메뉴 건너뛰기




Volumn 312, Issue 20, 2006, Pages 4056-4069

P-selectin activates integrin-mediated colon carcinoma cell adhesion to fibronectin

Author keywords

Cell adhesion; Integrins; P selectin

Indexed keywords

CHIMERIC PROTEIN; FIBRONECTIN; IMMUNOGLOBULIN G; INTEGRIN; MITOGEN ACTIVATED PROTEIN KINASE P38; PADGEM PROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3 KINASE INHIBITOR; VERY LATE ACTIVATION ANTIGEN 5;

EID: 37849188247     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2006.09.008     Document Type: Article
Times cited : (33)

References (111)
  • 1
    • 0034953811 scopus 로고    scopus 로고
    • Tumor cell adhesion under hydrodynamic conditions of fluid flow
    • Haier J., and Nicolson G. Tumor cell adhesion under hydrodynamic conditions of fluid flow. APMIS 109 (2001) 241-262
    • (2001) APMIS , vol.109 , pp. 241-262
    • Haier, J.1    Nicolson, G.2
  • 2
    • 0029964982 scopus 로고    scopus 로고
    • A human colon carcinoma cell line exhibits adhesive interactions with P-selectin under fluid flow via a PSGL-1-independent mechanism
    • Goetz D., Ding H., Atkinson W., Vachino G., Camphausen R., Cumming D., and Luscinskas F. A human colon carcinoma cell line exhibits adhesive interactions with P-selectin under fluid flow via a PSGL-1-independent mechanism. Am. J. Pathol. 149 (1996) 1661-1673
    • (1996) Am. J. Pathol. , vol.149 , pp. 1661-1673
    • Goetz, D.1    Ding, H.2    Atkinson, W.3    Vachino, G.4    Camphausen, R.5    Cumming, D.6    Luscinskas, F.7
  • 3
    • 0036488589 scopus 로고    scopus 로고
    • Role of integrins in cell invasion and migration
    • Hood J., and Cheresh D. Role of integrins in cell invasion and migration. Nat. Rev., Cancer. 2 (2002) 91-100
    • (2002) Nat. Rev., Cancer. , vol.2 , pp. 91-100
    • Hood, J.1    Cheresh, D.2
  • 4
    • 0032555123 scopus 로고    scopus 로고
    • P-selectin mediates adhesion of the human melanoma cell line NKI-4: identification of glycoprotein ligands
    • Kaytes P., and Geng J. P-selectin mediates adhesion of the human melanoma cell line NKI-4: identification of glycoprotein ligands. Biochemistry 37 (1998) 10514-10521
    • (1998) Biochemistry , vol.37 , pp. 10514-10521
    • Kaytes, P.1    Geng, J.2
  • 5
    • 0026438280 scopus 로고
    • Biomechanical interactions of cancer cells with the microvasculature during hematogenous metastasis
    • Weiss L. Biomechanical interactions of cancer cells with the microvasculature during hematogenous metastasis. Cancer Metastasis Rev. 11 (1992) 227-235
    • (1992) Cancer Metastasis Rev. , vol.11 , pp. 227-235
    • Weiss, L.1
  • 6
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: bidirectional, allosteric signaling machines
    • Hynes R. Integrins: bidirectional, allosteric signaling machines. Cell 110 (2002) 673-687
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.1
  • 7
    • 3442879850 scopus 로고    scopus 로고
    • Mitogenic signal transduction by integrin- and growth factor receptor-mediated pathways
    • Lee J., and Juliano R. Mitogenic signal transduction by integrin- and growth factor receptor-mediated pathways. Mol. Cell. Biol. 17 (2004) 188-202
    • (2004) Mol. Cell. Biol. , vol.17 , pp. 188-202
    • Lee, J.1    Juliano, R.2
  • 8
    • 0036229694 scopus 로고    scopus 로고
    • Networks and crosstalk: integrin signalling spreads
    • Schwartz M., and Ginsberg M. Networks and crosstalk: integrin signalling spreads. Nat. Cell Biol. 4 (2002) E65-E68
    • (2002) Nat. Cell Biol. , vol.4
    • Schwartz, M.1    Ginsberg, M.2
  • 9
    • 0035724579 scopus 로고    scopus 로고
    • Function and interactions of integrins
    • van der Flier A., and Sonnenberg A. Function and interactions of integrins. Cell Tissue Res. 305 (2001) 238-285
    • (2001) Cell Tissue Res. , vol.305 , pp. 238-285
    • van der Flier, A.1    Sonnenberg, A.2
  • 10
    • 0033551899 scopus 로고    scopus 로고
    • Integrin signaling
    • Giancotti F., and Ruoslahti E. Integrin signaling. Science 285 (1999) 1028-1032
    • (1999) Science , vol.285 , pp. 1028-1032
    • Giancotti, F.1    Ruoslahti, E.2
  • 11
    • 0037009042 scopus 로고    scopus 로고
    • Integrin activation takes shape
    • Liddington R., and Ginsberg M. Integrin activation takes shape. J. Cell Biol. 158 (2002) 833-839
    • (2002) J. Cell Biol. , vol.158 , pp. 833-839
    • Liddington, R.1    Ginsberg, M.2
  • 12
    • 0027373782 scopus 로고
    • Activation of protein kinase C precedes alpha 5 beta 1 integrin-mediated cell spreading on fibronectin
    • Vuori K., and Ruoslahti E. Activation of protein kinase C precedes alpha 5 beta 1 integrin-mediated cell spreading on fibronectin. J. Biol. Chem. 268 (1993) 21459-21462
    • (1993) J. Biol. Chem. , vol.268 , pp. 21459-21462
    • Vuori, K.1    Ruoslahti, E.2
  • 13
    • 0024828456 scopus 로고
    • Enhancement of LFA-1-mediated cell adhesion by triggering through CD2 or CD3 on T lymphocytes
    • van Kooyk Y., van de Wiel-van Kemenade P., Weder P., Kuijpers T., and Figdor C. Enhancement of LFA-1-mediated cell adhesion by triggering through CD2 or CD3 on T lymphocytes. Nature 342 (1989) 811-813
    • (1989) Nature , vol.342 , pp. 811-813
    • van Kooyk, Y.1    van de Wiel-van Kemenade, P.2    Weder, P.3    Kuijpers, T.4    Figdor, C.5
  • 14
    • 0031952651 scopus 로고    scopus 로고
    • Are changes in integrin affinity and conformation overemphasized?
