메뉴 건너뛰기




Volumn 9, Issue 2, 1997, Pages 219-226

Amino acid residues required for binding of vascular cell adhesion molecule-1 to integrin α4β7

Author keywords

4 7 integrin; Cation titration profiles; Peptide inhibition; Recognition sites; Structure function analysis; VCAM 1; VCAM 1 mutagenesis

Indexed keywords

INTEGRIN; VASCULAR CELL ADHESION MOLECULE 1;

EID: 0031050357     PISSN: 09538178     EISSN: None     Source Type: Journal    
DOI: 10.1093/intimm/9.2.219     Document Type: Article
Times cited : (6)

References (30)
  • 1
    • 0027768713 scopus 로고
    • The α4β1/VCAM-1 adhesion pathway in physiology and disease
    • Postigo, A. A., Teixido, J. and Sanchez Madrid, F 1993. The α4β1/VCAM-1 adhesion pathway in physiology and disease. Res. Immunol. 144:723
    • (1993) Res. Immunol. , vol.144 , pp. 723
    • Postigo, A.A.1    Teixido, J.2    Sanchez Madrid, F.3
  • 2
    • 0028173015 scopus 로고
    • The pathophysiologic role of α4 integrins in vivo
    • Lobb, R. R. and Hemler, M. E. 1994. The pathophysiologic role of α4 integrins in vivo. J. Clin. Invest. 94:1722
    • (1994) J. Clin. Invest. , vol.94 , pp. 1722
    • Lobb, R.R.1    Hemler, M.E.2
  • 5
    • 0025195762 scopus 로고
    • Structure of the integrin VLA-4 and its cell-cell and cell-matrix adhesion functions
    • Hemler, M. E., Elices, M. J., Parker, C. and Takada, Y. 1990. Structure of the integrin VLA-4 and its cell-cell and cell-matrix adhesion functions, Immunol. Rev. 114:45
    • (1990) Immunol. Rev. , vol.114 , pp. 45
    • Hemler, M.E.1    Elices, M.J.2    Parker, C.3    Takada, Y.4
  • 6
    • 0026574125 scopus 로고
    • Role of integrin α4β7/α4βp in lymphocyte adherence to fibronectin and VCAM-1 and in homotypic cell clustering
    • Ruegg, C., Postigo, A. A., Sikorski, E. E., Butcher, E. C., Pytela, R. and Erle, D. J. 1992. Role of integrin α4β7/α4βp in lymphocyte adherence to fibronectin and VCAM-1 and in homotypic cell clustering. J. Cell Biol. 117:179
    • (1992) J. Cell Biol. , vol.117 , pp. 179
    • Ruegg, C.1    Postigo, A.A.2    Sikorski, E.E.3    Butcher, E.C.4    Pytela, R.5    Erle, D.J.6
  • 7
  • 8
    • 0025161990 scopus 로고
    • VCAM-1 on activated endothelium interacts with the leukocyte integrin VLA-4 at a site distinct from the VLA-4/fibronectin binding site
    • Elices, M. J., Osborn, L., Takada, Y.,Crouse, C., Luhowskyj, S., Hemler, M. E. and Lobb, R. R. 1990. VCAM-1 on activated endothelium interacts with the leukocyte integrin VLA-4 at a site distinct from the VLA-4/fibronectin binding site. Cell 60:577
    • (1990) Cell , vol.60 , pp. 577
    • Elices, M.J.1    Osborn, L.2    Takada, Y.3    Crouse, C.4    Luhowskyj, S.5    Hemler, M.E.6    Lobb, R.R.7
  • 9
    • 0026642672 scopus 로고
    • Activated endothelium binds lymphocytes through a novel binding site in the alternately spliced domain of vascular cell adhesion molecule-1
    • Osborn, L., Vassallo, C. and Benjamin, C. D. 1992. Activated endothelium binds lymphocytes through a novel binding site in the alternately spliced domain of vascular cell adhesion molecule-1. J. Exp. Med. 176:99
    • (1992) J. Exp. Med. , vol.176 , pp. 99
    • Osborn, L.1    Vassallo, C.2    Benjamin, C.D.3
  • 10
    • 0026504051 scopus 로고
    • Lymphocyte adhesion through very late antigen 4: Evidence for a novel binding site in the alternatively spliced domain of vascular cell adhesion molecule 1 and an additional α4 integrin counter-receptor on stimulated endothelium
    • Vonderheide, R. H. and Springer, T. A. 1992. Lymphocyte adhesion through very late antigen 4: evidence for a novel binding site in the alternatively spliced domain of vascular cell adhesion molecule 1 and an additional α4 integrin counter-receptor on stimulated endothelium. J. Exp. Med. 175:1433
    • (1992) J. Exp. Med. , vol.175 , pp. 1433
    • Vonderheide, R.H.1    Springer, T.A.2
