1    Ginsberg, M.H.2    Plow, E.F.3    Shattil, S.J.4
  • 15
    • 0024208260 scopus 로고
    • Occupancy of an adhesive glycoprotein receptor modulates expression of an antigenic site involved in cell adhesion
    • Frelinger, A.L., Lam, S.C.-T., Plow, E.F., Smith, M.A., Loftus, J.C., and Ginsberg, M.H. (1988) Occupancy of an adhesive glycoprotein receptor modulates expression of an antigenic site involved in cell adhesion. J. Biol. Chem. 263, 12397-12402
    • (1988) J. Biol. Chem. , vol.263 , pp. 12397-12402
    • Frelinger, A.L.1    Lam, S.C.-T.2    Plow, E.F.3    Smith, M.A.4    Loftus, J.C.5    Ginsberg, M.H.6
  • 17
    • 0026063230 scopus 로고
    • Monoclonal antibodies to ligand-occupied conformers of integrin αIIbβ3 (glycoprotein IIb-IIIa) alter receptor affinity, specificity, and function
    • Frelinger, A.L., Du, X.P., Plow, E.F., and Ginsberg, M.H. (1991) Monoclonal antibodies to ligand-occupied conformers of integrin αIIbβ3 (glycoprotein IIb-IIIa) alter receptor affinity, specificity, and function. J. Biol. Chem. 266, 17106-17111
    • (1991) J. Biol. Chem. , vol.266 , pp. 17106-17111
    • Frelinger, A.L.1    Du, X.P.2    Plow, E.F.3    Ginsberg, M.H.4
  • 18
    • 0025241904 scopus 로고
    • Selective inhibition of integrin function by antibodies specific for ligand-occupied receptor conformers
    • Frelinger, A.L., Cohen, I., Plow, E.F., Smith, M.A., Roberts, J., Lam, S.C., and Ginsberg, M.H. (1990) Selective inhibition of integrin function by antibodies specific for ligand-occupied receptor conformers. J. Biol. Chem. 265, 6346-6352
    • (1990) J. Biol. Chem. , vol.265 , pp. 6346-6352
    • Frelinger, A.L.1    Cohen, I.2    Plow, E.F.3    Smith, M.A.4    Roberts, J.5    Lam, S.C.6    Ginsberg, M.H.7
  • 19
    • 0029039630 scopus 로고
    • Topography of ligand-induced binding sites, including a novel cation-sensitive epitope (AP5) at the amino terminus, of the human integrin β3 subunit
    • Honda, S., Tomiyama, Y., Pelletier, A.J., Annis, D., Honda, Y., Orchekowski, R., Ruggeri, Z., and Kunicki, T.J. (1995) Topography of ligand-induced binding sites, including a novel cation-sensitive epitope (AP5) at the amino terminus, of the human integrin β3 subunit. J. Biol. Chem. 270, 11947-11954
    • (1995) J. Biol. Chem. , vol.270 , pp. 11947-11954
    • Honda, S.1    Tomiyama, Y.2    Pelletier, A.J.3    Annis, D.4    Honda, Y.5    Orchekowski, R.6    Ruggeri, Z.7    Kunicki, T.J.8
  • 20
    • 0023784561 scopus 로고
    • Interaction of fibrinogen with its platelet receptor. Differential effects of alpha and gamma chain fibrinogen peptides on the glycoprotein IIb-IIIa complex
    • Bennet, J.S., Shattil, S.J., Plow, E.F., and Gartner, T.K. (1988) Interaction of fibrinogen with its platelet receptor. Differential effects of alpha and gamma chain fibrinogen peptides on the glycoprotein IIb-IIIa complex. J. Biol. Chem. 263, 12948-12953
    • (1988) J. Biol. Chem. , vol.263 , pp. 12948-12953
    • Bennet, J.S.1    Shattil, S.J.2    Plow, E.F.3    Gartner, T.K.4
  • 21
    • 0028858576 scopus 로고
    • Monoclonal antibody 9EG7 defines a novel β1 integrin epitope induced by soluble ligand and manganese, but inhibited by calcium
    • Bazzoni, G., Shih, D.T., Buck, C.A., and Hemler, M.E. (1995) Monoclonal antibody 9EG7 defines a novel β1 integrin epitope induced by soluble ligand and manganese, but inhibited by calcium. J. Biol. Chem. 270, 25570-25577
    • (1995) J. Biol. Chem. , vol.270 , pp. 25570-25577
    • Bazzoni, G.1    Shih, D.T.2    Buck, C.A.3    Hemler, M.E.4