    • Bazzoni G., and Hemler M. Are changes in integrin affinity and conformation overemphasized?. Trends Biochem. Sci. 23 (1998) 30-34
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 30-34
    • Bazzoni, G.1    Hemler, M.2
  • 15
    • 0032904627 scopus 로고    scopus 로고
    • Mechanisms that regulate the function of the selectins and their ligands
    • Vestweber D., and Blanks J. Mechanisms that regulate the function of the selectins and their ligands. Physiol. Rev. 79 (1999) 181-213
    • (1999) Physiol. Rev. , vol.79 , pp. 181-213
    • Vestweber, D.1    Blanks, J.2
  • 17
    • 0027249917 scopus 로고
    • P-selectin mediates adhesion of platelets to neuroblastoma and small cell lung cancer
    • Stone J., and Wagner D. P-selectin mediates adhesion of platelets to neuroblastoma and small cell lung cancer. J. Clin. Invest. 92 (1993) 804-813
    • (1993) J. Clin. Invest. , vol.92 , pp. 804-813
    • Stone, J.1    Wagner, D.2
  • 18
    • 0027982876 scopus 로고
    • Traffic signals for lymphocytes recirculation and leukocyte emigration: the multistep paradigm
    • Springer T. Traffic signals for lymphocytes recirculation and leukocyte emigration: the multistep paradigm. Cell 76 (1994) 301-314
    • (1994) Cell , vol.76 , pp. 301-314
    • Springer, T.1
  • 19
    • 0033233156 scopus 로고    scopus 로고
    • b1-integrin mediated dynamic adhesion of colon carcinoma cells to extracellular matrix under laminar flow
    • Haier J., Nasralla M., and Nicolson G. b1-integrin mediated dynamic adhesion of colon carcinoma cells to extracellular matrix under laminar flow. Clin. Exp. Metastasis 17 (1999) 377-387
    • (1999) Clin. Exp. Metastasis , vol.17 , pp. 377-387
    • Haier, J.1    Nasralla, M.2    Nicolson, G.3
  • 20
    • 0028172398 scopus 로고
    • Integrin alpha(4)beta(1)-mediate melanoma cell adhesion and migration on vascular cell adhesion molecule-1 (VCAM-1) and the alternatively splice IIICS region of fibronectin
    • Mould A., Askari J., Craig S., Garratt A., Clements J., and Humphries M. Integrin alpha(4)beta(1)-mediate melanoma cell adhesion and migration on vascular cell adhesion molecule-1 (VCAM-1) and the alternatively splice IIICS region of fibronectin. J. Biol. Chem. 269 (1994) 27224-27230
    • (1994) J. Biol. Chem. , vol.269 , pp. 27224-27230
    • Mould, A.1    Askari, J.2    Craig, S.3    Garratt, A.4    Clements, J.5    Humphries, M.6
  • 21
    • 0028044784 scopus 로고
    • Differential E-selectin-dependent adhesion efficiency in sublines of a human colon cancer exhibiting distinct metastatic potentials
    • Sawada R., Tsuboi S., and Fukuda M. Differential E-selectin-dependent adhesion efficiency in sublines of a human colon cancer exhibiting distinct metastatic potentials. J. Biol. Chem. 269 (1994) 1425-1431
    • (1994) J. Biol. Chem. , vol.269 , pp. 1425-1431
    • Sawada, R.1    Tsuboi, S.2    Fukuda, M.3
  • 22
    • 0025572708 scopus 로고
    • Recognition by ELAM-1 of the sialyl-Lex determinant on myeloid and tumor cells
    • Walz G., Aruffo A., Kolanus W., Bevilacqua M., and Seed B. Recognition by ELAM-1 of the sialyl-Lex determinant on myeloid and tumor cells. Science 250 (1990) 1132-1135
    • (1990) Science , vol.250 , pp. 1132-1135
    • Walz, G.1    Aruffo, A.2    Kolanus, W.3    Bevilacqua, M.4    Seed, B.5
  • 26
    • 0032528432 scopus 로고    scopus 로고
    • Molecular regulation of the interaction between leukocyte function-associated antigen-1 and soluble ICAM-1 by divalent metal cations
    • Labadia M., Jeanfavre D., Caviness G., and Morelock M. Molecular regulation of the interaction between leukocyte function-associated antigen-1 and soluble ICAM-1 by divalent metal cations. J. Immnol. 161 (1998) 836-842
    • (1998) J. Immnol. , vol.161 , pp. 836-842
    • Labadia, M.1    Jeanfavre, D.2    Caviness, G.3    Morelock, M.4
  • 27
    • 0031975762 scopus 로고    scopus 로고
    • Affinity and kinetic analysis of L-selectin (CD62L) binding to glycosylation-dependent cell-adhesion molecule-1
    • Nicholson M., Barclay A., Singer M., Rosen S., and van der Merwe P. Affinity and kinetic analysis of L-selectin (CD62L) binding to glycosylation-dependent cell-adhesion molecule-1. J. Biol. Chem. 273 (1998) 763-770
    • (1998) J. Biol. Chem. , vol.273 , pp. 763-770
    • Nicholson, M.1    Barclay, A.2    Singer, M.3    Rosen, S.4    van der Merwe, P.5
  • 28
    • 0347949622 scopus 로고    scopus 로고
    • The molecular mechanics of P- and L-selectin lectin domains binding to PSGL-1
    • Rinko L., Lawrence M., and Guilford W. The molecular mechanics of P- and L-selectin lectin domains binding to PSGL-1. Biophys. J. 86 (2004) 544-554
    • (2004) Biophys. J. , vol.86 , pp. 544-554
    • Rinko, L.1    Lawrence, M.2    Guilford, W.3
  • 30
    • 0031913666 scopus 로고    scopus 로고
    • Stimulation of P-selectin glycoprotein ligand-1 on mouse neutrophils activates beta 2-integrin mediated cell attachment to ICAM-1
    • Blanks J., Moll T., Eytner R., and Vestweber D. Stimulation of P-selectin glycoprotein ligand-1 on mouse neutrophils activates beta 2-integrin mediated cell attachment to ICAM-1. Eur. J. Immunol. 28 (1998) 433-443
    • (1998) Eur. J. Immunol. , vol.28 , pp. 433-443
    • Blanks, J.1    Moll, T.2    Eytner, R.3    Vestweber, D.4
  • 31
    • 0031066763 scopus 로고    scopus 로고
    • T cell adhesion to P-selectin induces tyrosine phosphorylation of pp125 focal adhesion kinase and other substrates
    • Haller H., Kunzendorf U., Sacherer K., Lindschau C., Walz G., Distler A., and Luft F. T cell adhesion to P-selectin induces tyrosine phosphorylation of pp125 focal adhesion kinase and other substrates. J. Immunol. 158 (1997) 1061-1067
