메뉴 건너뛰기




Volumn 57, Issue 17, 1997, Pages 3812-3817

An epitope on VLA-6 (α6β1) integrin involved in migration but not adhesion is required for extravasation of murine melanoma B16F1 cells in liver

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; INTEGRIN; LAMININ; LAMININ RECEPTOR; MATRIX PROTEIN; VERY LATE ACTIVATION ANTIGEN;

EID: 0030828894     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (45)

References (51)
  • 1
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: A physically integrated molecular process
    • Lauffenburger, D. A., and Horwitz, A. F. Cell migration: a physically integrated molecular process. Cell, 84: 359-369, 1996.
    • (1996) Cell , vol.84 , pp. 359-369
    • Lauffenburger, D.A.1    Horwitz, A.F.2
  • 2
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes, R. O. Integrins: versatility, modulation, and signaling in cell adhesion. Cell, 69: 11-25, 1992.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 3
    • 0029740182 scopus 로고    scopus 로고
    • Ligand binding regulates the direct movement of β1 integrins on fibroblasts
    • Felsenfeld, D. P., Choquet, D., and Sheetz, M. P. Ligand binding regulates the direct movement of β1 integrins on fibroblasts. Nature (Lond.), 383: 438-440, 1996.
    • (1996) Nature (Lond.) , vol.383 , pp. 438-440
    • Felsenfeld, D.P.1    Choquet, D.2    Sheetz, M.P.3
  • 5
    • 0027314520 scopus 로고
    • Role of integrin α2β1 (VLA-2) in the migration of human melanoma cells on laminin and type IV collagen
    • Etoh, T., Thomas, L., Pastel-Levy, C., Colvin, R. B., Mihm, M. C. J., and Byers, H. R. Role of integrin α2β1 (VLA-2) in the migration of human melanoma cells on laminin and type IV collagen. J. Invest. Dermatol., 100: 640-647, 1993.
    • (1993) J. Invest. Dermatol. , vol.100 , pp. 640-647
    • Etoh, T.1    Thomas, L.2    Pastel-Levy, C.3    Colvin, R.B.4    Mihm, M.C.J.5    Byers, H.R.6
  • 6
    • 0027227425 scopus 로고
    • Maximal migration of human smooth muscle cells on fibronectin and type IV collagen occurs at an intermediate attachment strength
    • DiMilla, P. A., Stone, J. A., Quinn, J. A., Albelda, S. M., and Lauffenburger, D. A. Maximal migration of human smooth muscle cells on fibronectin and type IV collagen occurs at an intermediate attachment strength. J. Cell Biol., 122: 729-737, 1993.
    • (1993) J. Cell Biol. , vol.122 , pp. 729-737
    • DiMilla, P.A.1    Stone, J.A.2    Quinn, J.A.3    Albelda, S.M.4    Lauffenburger, D.A.5
  • 8
    • 0028918625 scopus 로고
    • Alteration of collagen-dependent adhesion, motility, and morphogenesis by the expression of antisense α2 integrin mRNA in mammary cells
    • Keely, P. J., Fong, A. M., Zutter, M. M., and Santoro, S. A. Alteration of collagen-dependent adhesion, motility, and morphogenesis by the expression of antisense α2 integrin mRNA in mammary cells. J. Cell Sci., 108: 595-607, 1995.
    • (1995) J. Cell Sci. , vol.108 , pp. 595-607
    • Keely, P.J.1    Fong, A.M.2    Zutter, M.M.3    Santoro, S.A.4
  • 9
    • 0029820264 scopus 로고    scopus 로고
    • Modulation of cell migration by integrin-mediated cytoskeletal linkages and ligand-binding affinity
    • Huttenlocher, A., Ginsberg, M. H., and Horwitz, A. F. Modulation of cell migration by integrin-mediated cytoskeletal linkages and ligand-binding affinity. J. Cell Biol., 134: 1551-1562, 1996.
    • (1996) J. Cell Biol. , vol.134 , pp. 1551-1562
    • Huttenlocher, A.1    Ginsberg, M.H.2    Horwitz, A.F.3
  • 11
    • 0027459771 scopus 로고
    • Signal transduction from the extracellular matrix
    • Juliano, R. L., and Haskill, S. Signal transduction from the extracellular matrix. J. Cell Biol., 120: 577-585, 1993.
    • (1993) J. Cell Biol. , vol.120 , pp. 577-585
    • Juliano, R.L.1    Haskill, S.2
  • 12
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Washington DC
    • Clark, E. A., and Brugge, J. S. Integrins and signal transduction pathways: the road taken. Science (Washington DC), 268: 233-239, 1995.
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 15
    • 0028331263 scopus 로고
