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Volumn 161, Issue 11, 1998, Pages 5978-5986

Sequence motifs in the integrin α4 cytoplasmic tail required for regulation of in vivo expansion of murine lymphoma cells

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; INTEGRIN; INTEGRIN RECEPTOR; INTERCELLULAR ADHESION MOLECULE 1; LIGAND; VASCULAR CELL ADHESION MOLECULE 1;

EID: 0032402245     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (8)

References (62)
  • 1
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark, E. A., and J. S. Brugge. 1995. Integrins and signal transduction pathways: the road taken. Science 268:233.
    • (1995) Science , vol.268 , pp. 233
    • Clark, E.A.1    Brugge, J.S.2
  • 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.
    • (1992) Cell , vol.69 , pp. 11
    • Hynes, R.O.1
  • 3
    • 0029932651 scopus 로고    scopus 로고
    • Integrins as promiscuous signal transduction devices
    • Petty, H. R., and R. F. Todd. 1996. Integrins as promiscuous signal transduction devices. Immunol. Today 17:209.
    • (1996) Immunol. Today , vol.17 , pp. 209
    • Petty, H.R.1    Todd, R.F.2
  • 4
    • 0025195762 scopus 로고
    • Structure of the integrin VLA-4 and its cell-cell and cell-matrix adhesion functions
    • Hemler, M. E., M. J. Elices, C. Parker, and Y. Takada. 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
  • 9
    • 0028982172 scopus 로고
    • 7 and LFA-1 in lymphocyte homing to Peyer's patch-HEV in situ: The multistep model confirmed and refined
    • 7 and LFA-1 in lymphocyte homing to Peyer's patch-HEV in situ: the multistep model confirmed and refined. Immunity 3:99.
    • (1995) Immunity , vol.3 , pp. 99
    • Bargatze, R.F.1    Jutila, M.A.2    Butcher, E.C.3
  • 11
    • 0029891725 scopus 로고    scopus 로고
    • 4-integrin supports leukocyte rolling and adhesion in chronically inflamed postcapillary venules in vivo
    • 4-integrin supports leukocyte rolling and adhesion in chronically inflamed postcapillary venules in vivo. J. Exp. Med. 183:1995.
    • (1996) J. Exp. Med. , vol.183 , pp. 1995
    • Johnston, B.1    Issekutz, T.B.2    Kubes, P.3
  • 12
    • 0028138618 scopus 로고
    • L-selectin and very late antigen-4 integrin promote eosinophil rolling at physiological shear rates in vivo
    • Sriramarao, P., U. H. von Andrian, E. C. Butcher, M. A. Bourdon, and D. H. Broide. 1994. L-selectin and very late antigen-4 integrin promote eosinophil rolling at physiological shear rates in vivo. J. Immunol. 153:4238.
    • (1994) J. Immunol. , vol.153 , pp. 4238
    • Sriramarao, P.1    Von Andrian, U.H.2    Butcher, E.C.3    Bourdon, M.A.4    Broide, D.H.5
  • 15
    • 0031454545 scopus 로고    scopus 로고
    • 7 integrins in hematopoiesis, lymphocyte trafficking, and organ development
    • 7 integrins in hematopoiesis, lymphocyte trafficking, and organ development. Curr. Top. Microbiol. Immunol. 231:23.
    • (1998) Curr. Top. Microbiol. Immunol. , vol.231 , pp. 23
    • Wagner, N.1    Müller, W.2
  • 19
    • 0028324995 scopus 로고
    • Ligand-induced adhesion to activate endothelium and to vascular cell adhesion molecule-1 in lymphocytes transfected with N-formyl peptide receptor
    • Honda, S., J. J. Campbell, D. P. Andrew, B. Engelhardt, B. A. Butcher, R. A. Warnk, R. D. Ye, and E. C. Butcher. 1994. Ligand-induced adhesion to activate endothelium and to vascular cell adhesion molecule-1 in lymphocytes transfected with N-formyl peptide receptor. J. Immunol. 152:4026.
    • (1994) J. Immunol. , vol.152 , pp. 4026
    • Honda, S.1    Campbell, J.J.2    Andrew, D.P.3    Engelhardt, B.4    Butcher, B.A.5    Warnk, R.A.6    Ye, R.D.7    Butcher, E.C.8
  • 20
    • 0030026692 scopus 로고    scopus 로고
    • Chemokines regulate T cell adherence to recombinant adhesion molecules and extracellular matrix proteins
    • Lloyd, A. R., J. J. Oppenheim, D. J. Kelvin, and D. D. Taub. 1996. Chemokines regulate T cell adherence to recombinant adhesion molecules and extracellular matrix proteins. J. Immunol. 156:932.