    • (1997) J. Immunol. , vol.158 , pp. 1061-1067
    • Haller, H.1    Kunzendorf, U.2    Sacherer, K.3    Lindschau, C.4    Walz, G.5    Distler, A.6    Luft, F.7
  • 32
    • 0027483361 scopus 로고
    • Identification of a glycoprotein ligand for E-selectin on mouse myeloid cells
    • Levinovitz A., Muhlhoff J., Isenmann S., and Vestweber D. Identification of a glycoprotein ligand for E-selectin on mouse myeloid cells. J. Cell Biol. 121 (1993) 449-459
    • (1993) J. Cell Biol. , vol.121 , pp. 449-459
    • Levinovitz, A.1    Muhlhoff, J.2    Isenmann, S.3    Vestweber, D.4
  • 34
    • 0030988260 scopus 로고    scopus 로고
    • Adhesion of HT-29 colon carcinoma cells to E-selectin results in increased tyrosine phosphorylation and decreased activity of c-src
    • Soltesz S., Powers E., Geng J., and Fisher C. Adhesion of HT-29 colon carcinoma cells to E-selectin results in increased tyrosine phosphorylation and decreased activity of c-src. Int. J. Cancer 71 (1997) 645-653
    • (1997) Int. J. Cancer , vol.71 , pp. 645-653
    • Soltesz, S.1    Powers, E.2    Geng, J.3    Fisher, C.4
  • 35
    • 0024359871 scopus 로고
    • Analysis of fibronectin receptor function with monoclonal antibodies: roles in cell adhesion, migration, matrix assembly, and cytoskeletal organization
    • Akiyama S., Yamada S., Chen W., and Yamada K. Analysis of fibronectin receptor function with monoclonal antibodies: roles in cell adhesion, migration, matrix assembly, and cytoskeletal organization. J. Cell Biol. 109 (1989) 863-875
    • (1989) J. Cell Biol. , vol.109 , pp. 863-875
    • Akiyama, S.1    Yamada, S.2    Chen, W.3    Yamada, K.4
  • 36
    • 0027994108 scopus 로고
    • Single subunit chimeric integrins as mimics and inhibitors of endogenous integrin function in receptor localization, cell spreading and migration, and matrix assembly
    • LaFlamme S., Thomas L., Yamada S., and Yamada K. Single subunit chimeric integrins as mimics and inhibitors of endogenous integrin function in receptor localization, cell spreading and migration, and matrix assembly. J. Cell Biol. 126 (1994) 1287-1298
    • (1994) J. Cell Biol. , vol.126 , pp. 1287-1298
    • LaFlamme, S.1    Thomas, L.2    Yamada, S.3    Yamada, K.4
  • 37
    • 0019941809 scopus 로고
    • Rapid methods for isolation of human plasma fibronectin
    • Miekka S., Ingham K., and Menache D. Rapid methods for isolation of human plasma fibronectin. Thromb. Res. 27 (1982) 1-14
    • (1982) Thromb. Res. , vol.27 , pp. 1-14
    • Miekka, S.1    Ingham, K.2    Menache, D.3
  • 38
    • 0021979244 scopus 로고
    • The interaction of plasma fibronectin with fibroblastic cells in suspension
    • Akiyama S., and Yamada K. The interaction of plasma fibronectin with fibroblastic cells in suspension. J. Biol. Chem. 260 (1985) 4492-4500
    • (1985) J. Biol. Chem. , vol.260 , pp. 4492-4500
    • Akiyama, S.1    Yamada, K.2
  • 39
    • 0035241616 scopus 로고    scopus 로고
    • Activation of beta1 integrins induces cell-cell adhesion
    • Whittard J., and Akiyama S. Activation of beta1 integrins induces cell-cell adhesion. Exp. Cell Res. 263 (2001) 65-76
    • (2001) Exp. Cell Res. , vol.263 , pp. 65-76
    • Whittard, J.1    Akiyama, S.2
  • 40
    • 0022569858 scopus 로고
    • Characterization of a 140-kD avian cell surface antigen as a fibronectin-binding molecule
    • Akiyama S., Yamada S., and Yamada K. Characterization of a 140-kD avian cell surface antigen as a fibronectin-binding molecule. J. Biol. Chem. 102 (1986) 442-448
    • (1986) J. Biol. Chem. , vol.102 , pp. 442-448
    • Akiyama, S.1    Yamada, S.2    Yamada, K.3
  • 41
    • 0035010472 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase mediates integrin-dependent NF-kappaB and MAPK activation through separate signaling pathways
    • Reyes-Reyes M., Mora N., Zentella A., and Rosales C. Phosphatidylinositol 3-kinase mediates integrin-dependent NF-kappaB and MAPK activation through separate signaling pathways. J. Cell. Sci. 114 (2001) 1579-1589
    • (2001) J. Cell. Sci. , vol.114 , pp. 1579-1589
    • Reyes-Reyes, M.1    Mora, N.2    Zentella, A.3    Rosales, C.4
  • 42
  • 43
    • 0031019073 scopus 로고    scopus 로고
    • Platelets mediate tumor cell adhesion to the subendothelium under flow conditions: involvement of platelet GPIIb-IIIa and tumor cell alpha(v) integrins
    • Dardik R., Kaufmann Y., Savion N., Rosenberg N., Shenkman B., and Varon D. Platelets mediate tumor cell adhesion to the subendothelium under flow conditions: involvement of platelet GPIIb-IIIa and tumor cell alpha(v) integrins. Int. J. Cancer 70 (1997) 201-207
    • (1997) Int. J. Cancer , vol.70 , pp. 201-207
    • Dardik, R.1    Kaufmann, Y.2    Savion, N.3    Rosenberg, N.4    Shenkman, B.5    Varon, D.6
  • 44
    • 0031777293 scopus 로고    scopus 로고
    • Thrombin promotes platelet-mediated melanoma cell adhesion to endothelial cells under flow conditions: role of platelet glycoproteins P-selectin and GPIIb-IIIA
    • Dardik R., Savion N., Kaufmann Y., and Varon D. Thrombin promotes platelet-mediated melanoma cell adhesion to endothelial cells under flow conditions: role of platelet glycoproteins P-selectin and GPIIb-IIIA. Br. J. Cancer 77 (1998) 2069-2075
    • (1998) Br. J. Cancer , vol.77 , pp. 2069-2075
    • Dardik, R.1    Savion, N.2    Kaufmann, Y.3    Varon, D.4
  • 45
    • 0025781381 scopus 로고
    • Effect of platelet activation on the conformation of the plasma membrane glycoprotein IIb-IIIa complex
