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Volumn 29, Issue 9, 1999, Pages 2875-2885

The small GTP-binding proteins Rho and Rac induce T cell adhesion to the mucosal addressin MAdCAM-1 in a hierarchical fashion

Author keywords

Integrin activation; Integrin 4 7; MAdCAM 1; Rac1; RhoA

Indexed keywords

ENZYME; GUANINE NUCLEOTIDE BINDING PROTEIN; INTEGRIN; MANGANESE; MEVINOLIN; MICROSPHERE; MUCOSAL ADDRESSIN CELL ADHESION MOLECULE 1; PROTEIN KINASE C; PROTEIN TYROSINE KINASE;

EID: 0033391502     PISSN: 00142980     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1521-4141(199909)29:09<2875::aid-immu2875>3.0.co;2-i     Document Type: Article
Times cited : (7)

References (41)
  • 1
    • 0024469059 scopus 로고
    • Peyer's patch-specific lymphocyte homing receptors consist of a VLA-4-like α chain associated with either of two integrin β chains, one of which is novel
    • Holzmann, B. and Weissmann, I. L., Peyer's patch-specific lymphocyte homing receptors consist of a VLA-4-like α chain associated with either of two integrin β chains, one of which is novel. EMBO J. 1989. 8: 1735-1741.
    • (1989) EMBO J. , vol.8 , pp. 1735-1741
    • Holzmann, B.1    Weissmann, I.L.2
  • 6
    • 0029145205 scopus 로고
    • Construction and adhesive properties of a soluble MAdCAM-1-Fc chimera expressed in a baculovirus system: Phylogenetic conservation of receptor-ligand interaction
    • Yang, Y., Sammar, M., Harrison, J. E. B., Lehnert, K., Print, C. G., Leung, E., Prestidge, R. and Krissansen, G. W., Construction and adhesive properties of a soluble MAdCAM-1-Fc chimera expressed in a baculovirus system: phylogenetic conservation of receptor-ligand interaction. Scand. J. Immunol. 1995. 42: 235-247.
    • (1995) Scand. J. Immunol. , vol.42 , pp. 235-247
    • Yang, Y.1    Sammar, M.2    Harrison, J.E.B.3    Lehnert, K.4    Print, C.G.5    Leung, E.6    Prestidge, R.7    Krissansen, G.W.8
  • 7
    • 0027944111 scopus 로고
    • Adhesion between epithelial cells and T lymphocytes mediated by E-cadherin and the α4β7 integrin
    • Cepek, K. L., Shaw, S. K., Parker, C. M., Russell, G. J., Morrow, J. S., Rimm, D. L. and Brenner, M. B., Adhesion between epithelial cells and T lymphocytes mediated by E-cadherin and the α4β7 integrin. Nature 1994. 372: 190-193.
    • (1994) Nature , vol.372 , pp. 190-193
    • Cepek, K.L.1    Shaw, S.K.2    Parker, C.M.3    Russell, G.J.4    Morrow, J.S.5    Rimm, D.L.6    Brenner, M.B.7
  • 8
    • 0028954002 scopus 로고
    • Recognition of E-cadherin on epithelial cells by the mucosal T cell integrin αM290β7 (α4β7)
    • Karecla, P. I., Bowden, S. J., Green, S. J. and Kilshaw, P. J., Recognition of E-cadherin on epithelial cells by the mucosal T cell integrin αM290β7 (α4β7). Eur. J. Immunol. 1995. 25: 852-856.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 852-856
    • Karecla, P.I.1    Bowden, S.J.2    Green, S.J.3    Kilshaw, P.J.4
  • 10
    • 0030840113 scopus 로고    scopus 로고
    • Mutational evidence for control of cell adhesion through integrin diffusion/clustering, independent of ligand binding
    • Yauch, R. L., Felsenfeld, D. P., Kraeft, S.-K., Chen, L. B., Sheetz, M. P. and Hemler, M. E., Mutational evidence for control of cell adhesion through integrin diffusion/clustering, independent of ligand binding. J. Exp. Med. 1997. 186: 1347-1355.
    • (1997) J. Exp. Med. , vol.186 , pp. 1347-1355
    • Yauch, R.L.1    Felsenfeld, D.P.2    Kraeft, S.-K.3    Chen, L.B.4    Sheetz, M.P.5    Hemler, M.E.6
  • 11
    • 0028984448 scopus 로고
    • Vascular cell adhesion molecule (VCAM)-lg fusion protein defines distinct affinity states of the very late antigen-4 (VLA-4) receptor