  • 22
    • 0028973093 scopus 로고
    • α4β1 integrin-dependent cell adhesion is regulated by a low affinity receptor pool that is conformationally responsive to ligand
    • Yednock, T.A., Cannon, C., Vandevert, C., Goldbach, E.G., Shaw, G., Ellis, D.K., Liaw, C., Fritz, L.C., and Tanner, L.I. (1995) α4β1 integrin-dependent cell adhesion is regulated by a low affinity receptor pool that is conformationally responsive to ligand. J. Biol. Chem. 270, 28740-28750
    • (1995) J. Biol. Chem. , vol.270 , pp. 28740-28750
    • Yednock, T.A.1    Cannon, C.2    Vandevert, C.3    Goldbach, E.G.4    Shaw, G.5    Ellis, D.K.6    Liaw, C.7    Fritz, L.C.8    Tanner, L.I.9
  • 23
    • 0027255758 scopus 로고
    • Ligand intercellular adhesion molecule 1 has a necessary role in activation of integrin lymphocyte function-associated molecule 1
    • Cabanas, C. and Hogg, N. (1993) Ligand intercellular adhesion molecule 1 has a necessary role in activation of integrin lymphocyte function-associated molecule 1. Proc. Natl. Acad. Sci. USA 90, 5838-5842
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5838-5842
    • Cabanas, C.1    Hogg, N.2
  • 24
    • 0028900673 scopus 로고
    • Identification of putative ligand-binding sites of the integrin α4β1 (VLA-4, cd49d/CD29)
    • Kamata, T., Puzon, W., and Takada, Y. (1995) Identification of putative ligand-binding sites of the integrin α4β1 (VLA-4, cd49d/CD29). Biochem. J. 305, 945-951
    • (1995) Biochem. J. , vol.305 , pp. 945-951
    • Kamata, T.1    Puzon, W.2    Takada, Y.3
  • 25
    • 0026061621 scopus 로고
    • Monoclonal antibodies that inhibit binding of propolypeptide of von Willebrand factor to collagen. Localization of epitopes
    • Fujisawa, T., Takagi, J., Sekiya, F., Goto, A., Miake, F., and Saito, Y. (1991) Monoclonal antibodies that inhibit binding of propolypeptide of von Willebrand factor to collagen. Localization of epitopes. Eur. J. Biochem. 196, 673-677
    • (1991) Eur. J. Biochem. , vol.196 , pp. 673-677
    • Fujisawa, T.1    Takagi, J.2    Sekiya, F.3    Goto, A.4    Miake, F.5    Saito, Y.6
  • 26
    • 0024346099 scopus 로고
    • A collagen-binding glycoprotein from bovine platelets is identical to propolypeptide of von Willebrand factor
    • Takagi, J., Kasahara, K., Sekiya, F., Inada, Y., and Saito, Y. (1989) A collagen-binding glycoprotein from bovine platelets is identical to propolypeptide of von Willebrand factor. J. Biol. Chem. 264, 10425-10430
    • (1989) J. Biol. Chem. , vol.264 , pp. 10425-10430
    • Takagi, J.1    Kasahara, K.2    Sekiya, F.3    Inada, Y.4    Saito, Y.5
  • 27
    • 0027248518 scopus 로고
    • Identification of a regulatory region of integrin β1 subunit using activating and inhibiting antibodies
    • Takada, Y. and Puzon, W. (1993) Identification of a regulatory region of integrin β1 subunit using activating and inhibiting antibodies. J. Biol. Chem. 268, 17597-17601
    • (1993) J. Biol. Chem. , vol.268 , pp. 17597-17601
    • Takada, Y.1    Puzon, W.2
  • 28
    • 0028805249 scopus 로고
    • Critical amino acid residues for ligand binding are clustered in a predicted beta-turn of the third N-terminal repeat in the integrin α4 and α5 subunits
    • Irie, A., Kamata, T., Puzon-McLaughlin, W., and Takada, Y. (1995) Critical amino acid residues for ligand binding are clustered in a predicted beta-turn of the third N-terminal repeat in the integrin α4 and α5 subunits. EMBO J. 14, 5550-5556
    • (1995) EMBO J. , vol.14 , pp. 5550-5556