    • (1996) J. Immunol. , vol.156 , pp. 932
    • Lloyd, A.R.1    Oppenheim, J.J.2    Kelvin, D.J.3    Taub, D.D.4
  • 22
    • 0031952651 scopus 로고    scopus 로고
    • Are changes in integrin affinity and conformation overemphasized?
    • Bazzoni, G., and M. E. Hemler. 1998. Are changes in integrin affinity and conformation overemphasized? Trends. Biochem. Sci. 23:30.
    • (1998) Trends. Biochem. Sci. , vol.23 , pp. 30
    • Bazzoni, G.1    Hemler, M.E.2
  • 27
    • 0030059222 scopus 로고    scopus 로고
    • Role of rho in chemoattractant-activated leukocyte adhesion through integrins
    • Laudanna, C., J. J. Campbell, and E. C. Butcher. 1996. Role of rho in chemoattractant-activated leukocyte adhesion through integrins. Science 271:981.
    • (1996) Science , vol.271 , pp. 981
    • Laudanna, C.1    Campbell, J.J.2    Butcher, E.C.3
  • 28
    • 0029995797 scopus 로고    scopus 로고
    • Rho-stimulated contractility drives the formation of stress fibers and focal adhesions
    • Chrzanowska-Wodnicka, M., and K. Burridge. 1996. Rho-stimulated contractility drives the formation of stress fibers and focal adhesions. J. Cell Biol. 133:1403.
    • (1996) J. Cell Biol. , vol.133 , pp. 1403
    • Chrzanowska-Wodnicka, M.1    Burridge, K.2
  • 29
    • 0026778133 scopus 로고
    • The small GTP-binding protein Rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley, A. J., and A. Hall. 1992. The small GTP-binding protein Rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70:389.
    • (1992) Cell , vol.70 , pp. 389
    • Ridley, A.J.1    Hall, A.2
  • 30
    • 0029076191 scopus 로고
    • Role of the VLA-4 molecule in T cell costimulation: Identification of the tyrosine phosphorylation pattern induced by the ligation of VLA-4
    • Sato, T., K. Tachibana, Y. Nojima, N. D'Avirro, and C. Morimoto. 1995. Role of the VLA-4 molecule in T cell costimulation: identification of the tyrosine phosphorylation pattern induced by the ligation of VLA-4. J. Immunol. 155:2938.
    • (1995) J. Immunol. , vol.155 , pp. 2938
    • Sato, T.1    Tachibana, K.2    Nojima, Y.3    D'Avirro, N.4    Morimoto, C.5
  • 33
    • 0026002871 scopus 로고
    • Signaling by vascular cell adhesion molecule-1 (VCAM-1) through VLA-4 promotes CD3-dependent T cell proliferation
    • Burkly, L. C. A. Jakubowski, B. M. Newman, M. D. Rosa, G. Chi Rosso, and R. R. Lobb. 1991. Signaling by vascular cell adhesion molecule-1 (VCAM-1) through VLA-4 promotes CD3-dependent T cell proliferation. Eur. J. Immunol. 21:2871.
    • (1991) Eur. J. Immunol. , vol.21 , pp. 2871
    • Burkly, L.C.1    Jakubowski, A.2    Newman, B.M.3    Rosa, M.D.4    Chi Rosso, G.5    Lobb, R.R.6
  • 34
    • 0030240560 scopus 로고    scopus 로고
    • 1 (CD49d/CD29) integrin costimulation of human T cells enhances transcription factor and cytokine induction in the absence of altered sensitivity to anti-CD3 stimulation
    • 1 (CD49d/CD29) integrin costimulation of human T cells enhances transcription factor and cytokine induction in the absence of altered sensitivity to anti-CD3 stimulation. J. Immunol. 157:1965.
    • (1996) J. Immunol. , vol.157 , pp. 1965
    • Udagawa, T.1    Woodside, D.G.2    McIntyre, B.W.3
  • 36
    • 0028362088 scopus 로고
    • The induction of 72-kD gelatinase in T cells upon adhesion to endothelial cells is VCAM-1 dependent
    • Romanic, A. M., and J. A. Madri. 1994. The induction of 72-kD gelatinase in T cells upon adhesion to endothelial cells is VCAM-1 dependent. J. Cell Biol. 125:1165.