    • Sims P., Ginsberg M., Plow E., and Shattil S. Effect of platelet activation on the conformation of the plasma membrane glycoprotein IIb-IIIa complex. J. Biol. Chem. 266 (1991) 7345-7352
    • (1991) J. Biol. Chem. , vol.266 , pp. 7345-7352
    • Sims, P.1    Ginsberg, M.2    Plow, E.3    Shattil, S.4
  • 47
    • 15844363687 scopus 로고    scopus 로고
    • Activated conformations of very late activation integrins detected by a group of antibodies (HUTS) specific for a novel regulatory region of the common beta 1 chain
    • Luque A., Gomez M., Puzon W., Takada Y., Sanchez-Madrid F., and Cabanas C. Activated conformations of very late activation integrins detected by a group of antibodies (HUTS) specific for a novel regulatory region of the common beta 1 chain. J. Biol. Chem. 271 (1996) 11067-11075
    • (1996) J. Biol. Chem. , vol.271 , pp. 11067-11075
    • Luque, A.1    Gomez, M.2    Puzon, W.3    Takada, Y.4    Sanchez-Madrid, F.5    Cabanas, C.6
  • 48
    • 0034646651 scopus 로고    scopus 로고
    • Arachidonic acid activates mitogen-activated protein (MAP) kinase-activated protein kinase and mediates adhesion of a human breast carcinoma cell line to collagen type IV through a p38 MAP kinase-dependent pathway
    • Paine E., Palmantier R., Akiyama S., Olden K., and Robert J. Arachidonic acid activates mitogen-activated protein (MAP) kinase-activated protein kinase and mediates adhesion of a human breast carcinoma cell line to collagen type IV through a p38 MAP kinase-dependent pathway. J. Biol. Chem. 275 (2000) 11284-11290
    • (2000) J. Biol. Chem. , vol.275 , pp. 11284-11290
    • Paine, E.1    Palmantier, R.2    Akiyama, S.3    Olden, K.4    Robert, J.5
  • 49
    • 0036221263 scopus 로고    scopus 로고
    • Dysregulation of Met receptor tyrosine kinase activity in invasive tumors
    • Danilkovitch-Miagkova A., and Zbar B. Dysregulation of Met receptor tyrosine kinase activity in invasive tumors. J. Clin. Invest. 109 (2002) 863-867
    • (2002) J. Clin. Invest. , vol.109 , pp. 863-867
    • Danilkovitch-Miagkova, A.1    Zbar, B.2
  • 50
    • 0034004457 scopus 로고    scopus 로고
    • Rap1 is a potent activation signal for leukocyte function-associated antigen 1 distinct from protein kinase C and phosphatidylinositol-3-OH kinase
    • Katagiri K., Hattori M., Minato N., Irie S., Takatsu K., and Kinashi T. Rap1 is a potent activation signal for leukocyte function-associated antigen 1 distinct from protein kinase C and phosphatidylinositol-3-OH kinase. Mol. Cell. Biol. 20 (2000) 1956-1969
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1956-1969
    • Katagiri, K.1    Hattori, M.2    Minato, N.3    Irie, S.4    Takatsu, K.5    Kinashi, T.6
  • 52
    • 0028063478 scopus 로고
    • Mammary carcinoma cell lines of high and low metastatic potential differ not in extravasation but in subsequent migration and growth
    • Morris V., Koop S., MacDonald I., Schmidt E., Grattan M., Percy D., Chambers A., and Groom A. Mammary carcinoma cell lines of high and low metastatic potential differ not in extravasation but in subsequent migration and growth. Clin. Exp. Metastasis 12 (1994) 357-367
    • (1994) Clin. Exp. Metastasis , vol.12 , pp. 357-367
    • Morris, V.1    Koop, S.2    MacDonald, I.3    Schmidt, E.4    Grattan, M.5    Percy, D.6    Chambers, A.7    Groom, A.8
  • 54
    • 0036794592 scopus 로고    scopus 로고
    • Cancer spread and micrometastasis development: quantitative approaches for in vivo models
    • MacDonald I., Groom A., and Chambers A. Cancer spread and micrometastasis development: quantitative approaches for in vivo models. Bioessays 24 (2002) 885-893
    • (2002) Bioessays , vol.24 , pp. 885-893
    • MacDonald, I.1    Groom, A.2    Chambers, A.3
  • 56
    • 0027398098 scopus 로고
    • Contribution of carbohydrate antigens sialyl Lewis A and sialyl Lewis X to adhesion of human cancer cells to vascular endothelium
    • Takada A., Ohmori K., Yoneda T., Tsuyuoka K., Hasegawa A., Kiso M., and Kannagi R. Contribution of carbohydrate antigens sialyl Lewis A and sialyl Lewis X to adhesion of human cancer cells to vascular endothelium. Cancer Res. 53 (1993) 354-361
    • (1993) Cancer Res. , vol.53 , pp. 354-361
    • Takada, A.1    Ohmori, K.2    Yoneda, T.3    Tsuyuoka, K.4    Hasegawa, A.5    Kiso, M.6    Kannagi, R.7
  • 57
    • 0026578078 scopus 로고
    • Endothelial leukocyte adhesion molecule-1-dependent adhesion of colon carcinoma cells to vascular endothelium is inhibited by an anti-body to Lewis fucosylated type I carbohydrate chain
    • Dejana E., Martin-Padura D., Lauri S., Bernasconi M., and Bani A. Endothelial leukocyte adhesion molecule-1-dependent adhesion of colon carcinoma cells to vascular endothelium is inhibited by an anti-body to Lewis fucosylated type I carbohydrate chain. Lab. Invest. 66 (1992) 324-330
    • (1992) Lab. Invest. , vol.66 , pp. 324-330
    • Dejana, E.1    Martin-Padura, D.2    Lauri, S.3    Bernasconi, M.4    Bani, A.5
  • 58
    • 0027197603 scopus 로고
    • Importance of E-selectin (ELAM-1) and sialyl Lewis(a) in the adhesion of pancreatic carcinoma cells to activated endothelium
    • Iwai K., Ishikura H., Kaji M., Sugiura H., Ishizu A., Takahashi C., Kato H., Tanabe T., and Yoshiki T. Importance of E-selectin (ELAM-1) and sialyl Lewis(a) in the adhesion of pancreatic carcinoma cells to activated endothelium. Int. J. Cancer 54 (1993) 972-977
    • (1993) Int. J. Cancer , vol.54 , pp. 972-977
    • Iwai, K.1    Ishikura, H.2    Kaji, M.3    Sugiura, H.4    Ishizu, A.5    Takahashi, C.6    Kato, H.7    Tanabe, T.8    Yoshiki, T.9
  • 59
    • 0035823598 scopus 로고    scopus 로고