    • Irie, A.1    Kamata, T.2    Puzon-McLaughlin, W.3    Takada, Y.4
  • 29
    • 0028177372 scopus 로고
    • β1-integrin-mediated adhesion of melanoma cells to the propolypeptide of von Willebrand factor
    • Takagi, J., Sudo, Y., Saito, T., and Saito, Y. (1994) β1-integrin-mediated adhesion of melanoma cells to the propolypeptide of von Willebrand factor. Eur. J. Biochem. 222, 861-867
    • (1994) Eur. J. Biochem. , vol.222 , pp. 861-867
    • Takagi, J.1    Sudo, Y.2    Saito, T.3    Saito, Y.4
  • 30
    • 0023730954 scopus 로고
    • Regulation of the fibronectin receptor affinity by divalent cations
    • Gailit, J. and Ruoslahti, E. (1988) Regulation of the fibronectin receptor affinity by divalent cations. J. Biol. Chem. 263, 12927-12932
    • (1988) J. Biol. Chem. , vol.263 , pp. 12927-12932
    • Gailit, J.1    Ruoslahti, E.2
  • 31
    • 0026040206 scopus 로고
    • Characterization of regions of fibronectin besides the arginine-glycine-aspartic acid sequence required for adhesive function of the cell-binding domain using site-directed mutagenesis
    • Aota, S., Nagai, T., and Yamada, K.M. (1991) Characterization of regions of fibronectin besides the arginine-glycine-aspartic acid sequence required for adhesive function of the cell-binding domain using site-directed mutagenesis. J. Biol. Chem. 266, 15938-15943
    • (1991) J. Biol. Chem. , vol.266 , pp. 15938-15943
    • Aota, S.1    Nagai, T.2    Yamada, K.M.3
  • 32
    • 0027421094 scopus 로고
    • A monoclonal antibody against an activation epitope on mouse integrin chain β1 blocks adhesion of lymphocytes to the endothelial integrin α6β1
    • Lenter, M., Uhlig, H., Hamann, A., Jeno, P., Imhof, B., and Vestweber, D. (1993) A monoclonal antibody against an activation epitope on mouse integrin chain β1 blocks adhesion of lymphocytes to the endothelial integrin α6β1. Proc. Natl. Acad. Sci. USA 90, 9051-9055
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9051-9055
    • Lenter, M.1    Uhlig, H.2    Hamann, A.3    Jeno, P.4    Imhof, B.5    Vestweber, D.6
  • 33
    • 0029820903 scopus 로고    scopus 로고
    • A novel activating anti-β1 integrin monoclonal antibody binds to the cysteine-rich repeats in the β1 chain
    • Faull, R.J., Wang, J., Leavesley, D.I., Puzon, W., Russ, G.R., Vestweber, D., and Takada, Y. (1996) A novel activating anti-β1 integrin monoclonal antibody binds to the cysteine-rich repeats in the β1 chain. J. Biol. Chem. 271, 25099-25106
    • (1996) J. Biol. Chem. , vol.271 , pp. 25099-25106
    • Faull, R.J.1    Wang, J.2    Leavesley, D.I.3    Puzon, W.4    Russ, G.R.5    Vestweber, D.6    Takada, Y.7
  • 34
    • 0025912923 scopus 로고
    • Two-step model of leukocyte-endothelial cell interaction in imflammation: Distinct roles for LECAM-1 and leukocyte β2 integrins in vivo
    • Von-Andrian, U.H., Chambers, J.D., McEvoy, L.M., Bargatze, R.F., Arfors, K.E., and Butcher, E.C. (1991) Two-step model of leukocyte-endothelial cell interaction in imflammation: distinct roles for LECAM-1 and leukocyte β2 integrins in vivo. Proc. Natl. Acad. Sci. USA 88, 7538-7542
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7538-7542
    • Von-Andrian, U.H.1    Chambers, J.D.2    McEvoy, L.M.3    Bargatze, R.F.4    Arfors, K.E.5    Butcher, E.C.6
  • 35
    • 0024411402 scopus 로고
    • Cooperative interactions of LFA-1 and Mac-1 with intercellular adhesion molecule-1 in facilitating adherence and transendothelial migration of human neutrophiles in vitro