    • Jakubowski, A., Rosa, M. D., Bixler, S., Lobb, R. and Burkly, L. C., Vascular cell adhesion molecule (VCAM)-lg fusion protein defines distinct affinity states of the Very Late Antigen-4 (VLA-4) receptor. Cell Adhes. Commun. 1995. 3: 131-142.
    • (1995) Cell Adhes. Commun. , vol.3 , pp. 131-142
    • Jakubowski, A.1    Rosa, M.D.2    Bixler, S.3    Lobb, R.4    Burkly, L.C.5
  • 13
    • 0031806711 scopus 로고    scopus 로고
    • Rac regulates integrin-mediated spreading and increased adhesion of T lymphocytes
    • D'Souza-Schorey, C., Boettner, B. and van Aelst, L., Rac regulates integrin-mediated spreading and increased adhesion of T lymphocytes. Mol. Cell. Biol. 1998. 18: 3936-3946.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3936-3946
    • D'Souza-Schorey, C.1    Boettner, B.2    Van Aelst, L.3
  • 14
    • 0032528561 scopus 로고    scopus 로고
    • Secondary lymphoid-tissue chemokine (SLC) stimulates integrin alpha 4 beta 7-mediated adhesion of lymphocytes to mucosal addressin cell adhesion molecule-1 (MAdCAM-1) under flow
    • Pachynski, R. K., Wu, S. W., Gunn, M. D. and Erle, D. J., Secondary lymphoid-tissue chemokine (SLC) stimulates integrin alpha 4 beta 7-mediated adhesion of lymphocytes to mucosal addressin cell adhesion molecule-1 (MAdCAM-1) under flow. J. Immunol. 1998. 161: 952-956.
    • (1998) J. Immunol. , vol.161 , pp. 952-956
    • Pachynski, R.K.1    Wu, S.W.2    Gunn, M.D.3    Erle, D.J.4
  • 15
    • 0022181070 scopus 로고
    • Inhibition of lymphocyte and neutrophil chemotaxis by pertussis toxin
    • Spangrude, G. J., Sacchi, F., Hill, H. R., Van Epps, D. E. and Daynes, R. A., Inhibition of lymphocyte and neutrophil chemotaxis by pertussis toxin. J. Immunol. 1985. 135: 4135-4143.
    • (1985) J. Immunol. , vol.135 , pp. 4135-4143
    • Spangrude, G.J.1    Sacchi, F.2    Hill, H.R.3    Van Epps, D.E.4    Daynes, R.A.5
  • 16
    • 0021325825 scopus 로고
    • Molecular mechanisms of lymphocyte extravasation. I. Studies of two selective inhibitors of lymphocyte recirculation
    • Spangrude, G. J., Braaten, B. A. and Daynes, R. A., Molecular mechanisms of lymphocyte extravasation. I. Studies of two selective inhibitors of lymphocyte recirculation. J. Immunol. 1984. 132: 354-362.
    • (1984) J. Immunol. , vol.132 , pp. 354-362
    • Spangrude, G.J.1    Braaten, B.A.2    Daynes, R.A.3
  • 17
    • 0027965652 scopus 로고
    • Structures of active conformations of Giα1 and the mechanism of GTP hydrolysis
    • Coleman, D. E., Berghuis, A. M., Lee, E., Linder, M. E., Gilman, A. G. and Sprang, S. R., Structures of active conformations of Giα1 and the mechanism of GTP hydrolysis. Science 1994. 265: 1405-1412.
    • (1994) Science , vol.265 , pp. 1405-1412
    • Coleman, D.E.1    Berghuis, A.M.2    Lee, E.3    Linder, M.E.4    Gilman, A.G.5    Sprang, S.R.6
  • 18
    • 0031569360 scopus 로고    scopus 로고
    • Activation of G-proteins with AIF4-induces LFA-1-mediated adhesion of T-cell hybridoma cells to ICAM-1 by signal pathways that differ from phorbol ester-and manganese-induced adhesion
    • Driessens, M. H. E., Van Hulten, P. E. M., Van Rijthoven, E. A. M., Soede, R. D. M. and Roos, E., Activation of G-proteins with AIF4-induces LFA-1-mediated adhesion of T-cell hybridoma cells to ICAM-1 by signal pathways that differ from phorbol ester-and manganese-induced adhesion. Exp. Cell Res. 1997. 231: 242-250.
    • (1997) Exp. Cell Res. , vol.231 , pp. 242-250
    • Driessens, M.H.E.1    Van Hulten, P.E.M.2    Van Rijthoven, E.A.M.3    Soede, R.D.M.4    Roos, E.5
  • 19
    • 0030059222 scopus 로고    scopus 로고
    • Role of rho in chemoattractant-activated leukocyte adhesion through integrins
    • Laudanna, C., Campbell, J. J. and Butcher, E. C., Role of rho in chemoattractant-activated leukocyte adhesion through integrins. Science 1996. 271: 981-983.