  • 11
    • 0028988299 scopus 로고
    • Differential regulation of α4 integrin-dependent binding to domains 1 and 4 of vascular cell adhesion molecule-1
    • Kilger, G., Needham, L. A., Nielsen, P. J., Clements, J., Vestweber, D. and Holzmann, B. 1995. Differential regulation of α4 integrin-dependent binding to domains 1 and 4 of vascular cell adhesion molecule-1. J. Biol. Chem. 270:5979
    • (1995) J. Biol. Chem. , vol.270 , pp. 5979
    • Kilger, G.1    Needham, L.A.2    Nielsen, P.J.3    Clements, J.4    Vestweber, D.5    Holzmann, B.6
  • 13
    • 0026644782 scopus 로고
    • Adhesion to vascular cell adhesion molecule 1 and fibronectin. Comparison of α4β1 (VLA-4) and α4β7 on the human B cell line JY
    • Chan, B. M., Elices, M. J., Murphy, E. and Hemler, M. E. 1992. Adhesion to vascular cell adhesion molecule 1 and fibronectin. Comparison of α4β1 (VLA-4) and α4β7 on the human B cell line JY. J. Biol. Chem. 267:8366
    • (1992) J. Biol. Chem. , vol.267 , pp. 8366
    • Chan, B.M.1    Elices, M.J.2    Murphy, E.3    Hemler, M.E.4
  • 14
    • 0027216613 scopus 로고
    • α4β7 integrin mediates B cell binding to fibronectin and vascular cell adhesion molecule-1. Expression and function of α4 integrins on human B lymphocytes
    • Postigo, A. A., Sanchez Mateos, P., Lazarovits, A. I., Sanchez Madrid, F. and de Landazuri, M. O. 1993. α4β7 integrin mediates B cell binding to fibronectin and vascular cell adhesion molecule-1. Expression and function of α4 integrins on human B lymphocytes. J. Immunol. 151:2471
    • (1993) J. Immunol. , vol.151 , pp. 2471
    • Postigo, A.A.1    Sanchez Mateos, P.2    Lazarovits, A.I.3    Sanchez Madrid, F.4    De Landazuri, M.O.5
  • 16
    • 0027957165 scopus 로고
    • Arrangement of domains, and amino acid residues required for binding of vascular cell adhesion molecule-1 to its counter-receptor VLA-4 (α4β1)
    • Osborn, L., Vassallo, C., Browning, B. G., Tizard, R., Haskard, D. O., Benjamin, C. D., Dougas, I. and Kirchhausen, T. 1994. Arrangement of domains, and amino acid residues required for binding of vascular cell adhesion molecule-1 to its counter-receptor VLA-4 (α4β1). J. Cell Biol. 124:601
    • (1994) J. Cell Biol. , vol.124 , pp. 601
    • Osborn, L.1    Vassallo, C.2    Browning, B.G.3    Tizard, R.4    Haskard, D.O.5    Benjamin, C.D.6    Dougas, I.7    Kirchhausen, T.8
  • 17
    • 0028246595 scopus 로고
    • Structural requirements for adhesion of soluble recombinant murine vascular cell adhesion molecule-1 to α4β1
    • Renz, M. E., Chiu, H. H., Jones, S., Fox, J., Kim, K. J., Presta, L. G. and Fong, S. 1994. Structural requirements for adhesion of soluble recombinant murine vascular cell adhesion molecule-1 to α4β1. J. Cell Biol. 125:1395
    • (1994) J. Cell Biol. , vol.125 , pp. 1395
    • Renz, M.E.1    Chiu, H.H.2    Jones, S.3    Fox, J.4    Kim, K.J.5    Presta, L.G.6    Fong, S.7
  • 18
    • 0028208244 scopus 로고
    • Residues within a conserved amino acid motif of domains 1 and 4 of VCAM-1 are required for binding to VLA-4
    • Vonderheide, R. H., Tedder, T. F., Springer, T. A. and Staunton, D. E. 1994. Residues within a conserved amino acid motif of domains 1 and 4 of VCAM-1 are required for binding to VLA-4. J. Cell Biol. 125:215
    • (1994) J. Cell Biol. , vol.125 , pp. 215
    • Vonderheide, R.H.1    Tedder, T.F.2    Springer, T.A.3    Staunton, D.E.4
  • 20
    • 0028853677 scopus 로고
    • Similar but nonidentical amino acid residues on vascular cell adhesion molecule-1 are involved in the interaction with α4β1 and α4β7 under different activity states
    • Chiu, H. H., Crowe, D. T., Renz, M. E., Presta, L. G., Jones, S., Weissman, I. L. and Fong, S. 1995. Similar but nonidentical amino acid residues on vascular cell adhesion molecule-1 are involved in the interaction with α4β1 and α4β7 under different activity states. J. Immunol. 155:5257