    • Transendothelial migration of colon carcinoma cells requires expression of E-selectin by endothelial cells and activation of stress-activated protein kinase-2 (SAPK2/p38) in the tumor cells
    • Laferriere J., Houle F., Taher M., Valerie K., and Huot J. Transendothelial migration of colon carcinoma cells requires expression of E-selectin by endothelial cells and activation of stress-activated protein kinase-2 (SAPK2/p38) in the tumor cells. J. Biol. Chem. 276 (2001) 33762-33772
    • (2001) J. Biol. Chem. , vol.276 , pp. 33762-33772
    • Laferriere, J.1    Houle, F.2    Taher, M.3    Valerie, K.4    Huot, J.5
  • 61
    • 0026553465 scopus 로고
    • Recombinant E-selectin-protein mediates tumor cell adhesion via sialyl-Le(a) and sialyl-Le(x)
    • Majuri M., Mattila P., and Renkonen R. Recombinant E-selectin-protein mediates tumor cell adhesion via sialyl-Le(a) and sialyl-Le(x). Biochem. Biophys. Res. Commun. 182 (1992) 1376-1382
    • (1992) Biochem. Biophys. Res. Commun. , vol.182 , pp. 1376-1382
    • Majuri, M.1    Mattila, P.2    Renkonen, R.3
  • 63
    • 0034834329 scopus 로고    scopus 로고
    • Fibronectin, integrins, and growth control
    • Danen E., and Yamada K. Fibronectin, integrins, and growth control. J. Cell. Physiol. 189 (2001) 1-13
    • (2001) J. Cell. Physiol. , vol.189 , pp. 1-13
    • Danen, E.1    Yamada, K.2
  • 64
    • 0027787824 scopus 로고
    • Differential expression of extracellular matrix proteins and integrins in hepatocellular carcinoma and chronic liver disease
    • Jaskiewicz K., Chasen M., Robson S., Jaskiewicz K., Chasen M.R., and Robson S.C. Differential expression of extracellular matrix proteins and integrins in hepatocellular carcinoma and chronic liver disease. Anticancer Res. 13 (1993) 2229-2237
    • (1993) Anticancer Res. , vol.13 , pp. 2229-2237
    • Jaskiewicz, K.1    Chasen, M.2    Robson, S.3    Jaskiewicz, K.4    Chasen, M.R.5    Robson, S.C.6
  • 66
    • 0028597919 scopus 로고
    • Colorectal cancer and the integrin family of cell adhesion receptors: current status and future directions
    • Agrez M., and Bates R. Colorectal cancer and the integrin family of cell adhesion receptors: current status and future directions. Eur. J. Cancer 30A (1994) 2166-2170
    • (1994) Eur. J. Cancer , vol.30 A , pp. 2166-2170
    • Agrez, M.1    Bates, R.2
  • 67
    • 14944348752 scopus 로고    scopus 로고
    • Transcriptional activation of integrin beta6 during the epithelial-mesenchymal transition defines a novel prognostic indicator of aggressive colon carcinoma
    • Bates R., Bellovin D., Brown C., Maynard E., Wu B., Kawakatsu H., Sheppard D., Oettgen P., and Mercurio A. Transcriptional activation of integrin beta6 during the epithelial-mesenchymal transition defines a novel prognostic indicator of aggressive colon carcinoma. J. Clin. Invest. 115 (2005) 339-347
    • (2005) J. Clin. Invest. , vol.115 , pp. 339-347
    • Bates, R.1    Bellovin, D.2    Brown, C.3    Maynard, E.4    Wu, B.5    Kawakatsu, H.6    Sheppard, D.7    Oettgen, P.8    Mercurio, A.9
  • 68
    • 0026537524 scopus 로고
    • Diminished expression of integrin adhesion molecules on human colonic epithelial cells during the benign to malign tumour transformation
    • Stallmach A., von Lampe B., Matthes H., Bornhoft G., and Riecken E. Diminished expression of integrin adhesion molecules on human colonic epithelial cells during the benign to malign tumour transformation. Gut 33 (1992) 342-346
    • (1992) Gut , vol.33 , pp. 342-346
    • Stallmach, A.1    von Lampe, B.2    Matthes, H.3    Bornhoft, G.4    Riecken, E.5
  • 69
    • 0025073104 scopus 로고
    • Expression of the VLA family of integrins in human intestine.
    • Choy M., Richman P., Horton M., and MacDonald T. Expression of the VLA family of integrins in human intestine. J. Pathol. 160 (1990) 35-40
    • (1990) J. Pathol. , vol.160 , pp. 35-40
    • Choy, M.1    Richman, P.2    Horton, M.3    MacDonald, T.4
  • 70
    • 0025979573 scopus 로고
    • Expression of VLA-alpha 2, VLA-alpha 6, and VLA-beta 1 chains in normal mucosa and adenomas of the colon, and in colon carcinomas and their liver metastases
    • Koretz K., Schlag P., Boumsell L., and Moller P. Expression of VLA-alpha 2, VLA-alpha 6, and VLA-beta 1 chains in normal mucosa and adenomas of the colon, and in colon carcinomas and their liver metastases. Am. J. Pathol. 138 (1991) 741-750
    • (1991) Am. J. Pathol. , vol.138 , pp. 741-750
    • Koretz, K.1    Schlag, P.2    Boumsell, L.3    Moller, P.4
  • 71
    • 0027403283 scopus 로고
    • Interconnection of integrins alpha 2 and alpha 3 and structure of the basal membrane in colorectal cancer: relation to survival
    • Lindmark G., Gerdin B., Pahlman L., Glimelius B., Gehlsen K., and Rubin K. Interconnection of integrins alpha 2 and alpha 3 and structure of the basal membrane in colorectal cancer: relation to survival. Eur. J. Surg. Oncol. 19 (1993) 50-60
    • (1993) Eur. J. Surg. Oncol. , vol.19 , pp. 50-60
    • Lindmark, G.1    Gerdin, B.2    Pahlman, L.3    Glimelius, B.4    Gehlsen, K.5    Rubin, K.6
  • 73
    • 0032518992 scopus 로고    scopus 로고
    • A test of the role of alpha5 integrin/fibronectin interactions in tumorigenesis
    • Taverna D., Ullman-Cullere M., Rayburn H., Bronson R., and Hynes R. A test of the role of alpha5 integrin/fibronectin interactions in tumorigenesis. Cancer Res. 58 (1998) 848-853
    • (1998) Cancer Res. , vol.58 , pp. 848-853
    • Taverna, D.1    Ullman-Cullere, M.2    Rayburn, H.3    Bronson, R.4    Hynes, R.5
  • 74
    • 0031017019 scopus 로고    scopus 로고
    • Role of alpha 5 beta 1 integrin in determining malignant properties of colon carcinoma cells