    • Smith, C.W., Marlin, S.D., Rothlein, R., Toman, C., and Anderson, D.C. (1989) Cooperative interactions of LFA-1 and Mac-1 with intercellular adhesion molecule-1 in facilitating adherence and transendothelial migration of human neutrophiles in vitro. J. Clin. Invest. 83, 2008-2012
    • (1989) J. Clin. Invest. , vol.83 , pp. 2008-2012
    • Smith, C.W.1    Marlin, S.D.2    Rothlein, R.3    Toman, C.4    Anderson, D.C.5
  • 36
    • 0028324995 scopus 로고
    • Ligand-induced adhesion to activated endothelium and to vascular cell adhesion molecule-1 in lymphocytes transfected with the N-formyl peptide receptor
    • Honda S., Campbell, J.J., Andrew, D.P., Engelhardt, B., Butcher, B.A., Warnock, R.A., Ye, R.D., and Butcher, E.C. (1994) Ligand-induced adhesion to activated endothelium and to vascular cell adhesion molecule-1 in lymphocytes transfected with the N-formyl peptide receptor. J. Immunol. 152, 4026-4035
    • (1994) J. Immunol. , vol.152 , pp. 4026-4035
    • Honda, S.1    Campbell, J.J.2    Andrew, D.P.3    Engelhardt, B.4    Butcher, B.A.5    Warnock, R.A.6    Ye, R.D.7    Butcher, E.C.8
  • 37
    • 0023915420 scopus 로고
    • The platelet membrane glycoprotein IIb-IIIa complex
    • Philips, D.R., Charo, I.F., Parise, L.V., and Fitzgerald, L.A. (1988) The platelet membrane glycoprotein IIb-IIIa complex. Blood 71, 831-843
    • (1988) Blood , vol.71 , pp. 831-843
    • Philips, D.R.1    Charo, I.F.2    Parise, L.V.3    Fitzgerald, L.A.4
  • 38
    • 0024531099 scopus 로고
    • Cellular adhesion: GPIIb-IIIa as a prototypic adhesion receptor
    • Plow, E.F. and Ginsberg, M.H. (1989) Cellular adhesion: GPIIb-IIIa as a prototypic adhesion receptor. Prog. Hemostasis Thromb. 9, 117-156
    • (1989) Prog. Hemostasis Thromb. , vol.9 , pp. 117-156
    • Plow, E.F.1    Ginsberg, M.H.2
  • 39
    • 0029953173 scopus 로고    scopus 로고
    • Regulation of conformation and ligand binding function of integrin α5β1 by the beta1 cytoplasmic domain
    • Puzon-McLaughlin, W., Yednock, T.A., and Takada, Y. (1996) Regulation of conformation and ligand binding function of integrin α5β1 by the beta1 cytoplasmic domain. J. Biol. Chem. 271, 16580-16585
    • (1996) J. Biol. Chem. , vol.271 , pp. 16580-16585
    • Puzon-McLaughlin, W.1    Yednock, T.A.2    Takada, Y.3
  • 40
    • 0028986196 scopus 로고
    • Crystal structure of the A domain from the α subunit of integrin CR3 (CD11b/CD18)
    • Lee, J.O., Rieu, P., Arnaout, M.A., and Liddington, R. (1995) Crystal structure of the A domain from the α subunit of integrin CR3 (CD11b/CD18). Cell 80, 631-638
    • (1995) Cell , vol.80 , pp. 631-638
    • Lee, J.O.1    Rieu, P.2    Arnaout, M.A.3    Liddington, R.4
  • 41
    • 0027972994 scopus 로고
    • Integrin-mediated cell adhesion: The extracellular face
    • Loftus, J.C., Smith, J.W., and Ginsberg, M.H. (1994) Integrin-mediated cell adhesion: the extracellular face. J. Biol. Chem. 269, 25235-25238
    • (1994) J. Biol. Chem. , vol.269 , pp. 25235-25238
    • Loftus, J.C.1    Smith, J.W.2    Ginsberg, M.H.3
  • 42
    • 0029786408 scopus 로고    scopus 로고
    • Critical residues for ligand binding in an I domain-like structure of the integrin β1 subunit
    • Puzon-McLaughlin, W. and Takada, Y. (1996) Critical residues for ligand binding in an I domain-like structure of the integrin β1 subunit. J. Biol. Chem. 271, 20438-20443
    • (1996) J. Biol. Chem. , vol.271 , pp. 20438-20443
    • Puzon-McLaughlin, W.1    Takada, Y.2


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