    • (1994) J. Cell Biol. , vol.125 , pp. 1165
    • Romanic, M.A.1    Madri, J.A.2
  • 37
    • 0026756730 scopus 로고
    • Integrins as a primary signal transduction molecule regulating monocyte immediate-early gene induction
    • Yurochko, A. D., D. Y. Liu, D. Eierman, and S. Haskill. 1992. Integrins as a primary signal transduction molecule regulating monocyte immediate-early gene induction. Proc. Natl. Acad. Sci. USA 89:9034.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9034
    • Yurochko, A.D.1    Liu, D.Y.2    Eierman, D.3    Haskill, S.4
  • 39
    • 0030948463 scopus 로고    scopus 로고
    • VLA-4 integrin cross-linking on human monocytic THP-1 cells induces tissue factor expression by a mechanism involving mitogen-activated protein kinase
    • McGilvray, I. D., Z. Lu, R. Bitar, A. P. B. Dackiw, C. J. Davreux, and O. D. Rotstein. 1997. VLA-4 integrin cross-linking on human monocytic THP-1 cells induces tissue factor expression by a mechanism involving mitogen-activated protein kinase. J. Biol. Chem. 272:10287.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10287
    • McGilvray, I.D.1    Lu, Z.2    Bitar, R.3    Dackiw, A.P.B.4    Davreux, C.J.5    Rotstein, O.D.6
  • 40
    • 0027679403 scopus 로고
    • Integrin cytoplasmic domains: Mediators of cytoskeletal linkages and extra- And intracellular initiated transmembrane signaling
    • Sastry, S. K., and A. F. Horwitz. 1993. Integrin cytoplasmic domains: mediators of cytoskeletal linkages and extra-and intracellular initiated transmembrane signaling. Curr. Opin. Cell Biol. 5:819.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 819
    • Sastry, S.K.1    Horwitz, A.F.2
  • 42
    • 0026596337 scopus 로고
    • Distinct cellular functions mediated by different VLA integrin α subunit cytoplasmic domains
    • Chan, B. M., P. D. Kassner, J. A. Schiro, H. R. Byers, T. S. Kupper, and M. E. Hemler. 1992. Distinct cellular functions mediated by different VLA integrin α subunit cytoplasmic domains. Cell 68:1051.
    • (1992) Cell , vol.68 , pp. 1051
    • Chan, B.M.1    Kassner, P.D.2    Schiro, J.A.3    Byers, H.R.4    Kupper, T.S.5    Hemler, M.E.6
  • 43
    • 0027169160 scopus 로고
    • Interchangeable a chain cytoplasmic domains play a positive role in control of cell adhesion mediated by VLA-4, a β1 integrin
    • Kassner, P. D., and M. E. Hemler. 1993. Interchangeable a chain cytoplasmic domains play a positive role in control of cell adhesion mediated by VLA-4, a β1 integrin. J. Exp. Med. 178:649.
    • (1993) J. Exp. Med. , vol.178 , pp. 649
    • Kassner, P.D.1    Hemler, M.E.2
  • 47
    • 0025871814 scopus 로고
    • EA-1, a novel adhesion molecule involved in the homing of progenitor T lymphocytes to the thymus
    • Imhof, B. A., P. Ruiz, B. Hesse, R. Palacios, and D. Dunon. 1991. EA-1, a novel adhesion molecule involved in the homing of progenitor T lymphocytes to the thymus. J. Cell Biol. 114:1069.
    • (1991) J. Cell Biol. , vol.114 , pp. 1069
    • Imhof, B.A.1    Ruiz, P.2    Hesse, B.3    Palacios, R.4    Dunon, D.5
  • 48
    • 0023818890 scopus 로고
    • Qualitative and quantitative heterogeneity in Pgp-1 expression among murine thymocytes
    • Lesley, J., R. Schulte, J. Trotter, and R. Hyman. 1988. Qualitative and quantitative heterogeneity in Pgp-1 expression among murine thymocytes. Cell Immunol. 112:40.
    • (1988) Cell Immunol. , vol.112 , pp. 40
    • Lesley, J.1    Schulte, R.2    Trotter, J.3    Hyman, R.4
  • 49
    • 0029156951 scopus 로고
    • Expression of the mucosal vascular addressin, MAdCAM-1, on sinus-lining cells in the spleen
    • Kraal, G., K. Schornagel, P. R. Streeter, B. Holzmann, and E. C. Butcher. 1995. Expression of the mucosal vascular addressin, MAdCAM-1, on sinus-lining cells in the spleen. Am. J. Pathol. 147:763.