    • Gong J., Wang D., Sun L., Zborowska E., Willson J., and Brattain M. Role of alpha 5 beta 1 integrin in determining malignant properties of colon carcinoma cells. Cell Growth Differ. 8 (1997) 83-90
    • (1997) Cell Growth Differ. , vol.8 , pp. 83-90
    • Gong, J.1    Wang, D.2    Sun, L.3    Zborowska, E.4    Willson, J.5    Brattain, M.6
  • 75
    • 3843099220 scopus 로고    scopus 로고
    • Inhibition of alpha5 integrin decreases PI3K activation and cell adhesion of human colon cancers
    • Murillo C., Rychahou P., and Evers B. Inhibition of alpha5 integrin decreases PI3K activation and cell adhesion of human colon cancers. Surgery 136 (2004) 143-149
    • (2004) Surgery , vol.136 , pp. 143-149
    • Murillo, C.1    Rychahou, P.2    Evers, B.3
  • 76
    • 0028964699 scopus 로고
    • Inhibition of experimental metastasis of human breast carcinoma cells in athymic nude mice by anti-α5β1 fibronectin receptor integrin antibodies
    • Newton S., Reeves E., Gralnick H., Mohla S., Yamada K., Olden K., and Akiyama S. Inhibition of experimental metastasis of human breast carcinoma cells in athymic nude mice by anti-α5β1 fibronectin receptor integrin antibodies. Int. J. Oncol. 6 (1995) 1063-1070
    • (1995) Int. J. Oncol. , vol.6 , pp. 1063-1070
    • Newton, S.1    Reeves, E.2    Gralnick, H.3    Mohla, S.4    Yamada, K.5    Olden, K.6    Akiyama, S.7
  • 77
    • 0028926451 scopus 로고
    • Activation of human neutrophils through L-selectin and Mac-1 molecules
    • Crockett-Torabi E., Sulenbarger B., Smith C., and Fantone J. Activation of human neutrophils through L-selectin and Mac-1 molecules. J. Immunol. 154 (1995) 2291-2302
    • (1995) J. Immunol. , vol.154 , pp. 2291-2302
    • Crockett-Torabi, E.1    Sulenbarger, B.2    Smith, C.3    Fantone, J.4
  • 78
    • 0029098409 scopus 로고
    • L-selectin (CD62L) cross-linking signals neutrophil adhesive functions via the Mac-1 (CD11b/CD18) beta 2-integrin
    • Simon S., Burns A., Taylor A., Gopalan P., Lynam E., Sklar L., and Smith C. L-selectin (CD62L) cross-linking signals neutrophil adhesive functions via the Mac-1 (CD11b/CD18) beta 2-integrin. J. Immunol. 155 (1995) 1502-1514
    • (1995) J. Immunol. , vol.155 , pp. 1502-1514
    • Simon, S.1    Burns, A.2    Taylor, A.3    Gopalan, P.4    Lynam, E.5    Sklar, L.6    Smith, C.7
  • 79
    • 0034655225 scopus 로고    scopus 로고
    • Neutrophil tethering on E-selectin activates beta 2 integrin binding to ICAM-1 through a mitogen-activated protein kinase signal transduction pathway
    • Simon S., Hu Y., Vestweber D., and Smith C. Neutrophil tethering on E-selectin activates beta 2 integrin binding to ICAM-1 through a mitogen-activated protein kinase signal transduction pathway. J Immunol. 164 (2000) 4348-4358
    • (2000) J Immunol. , vol.164 , pp. 4348-4358
    • Simon, S.1    Hu, Y.2    Vestweber, D.3    Smith, C.4
  • 80
    • 0025819391 scopus 로고
    • Endothelial-leukocyte adhesion molecule 1 stimulates the adhesive activity of leukocyte integrin CR3 (CD11b/CD18, Mac-1, alpha m beta 2) on human neutrophils
    • Lo S., Lee S., Ramos R., Lobb R., Rosa M., Chi-Rosso G., and Wright S. Endothelial-leukocyte adhesion molecule 1 stimulates the adhesive activity of leukocyte integrin CR3 (CD11b/CD18, Mac-1, alpha m beta 2) on human neutrophils. J. Exp. Med. 173 (1991) 1493-1500
    • (1991) J. Exp. Med. , vol.173 , pp. 1493-1500
    • Lo, S.1    Lee, S.2    Ramos, R.3    Lobb, R.4    Rosa, M.5    Chi-Rosso, G.6    Wright, S.7
  • 81
    • 0028895383 scopus 로고
    • Differential roles of PI3-kinase and Kit tyrosine 821 in Kit receptor-mediated proliferation, survival and cell adhesion in mast cells
    • Serve H., Yee N., Stella G., Sepp-Lorenzino L., Tan J., and Besmer P. Differential roles of PI3-kinase and Kit tyrosine 821 in Kit receptor-mediated proliferation, survival and cell adhesion in mast cells. EMBO J. 14 (1995) 473-483
    • (1995) EMBO J. , vol.14 , pp. 473-483
    • Serve, H.1    Yee, N.2    Stella, G.3    Sepp-Lorenzino, L.4    Tan, J.5    Besmer, P.6
  • 82
    • 0033105673 scopus 로고    scopus 로고
    • Affinity modulation of very late antigen-5 through phosphatidylinositol 3-kinase in mast cells
    • Kinashi T., Asaoka T., Setoguchi R., and Takatsu K. Affinity modulation of very late antigen-5 through phosphatidylinositol 3-kinase in mast cells. J Immunol. 162 (1999) 2850-2857
    • (1999) J Immunol. , vol.162 , pp. 2850-2857
    • Kinashi, T.1    Asaoka, T.2    Setoguchi, R.3    Takatsu, K.4
  • 83
    • 0029154701 scopus 로고
    • Receptor tyrosine kinase stimulates cell-matrix adhesion by phosphatidylinositol 3 kinase and phospholipase C-gamma 1 pathways
    • Kinashi T., Escobedo J., Williams L., Takatsu K., and Springer T. Receptor tyrosine kinase stimulates cell-matrix adhesion by phosphatidylinositol 3 kinase and phospholipase C-gamma 1 pathways. Blood 86 (1995) 2086-2090
    • (1995) Blood , vol.86 , pp. 2086-2090
    • Kinashi, T.1    Escobedo, J.2    Williams, L.3    Takatsu, K.4    Springer, T.5
  • 84
    • 33646516014 scopus 로고    scopus 로고
    • MMP-2 mediates ethanol-induced invasion of mammary epithelial cells over-expressing ErbB2
    • Ke Z., Lin H., Fan Z., Cai T., Kaplan R., Ma C., Bower K., Shi X., and Luo J. MMP-2 mediates ethanol-induced invasion of mammary epithelial cells over-expressing ErbB2. Int. J. Cancer 119 (2006) 8-16
    • (2006) Int. J. Cancer , vol.119 , pp. 8-16
    • Ke, Z.1    Lin, H.2    Fan, Z.3    Cai, T.4    Kaplan, R.5    Ma, C.6    Bower, K.7    Shi, X.8    Luo, J.9
  • 85
    • 2442462505 scopus 로고    scopus 로고
    • The possible role of matrix metalloproteinase (MMP)-2 and MMP-9 in cancer, e.g. acute leukemia