    • (1996) Science , vol.271 , pp. 981-983
    • Laudanna, C.1    Campbell, J.J.2    Butcher, E.C.3
  • 20
    • 0027471215 scopus 로고
    • Inhibition of PMA-induced, LFA-1-dependent lymphocyte aggregation by ADP ribosylation of the small molecular weight GTP binding protein, rho
    • Tominaga, T., Sugie, K., Hirata, M., Morii, N., Fukata, J., Uchida, A., Imura, H. and Narumiya, S., Inhibition of PMA-induced, LFA-1-dependent lymphocyte aggregation by ADP ribosylation of the small molecular weight GTP binding protein, rho. J. Cell Biol. 1993. 120: 1529-1537.
    • (1993) J. Cell Biol. , vol.120 , pp. 1529-1537
    • Tominaga, T.1    Sugie, K.2    Hirata, M.3    Morii, N.4    Fukata, J.5    Uchida, A.6    Imura, H.7    Narumiya, S.8
  • 21
    • 0028961293 scopus 로고
    • Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes, C. D. and Hall, A., Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 1995. 81: 53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 22
    • 0027221825 scopus 로고
    • Mevalonate controls cytoskeleton organization and cell morphology in thyroid epithelial cells
    • Bifulco, M., Laezza, C., Aloi, S. M. and Garbi, C., Mevalonate controls cytoskeleton organization and cell morphology in thyroid epithelial cells. J. Cell Physiol. 1992. 155: 340-348.
    • (1992) J. Cell Physiol. , vol.155 , pp. 340-348
    • Bifulco, M.1    Laezza, C.2    Aloi, S.M.3    Garbi, C.4
  • 23
    • 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 Hall, A., The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 1992. 70: 389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 24
    • 0028321785 scopus 로고
    • Signal transduction pathways regulating Rho-mediated stress fibre formation: Requirement for a tyrosine kinase
    • Ridley, A. J. and Hall, A., Signal transduction pathways regulating Rho-mediated stress fibre formation: requirement for a tyrosine kinase. EMBO J. 1994. 13: 2600-2610.
    • (1994) EMBO J. , vol.13 , pp. 2600-2610
    • Ridley, A.J.1    Hall, A.2
  • 25
    • 0029965232 scopus 로고    scopus 로고
    • PI 3-kinase: A pivotal pathway in T-cell activation?
    • Ward, S. G., June, C. H. and Olive, D., PI 3-kinase: a pivotal pathway in T-cell activation? Immunol. Today 1996. 17: 187-196.
    • (1996) Immunol. Today , vol.17 , pp. 187-196
    • Ward, S.G.1    June, C.H.2    Olive, D.3
  • 26
    • 0025996803 scopus 로고
    • Fluoride is not an activator of the smaller (20-25 kDa) GTP-binding proteins
    • Kahn, R. A., Fluoride is not an activator of the smaller (20-25 kDa) GTP-binding proteins. J. Biol. Chem. 1991. 266: 15595-15597.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15595-15597
    • Kahn, R.A.1
  • 27
    • 0024445852 scopus 로고
    • Transfer of monoclonal antibodies into mammalian cells by electroporation
    • Chakrabati, R., Wylie, D. E. and Schuster, S. M., Transfer of monoclonal antibodies into mammalian cells by electroporation. J. Biol. Chem. 1989. 264: 15494-15500.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15494-15500
    • Chakrabati, R.1    Wylie, D.E.2    Schuster, S.M.3
  • 28
    • 0031881787 scopus 로고    scopus 로고
    • LPAM-1 (integrin α4β7)-ligand binding: Overlapping binding sites recognizing VCAM-1, MAdCAM-1 and CS-1 are blocked by fibrinogen, a fibronectin-like polymer and RGD-like cyclic peptides
    • Yang, Y., Cardarelli, P. M., Lehnert, K., Rowland, S. and Krissansen, G. W., LPAM-1 (integrin α4β7)-ligand binding: overlapping binding sites recognizing VCAM-1, MAdCAM-1 and CS-1 are blocked by fibrinogen, a fibronectin-like polymer and RGD-like cyclic peptides. Eur. J. Immunol. 1998. 28: 995-1004.
    • (1998) Eur. J. Immunol. , vol.28 , pp. 995-1004
    • Yang, Y.1    Cardarelli, P.M.2    Lehnert, K.3    Rowland, S.4    Krissansen, G.W.5