    • (1995) Am. J. Pathol. , vol.147 , pp. 763
    • Kraal, G.1    Schornagel, K.2    Streeter, P.R.3    Holzmann, B.4    Butcher, E.C.5
  • 50
    • 0024075849 scopus 로고
    • Expression of functional human EGF receptor on murine bone marrow cells
    • von Ruden, T., and E. F. Wagner. 1988. Expression of functional human EGF receptor on murine bone marrow cells. EMBO J. 7:2749.
    • (1988) EMBO J. , vol.7 , pp. 2749
    • Von Ruden, T.1    Wagner, E.F.2
  • 51
    • 0023871422 scopus 로고
    • A safe packaging line for gene transfer: Separating viral genes on two different plasmids
    • Markowitz, D., S. Golf, and A. Bank. 1988. A safe packaging line for gene transfer: separating viral genes on two different plasmids. J. Virol. 62:1120.
    • (1988) J. Virol. , vol.62 , pp. 1120
    • Markowitz, D.1    Golf, S.2    Bank, A.3
  • 52
    • 0027496638 scopus 로고
    • 4 subunit of the integrin VLA-4: Distinct effects on adhesion to CS1/ fibronectin, VCAM-1, and invasin
    • 4 subunit of the integrin VLA-4: distinct effects on adhesion to CS1/ fibronectin, VCAM-1, and invasin. J. Cell Biol. 123:245.
    • (1993) J. Cell Biol. , vol.123 , pp. 245
    • Masumoto, A.1    Hemler, M.E.2
  • 53
    • 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 M. E. Hemler. 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
  • 54
    • 0028128178 scopus 로고
    • Minimum α chain cytoplasmic tail sequences needed to support integrin-mediated adhesion
    • Kassner, P. D., S. Kawaguchi, and M. E. Hemler. 1994. Minimum α chain cytoplasmic tail sequences needed to support integrin-mediated adhesion. J. Biol. Chem. 269:19859.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19859
    • Kassner, P.D.1    Kawaguchi, S.2    Hemler, M.E.3
  • 55
    • 0030694439 scopus 로고    scopus 로고
    • 4 integrin antibody induces apoptosis in murine thymocytes and staphylococcal enterotoxin B-activated lymph node T cells
    • 4 integrin antibody induces apoptosis in murine thymocytes and staphylococcal enterotoxin B-activated lymph node T cells. Immunology 92:321.
    • (1997) Immunology , vol.92 , pp. 321
    • Tchilian, E.Z.1    Owen, J.J.T.2    Jenkinson, E.J.3
  • 56
    • 0030840113 scopus 로고    scopus 로고
    • Mutational evidence for control of cell adhesion through integrin diffusion/clustering, independent of ligand binding
    • Yauch, R. L., D. P. Felsenfeld, S.-K. Kraeft, L. B. Chen, M. P. Sheetz, and M. E. Hemler. 1997. Mutational evidence for control of cell adhesion through integrin diffusion/clustering, independent of ligand binding. J. Exp. Med. 186: 1347.
    • (1997) J. Exp. Med. , vol.186 , pp. 1347
    • Yauch, R.L.1    Felsenfeld, D.P.2    Kraeft, S.-K.3    Chen, L.B.4    Sheetz, M.P.5    Hemler, M.E.6
  • 59
    • 0024418764 scopus 로고
    • Identification and characterization of the T lymphocyte adhesion receptor for an alternative cell attachment domain (CS-1) in plasma fibronectin
    • Wayner, E. A., A. Garcia Pardo, M. J. Humphries, J. A. McDonald, and W.G. Carter. 1989. Identification and characterization of the T lymphocyte adhesion receptor for an alternative cell attachment domain (CS-1) in plasma fibronectin. J. Cell Biol. 109:1321.
    • (1989) J. Cell Biol. , vol.109 , pp. 1321
    • Wayner, E.A.1    Garcia Pardo, A.2    Humphries, M.J.3    McDonald, J.A.4    Carter, W.G.5
  • 60
    • 0028047388 scopus 로고
    • Focal adhesion as a signal transduction organelle
    • Lo, S. H., and L. B. Chen. 1994. Focal adhesion as a signal transduction organelle. Cancer Metastasis Rev. 13:9.
    • (1994) Cancer Metastasis Rev. , vol.13 , pp. 9
    • Lo, S.H.1    Chen, L.B.2
  • 62
    • 0028954797 scopus 로고
    • Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function
    • Miyamoto, S., S. K. Akiyama, and K. M. Yamada. 1995. Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function. Science 267:883. The Journal of Immunology, 1998, 161: 5987-5996.
    • (1995) Science , vol.267 , pp. 883
    • Miyamoto, S.1    Akiyama, S.K.2    Yamada, K.M.3


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