    • Klein G., Vellenga E., Fraaije M., Kamps W., and de Bont E. The possible role of matrix metalloproteinase (MMP)-2 and MMP-9 in cancer, e.g. acute leukemia. Crit. Rev. Oncol. Hematol. 50 (2004) 87-100
    • (2004) Crit. Rev. Oncol. Hematol. , vol.50 , pp. 87-100
    • Klein, G.1    Vellenga, E.2    Fraaije, M.3    Kamps, W.4    de Bont, E.5
  • 86
    • 25844467656 scopus 로고    scopus 로고
    • c-Src regulates constitutive and EGF-mediated VEGF expression in pancreatic tumor cells through activation of phosphatidyl inositol-3 kinase and p38 MAPK
    • Summy J., Trevino J., Baker C., and Gallick G. c-Src regulates constitutive and EGF-mediated VEGF expression in pancreatic tumor cells through activation of phosphatidyl inositol-3 kinase and p38 MAPK. Pancreas 31 (2005) 263-274
    • (2005) Pancreas , vol.31 , pp. 263-274
    • Summy, J.1    Trevino, J.2    Baker, C.3    Gallick, G.4
  • 87
    • 0842311598 scopus 로고    scopus 로고
    • Hypoxia-induced activation of p38 mitogen-activated protein kinase and phosphatidylinositol 3′-kinase signaling pathways contributes to expression of interleukin 8 in human ovarian carcinoma cells
    • Xu L., Pathak P., and Fukumura D. Hypoxia-induced activation of p38 mitogen-activated protein kinase and phosphatidylinositol 3′-kinase signaling pathways contributes to expression of interleukin 8 in human ovarian carcinoma cells. Clin. Cancer Res. 10 (2004) 701-707
    • (2004) Clin. Cancer Res. , vol.10 , pp. 701-707
    • Xu, L.1    Pathak, P.2    Fukumura, D.3
  • 88
    • 0035819050 scopus 로고    scopus 로고
    • Multiple signaling pathways involved in activation of matrix metalloproteinase-9 (MMP-9) by heregulin-beta1 in human breast cancer cells
    • Yao J., Xiong S., Klos K., Nguyen N., Grijalva R., Li P., and Yu D. Multiple signaling pathways involved in activation of matrix metalloproteinase-9 (MMP-9) by heregulin-beta1 in human breast cancer cells. Oncogene 20 (2001) 8066-8074
    • (2001) Oncogene , vol.20 , pp. 8066-8074
    • Yao, J.1    Xiong, S.2    Klos, K.3    Nguyen, N.4    Grijalva, R.5    Li, P.6    Yu, D.7
  • 89
    • 25844465843 scopus 로고    scopus 로고
    • Multiple signaling pathways are activated during insulin-like growth factor-I (IGF-I) stimulated breast cancer cell migration
    • Zhang X., Lin M., van Golen K., Yoshioka K., Itoh K., and Yee D. Multiple signaling pathways are activated during insulin-like growth factor-I (IGF-I) stimulated breast cancer cell migration. Breast Cancer Res. Treat. 93 (2005) 159-168
    • (2005) Breast Cancer Res. Treat. , vol.93 , pp. 159-168
    • Zhang, X.1    Lin, M.2    van Golen, K.3    Yoshioka, K.4    Itoh, K.5    Yee, D.6
  • 91
    • 27744496768 scopus 로고    scopus 로고
    • The biology of p38 kinase: a central role in inflammation
    • Schieven G. The biology of p38 kinase: a central role in inflammation. Curr. Top Med. Chem. 5 (2005) 921-928
    • (2005) Curr. Top Med. Chem. , vol.5 , pp. 921-928
    • Schieven, G.1
  • 92
    • 15044338824 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase in disease: timing, location, and scaffolding
    • Wymann M., and Marone R. Phosphoinositide 3-kinase in disease: timing, location, and scaffolding. Curr. Opin. Cell Biol. 17 (2005) 141-149
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 141-149
    • Wymann, M.1    Marone, R.2
  • 93
    • 0032497832 scopus 로고    scopus 로고
    • Structure and function of phosphoinositide 3-kinases
    • Wymann M., and Pirola L. Structure and function of phosphoinositide 3-kinases. Biochim. Biophys. Acta 1436 (1998) 127-150
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 127-150
    • Wymann, M.1    Pirola, L.2
  • 94
    • 0028675698 scopus 로고
    • NMR structure of the N-terminal SH3 domain of GRB2 and its complex with a proline-rich peptide from Sos
    • Goudreau N., Cornille F., Duchesne M., Parker F., Tocque B., Garbay C., and Roques B. NMR structure of the N-terminal SH3 domain of GRB2 and its complex with a proline-rich peptide from Sos. Nat. Struct. Biol. 1 (1994) 898-907
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 898-907
    • Goudreau, N.1    Cornille, F.2    Duchesne, M.3    Parker, F.4    Tocque, B.5    Garbay, C.6    Roques, B.7
  • 95
    • 0035890056 scopus 로고    scopus 로고
    • ShcA and Grb2 mediate polyoma middle T antigen-induced endothelial transformation and Gab1 tyrosine phosphorylation
    • Ong S., Dilworth S., Hauck-Schmalenberger I., Pawson T., and Kiefer F. ShcA and Grb2 mediate polyoma middle T antigen-induced endothelial transformation and Gab1 tyrosine phosphorylation. EMBO J. 20 (2001) 6327-6336
    • (2001) EMBO J. , vol.20 , pp. 6327-6336
    • Ong, S.1    Dilworth, S.2    Hauck-Schmalenberger, I.3    Pawson, T.4    Kiefer, F.5
  • 96
    • 0035875975 scopus 로고    scopus 로고
    • Differential regulation of cell migration and cell cycle progression by FAK complexes with Src, PI3K, Grb7 and Grb2 in focal contacts
    • Shen T., and Guan J. Differential regulation of cell migration and cell cycle progression by FAK complexes with Src, PI3K, Grb7 and Grb2 in focal contacts. FEBS Lett. 499 (2001) 176-181
    • (2001) FEBS Lett. , vol.499 , pp. 176-181
    • Shen, T.1    Guan, J.2
  • 97
    • 0035229933 scopus 로고    scopus 로고
    • Disruption of T cell signaling networks and development by Grb2 haploid insufficiency
    • Gong Q., Cheng A., Akk A., Alberola-Ila J., Gong G., Pawson T., and Chan A. Disruption of T cell signaling networks and development by Grb2 haploid insufficiency. Nat. Immunol. 2 (2001) 29-36
    • (2001) Nat. Immunol. , vol.2 , pp. 29-36