    • (1995) J. Immunol. , vol.155 , pp. 5257
    • Chiu, H.H.1    Crowe, D.T.2    Renz, M.E.3    Presta, L.G.4    Jones, S.5    Weissman, I.L.6    Fong, S.7
  • 21
    • 0026655693 scopus 로고
    • Cloning and expression of mouse integrin βp(β7): A functional role in Peyer's patch-specific lymphocyte homing
    • Hu, M. C., Crowe, D. T., Weissman, I. L. and Holzmann, B. 1992. Cloning and expression of mouse integrin βp(β7): a functional role in Peyer's patch-specific lymphocyte homing. Proc. Natl Acad. Sci. USA 89:8254
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 8254
    • Hu, M.C.1    Crowe, D.T.2    Weissman, I.L.3    Holzmann, B.4
  • 22
    • 0027398570 scopus 로고
    • Multiple activation states of VLA-4. Mechanistic differences between adhesion to CS1/ fibronectin and to vascular cell adhesion molecule-1
    • Masumoto, A. and Hemler, M. E. 1993. Multiple activation states of VLA-4. Mechanistic differences between adhesion to CS1/ fibronectin and to vascular cell adhesion molecule-1. J. Biol. Chem. 268:228
    • (1993) J. Biol. Chem. , vol.268 , pp. 228
    • Masumoto, A.1    Hemler, M.E.2
  • 23
    • 0029315817 scopus 로고
    • Do integrins use a 'MIDAS touch' to grasp an Asp?
    • Bergelson, J. M. and Hemler, M. E. 1995. Do integrins use a 'MIDAS touch' to grasp an Asp? Curr. Biol. 5:615
    • (1995) Curr. Biol. , vol.5 , pp. 615
    • Bergelson, J.M.1    Hemler, M.E.2
  • 24
    • 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
    • (1994) J Biol. Chem. , vol.269 , pp. 25235
    • Loftus, J.C.1    Smith, J.W.2    Ginsberg, M.H.3
  • 25
    • 0028986196 scopus 로고
    • Crystal structure of the A domain from the alpha 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 alpha subunit of integrin CR3 (CD11b/CD18). Cell 80:631
    • (1995) Cell , vol.80 , pp. 631
    • Lee, J.O.1    Rieu, P.2    Arnaout, M.A.3    Liddington, R.4
  • 26
    • 0028077510 scopus 로고
    • Ligand and cation binding are dual functions of a discrete segment of the integrin β3 subunit: Cation displacement is involved in ligand binding
    • D'Souza, S. E., Haas, T. A., Piotrowicz, R. S., Byers Ward, V., McGrath, D. E., Soule, H. R., Cierniewski, C., Plow, E. F. and Smith, J. W. 1994. Ligand and cation binding are dual functions of a discrete segment of the integrin β3 subunit: cation displacement is involved in ligand binding. Cell 79:659
    • (1994) Cell , vol.79 , pp. 659
    • D'Souza, S.E.1    Haas, T.A.2    Piotrowicz, R.S.3    Byers Ward, V.4    McGrath, D.E.5    Soule, H.R.6    Cierniewski, C.7    Plow, E.F.8    Smith, J.W.9
  • 27
    • 0026496886 scopus 로고
    • The three-dimensional structure of the tenth type III module of fibronectin: An insight into RGD-mediated interactions
    • Main, A. L., Harvey, T. S., Baron, M., Boyd, J. and Campbell, I. D. 1992. The three-dimensional structure of the tenth type III module of fibronectin: an insight into RGD-mediated interactions. Cell 71:671
    • (1992) Cell , vol.71 , pp. 671
    • Main, A.L.1    Harvey, T.S.2    Baron, M.3    Boyd, J.4    Campbell, I.D.5
  • 29
    • 0029046132 scopus 로고
    • The crystal structure of an N-terminal two-domain fragment of vascular cell adhesion molecule 1 (VCAM-1): A cyclic peptide based on the domain 1 C-D loop can inhibit VCAM-1-α4 integrin interaction
    • Wang, J., Pepinsky, R. B., Stehle, T., Liu, J., Karpusas, M., Browning, B. and Osborn, L. 1995. The crystal structure of an N-terminal two-domain fragment of vascular cell adhesion molecule 1 (VCAM-1): A cyclic peptide based on the domain 1 C-D loop can inhibit VCAM-1-α4 integrin interaction. Proc. Natl Acad. Sci. USA 92:5714
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 5714
    • Wang, J.1    Pepinsky, R.B.2    Stehle, T.3    Liu, J.4    Karpusas, M.5    Browning, B.6    Osborn, L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.