  • 29
    • 0029126042 scopus 로고
    • RANTES-activated human T lymphocytes. A role for phosphoinositide 3-kinase
    • Turner, L., Ward, S. G. and Westwick, J., RANTES-activated human T lymphocytes. A role for phosphoinositide 3-kinase. J. Immunol. 1995. 155: 2437-2444.
    • (1995) J. Immunol. , vol.155 , pp. 2437-2444
    • Turner, L.1    Ward, S.G.2    Westwick, J.3
  • 30
    • 0028837170 scopus 로고
    • Activation of the small GTP-binding proteins Rho and Rac by growth factor receptors
    • Nobes, C., Hawkins, P., Stephens, L. and Hall, A., Activation of the small GTP-binding proteins Rho and Rac by growth factor receptors. J. Cell Sci. 1995. 108: 225-233.
    • (1995) J. Cell Sci. , vol.108 , pp. 225-233
    • Nobes, C.1    Hawkins, P.2    Stephens, L.3    Hall, A.4
  • 33
    • 0031459917 scopus 로고    scopus 로고
    • Cdc42 and Rac1 induce integrin-mediated cell motility and invasiveness through PI(S)K
    • Parise, L. V., Cdc42 and Rac1 induce integrin-mediated cell motility and invasiveness through PI(S)K. Nature 1997. 390: 632-636.
    • (1997) Nature , vol.390 , pp. 632-636
    • Parise, L.V.1
  • 35
    • 0025992433 scopus 로고    scopus 로고
    • Evidence that the signal-initiating membrane protein CD9 is associated with small GTP-binding proteins
    • Seehafer, J. G. and Shaw, A. R., Evidence that the signal-initiating membrane protein CD9 is associated with small GTP-binding proteins. Biochem. Biophys. Res. Commun. 179: 401-406.
    • Biochem. Biophys. Res. Commun. , vol.179 , pp. 401-406
    • Seehafer, J.G.1    Shaw, A.R.2
  • 37
    • 0032935495 scopus 로고    scopus 로고
    • An essential part for rho-associated kinase in the transcellular invasion of tumor cells
    • Itoh, K., Yoshioka, K., Akedo, H., Uehata, M., Ishizaki, T. and Narumiya, S., An essential part for rho-associated kinase in the transcellular invasion of tumor cells. Nature Med. 1999. 5: 221-225.
    • (1999) Nature Med. , vol.5 , pp. 221-225
    • Itoh, K.1    Yoshioka, K.2    Akedo, H.3    Uehata, M.4    Ishizaki, T.5    Narumiya, S.6
  • 38
    • 0031878095 scopus 로고    scopus 로고
    • Na-H exchange acts downstream of RhoA to regulate integrin-induced cell adhesion and spreading
    • Tominaga, T. and Barber, D. L., Na-H exchange acts downstream of RhoA to regulate integrin-induced cell adhesion and spreading. Mol. Biol. Cell 1998. 9: 2287-2303.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2287-2303
    • Tominaga, T.1    Barber, D.L.2
  • 39
    • 0031893954 scopus 로고    scopus 로고
    • Rack1, a receptor for activated protein kinase C, interacts with integrin β subunit
    • Lilienthal, J. and Chang, D. D., Rack1, a receptor for activated protein kinase C, interacts with integrin β subunit. J. Biol. Chem. 1998. 273: 2379-2383.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2379-2383
    • Lilienthal, J.1    Chang, D.D.2
  • 40
    • 0032538433 scopus 로고    scopus 로고
    • The human WD repeat protein WAIT-1 specifically interacts with the cytoplasmic tails of beta7-integrins
    • Rietzler, M., Bittner, M., Kolanus, W., Schuster, A. and Holzmann, B., The human WD repeat protein WAIT-1 specifically interacts with the cytoplasmic tails of beta7-integrins. J. Biol. Chem. 1998. 273: 27459-27466.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27459-27466
    • Rietzler, M.1    Bittner, M.2    Kolanus, W.3    Schuster, A.4    Holzmann, B.5
  • 41
    • 0029151366 scopus 로고
    • Purification and assay of recombinant C3 transferase
    • Dillon, S. T. and Feig, L. A., Purification and assay of recombinant C3 transferase. Methods Enzymol. 1995. 256: 174-184.
    • (1995) Methods Enzymol. , vol.256 , pp. 174-184
    • Dillon, S.T.1    Feig, L.A.2


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