    • Gong, Q.1    Cheng, A.2    Akk, A.3    Alberola-Ila, J.4    Gong, G.5    Pawson, T.6    Chan, A.7
  • 98
    • 4644373631 scopus 로고    scopus 로고
    • Insulin receptor substrate-1/SHP-2 interaction, a phenotype-dependent switching machinery of insulin-like growth factor-I signaling in vascular smooth muscle cells
    • Hayashi K., Shibata K., Morita T., Iwasaki K., Watanabe M., and Sobue K. Insulin receptor substrate-1/SHP-2 interaction, a phenotype-dependent switching machinery of insulin-like growth factor-I signaling in vascular smooth muscle cells. J. Biol. Chem. 279 (2004) 40807-40818
    • (2004) J. Biol. Chem. , vol.279 , pp. 40807-40818
    • Hayashi, K.1    Shibata, K.2    Morita, T.3    Iwasaki, K.4    Watanabe, M.5    Sobue, K.6
  • 99
    • 2342418250 scopus 로고    scopus 로고
    • Gab1 contributes to cytoskeletal reorganization and chemotaxis in response to platelet-derived growth factor
    • Kallin A., Demoulin J., Nishida K., Hirano T., Ronnstrand L., and Heldin C. Gab1 contributes to cytoskeletal reorganization and chemotaxis in response to platelet-derived growth factor. J. Biol. Chem. 279 (2004) 17897-17904
    • (2004) J. Biol. Chem. , vol.279 , pp. 17897-17904
    • Kallin, A.1    Demoulin, J.2    Nishida, K.3    Hirano, T.4    Ronnstrand, L.5    Heldin, C.6
  • 100
    • 16444380748 scopus 로고    scopus 로고
    • Cooperation and selectivity of the two Grb2 binding sites of p52Shc in T-cell antigen receptor signaling to Ras family GTPases and Myc-dependent survival
    • Patrussi L., Savino M., Pellegrini M., Paccani S., Migliaccio E., Plyte S., Lanfrancone L., Pelicci P., and Baldari C. Cooperation and selectivity of the two Grb2 binding sites of p52Shc in T-cell antigen receptor signaling to Ras family GTPases and Myc-dependent survival. Oncogene 24 (2005) 2218-2228
    • (2005) Oncogene , vol.24 , pp. 2218-2228
    • Patrussi, L.1    Savino, M.2    Pellegrini, M.3    Paccani, S.4    Migliaccio, E.5    Plyte, S.6    Lanfrancone, L.7    Pelicci, P.8    Baldari, C.9
  • 102
    • 3042724643 scopus 로고    scopus 로고
    • Dominant negative 14-3-3 promotes cardiomyocyte apoptosis in early stage of type I diabetes mellitus through activation of JNK
    • Gurusamy N., Watanabe K., Ma M., Zhang S., Muslin A., Kodama M., and Aizawa Y. Dominant negative 14-3-3 promotes cardiomyocyte apoptosis in early stage of type I diabetes mellitus through activation of JNK. Biochem. Biophys. Res. Commun. 320 (2004) 773-780
    • (2004) Biochem. Biophys. Res. Commun. , vol.320 , pp. 773-780
    • Gurusamy, N.1    Watanabe, K.2    Ma, M.3    Zhang, S.4    Muslin, A.5    Kodama, M.6    Aizawa, Y.7
  • 103
    • 0042679580 scopus 로고    scopus 로고
    • The MSP receptor regulates alpha6beta4 and alpha3beta1 integrins via 14-3-3 proteins in keratinocyte migration
    • Santoro M., Gaudino G., and Marchisio P. The MSP receptor regulates alpha6beta4 and alpha3beta1 integrins via 14-3-3 proteins in keratinocyte migration. Dev. Cell 5 (2003) 257-271
    • (2003) Dev. Cell , vol.5 , pp. 257-271
    • Santoro, M.1    Gaudino, G.2    Marchisio, P.3
  • 104
    • 0344011971 scopus 로고    scopus 로고
    • Role of 14-3-3-mediated p38 mitogen-activated protein kinase inhibition in cardiac myocyte survival
    • Zhang S., Ren J., Zhang C., Treskov I., Wang Y., and Muslin A. Role of 14-3-3-mediated p38 mitogen-activated protein kinase inhibition in cardiac myocyte survival. Circ. Res. 93 (2003) 1026-1028
    • (2003) Circ. Res. , vol.93 , pp. 1026-1028
    • Zhang, S.1    Ren, J.2    Zhang, C.3    Treskov, I.4    Wang, Y.5    Muslin, A.6
  • 105
    • 0031594188 scopus 로고    scopus 로고
    • 14-3-3beta protein associates with insulin receptor substrate 1 and decreases insulin-stimulated phosphatidylinositol 3′-kinase activity in 3T3L1 adipocytes
    • Kosaki A., Yamada K., Suga J., Otaka A., and Kuzuya H. 14-3-3beta protein associates with insulin receptor substrate 1 and decreases insulin-stimulated phosphatidylinositol 3′-kinase activity in 3T3L1 adipocytes. J. Biol. Chem. 273 (1998) 940-944
    • (1998) J. Biol. Chem. , vol.273 , pp. 940-944
    • Kosaki, A.1    Yamada, K.2    Suga, J.3    Otaka, A.4    Kuzuya, H.5
  • 106
    • 0036192152 scopus 로고    scopus 로고
    • 14-3-3 facilitates insulin-stimulated intracellular trafficking of insulin receptor substrate 1
    • Xiang X., Yuan M., Song Y., Ruderman N., Wen R., and Luo Z. 14-3-3 facilitates insulin-stimulated intracellular trafficking of insulin receptor substrate 1. Mol. Endocrinol. 16 (2002) 552-562
    • (2002) Mol. Endocrinol. , vol.16 , pp. 552-562
    • Xiang, X.1    Yuan, M.2    Song, Y.3    Ruderman, N.4    Wen, R.5    Luo, Z.6
  • 108
    • 0028168082 scopus 로고
    • P-selectin interacts with a beta 2-integrin to enhance phagocytosis
    • Cooper D., Butcher C., Berndt M., and Vadas M. P-selectin interacts with a beta 2-integrin to enhance phagocytosis. J. Immunol. 153 (1994) 3199-3209
    • (1994) J. Immunol. , vol.153 , pp. 3199-3209
    • Cooper, D.1    Butcher, C.2    Berndt, M.3    Vadas, M.4
  • 109
  • 111
    • 0028839989 scopus 로고
    • E-selectin-mediated dynamic interactions of breast- and colon-cancer cells with endothelial-cell monolayers
    • Tozeren A., Kleinman H., Grant D., Morales D., Mercurio A., and Byers S. E-selectin-mediated dynamic interactions of breast- and colon-cancer cells with endothelial-cell monolayers. Int. J. Cancer 60 (1995) 426-431
    • (1995) Int. J. Cancer , vol.60 , pp. 426-431
    • Tozeren, A.1    Kleinman, H.2    Grant, D.3    Morales, D.4    Mercurio, A.5    Byers, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.