    • Tyrosine kinase activity, cytoskeletal organization, and motility in human vascular endothelial cells
    • Romer, L. H., McLean, N., Turner, C. E., and Burridge, K. Tyrosine kinase activity, cytoskeletal organization, and motility in human vascular endothelial cells. Mol. Biol. Cell, 5: 349-361, 1994.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 349-361
    • Romer, L.H.1    McLean, N.2    Turner, C.E.3    Burridge, K.4
  • 16
    • 0029741102 scopus 로고    scopus 로고
    • Inhibition of focal adhesion kinase (FAK) signaling in focal adhesion decreases cell motility and proliferation
    • Gilmore, A. P., and Romer, L. H. Inhibition of focal adhesion kinase (FAK) signaling in focal adhesion decreases cell motility and proliferation. Mol. Biol. Cell, 7: 1209-1224, 1996.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1209-1224
    • Gilmore, A.P.1    Romer, L.H.2
  • 17
    • 0029948080 scopus 로고    scopus 로고
    • Stimulation of cell migration by overexpression of focal adhesion kinase and its association with Src and Fyn
    • Cary, L. A., Chang, J. F., and Guan, J-L. Stimulation of cell migration by overexpression of focal adhesion kinase and its association with Src and Fyn. J. Cell Sci., 109: 1787-1794, 1996.
    • (1996) J. Cell Sci. , vol.109 , pp. 1787-1794
    • Cary, L.A.1    Chang, J.F.2    Guan, J.-L.3
  • 19
    • 0027599001 scopus 로고
    • Suppression of mouse melanoma metastasis by EA-1, a monoclonal antibody specific for α6 integrins
    • Ruiz, P., Dunon, D., Sonnenberg, A., and Imhof, B. A. Suppression of mouse melanoma metastasis by EA-1, a monoclonal antibody specific for α6 integrins. Cell Adhesion & Commun., 1: 67-81, 1993.
    • (1993) Cell Adhesion & Commun. , vol.1 , pp. 67-81
    • Ruiz, P.1    Dunon, D.2    Sonnenberg, A.3    Imhof, B.A.4
  • 20
    • 0029969536 scopus 로고    scopus 로고
    • VLA-β1 inlegrin subunit-specific monoclonal antibodies MB1.1 and MB1.2: Binding to epitopes not dependent on thymocyte development or regulated by phorbol ester and divalent cations
    • von Ballestrem, C. G., Uniyal, S., McCormick, J. I., Chau, T., Singh, B., and Chan, B. M. C. VLA-β1 inlegrin subunit-specific monoclonal antibodies MB1.1 and MB1.2: binding to epitopes not dependent on thymocyte development or regulated by phorbol ester and divalent cations. Hybridoma, 15: 125-132, 1996.
    • (1996) Hybridoma , vol.15 , pp. 125-132
    • Von Ballestrem, C.G.1    Uniyal, S.2    McCormick, J.I.3    Chau, T.4    Singh, B.5    Chan, B.M.C.6
  • 21
    • 0029758358 scopus 로고    scopus 로고
    • Integrin VLA-6 (α6β1) mediates adhesion of mouse bone marrow-derived mast cells to laminin
    • Fehlner-Gardiner, C., Uniyal, S., von Ballestrem, C., Dougherty, G. J., and Chan, B. M. C. Integrin VLA-6 (α6β1) mediates adhesion of mouse bone marrow-derived mast cells to laminin. Allergy, 51: 650-656, 1996.
    • (1996) Allergy , vol.51 , pp. 650-656
    • Fehlner-Gardiner, C.1    Uniyal, S.2    Von Ballestrem, C.3    Dougherty, G.J.4    Chan, B.M.C.5
  • 22
    • 0030474667 scopus 로고    scopus 로고
    • Integrin VLA-6 (α6β1) is transiently expressed during the development of mouse bone marrow-derived mast cells
    • Fehlner-Gardiner, C., Uniyal, S., and Chan, B. M. C. Integrin VLA-6 (α6β1) is transiently expressed during the development of mouse bone marrow-derived mast cells. Dev. Growth Differ., 38: 673-686, 1996.
    • (1996) Dev. Growth Differ. , vol.38 , pp. 673-686
    • Fehlner-Gardiner, C.1    Uniyal, S.2    Chan, B.M.C.3
  • 23
    • 0023664709 scopus 로고
    • A complex of platelet glycoproteins Ic and IIa identified by a rat monoclonal antibody
    • Sonnenberg, A., Janssen, H., Hogervorst, F., Calafat, J., and Hilgers, J. A complex of platelet glycoproteins Ic and IIa identified by a rat monoclonal antibody. J. Biol. Chem., 262: 10376-10383, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10376-10383
    • Sonnenberg, A.1    Janssen, H.2    Hogervorst, F.3    Calafat, J.4    Hilgers, J.5
  • 25
    • 0028097582 scopus 로고
    • Complement receptor 3 (CR3, Mac-1, integrin αMβ2, CD11b/CD18) is required for tyrosine pnosphorylation of paxillin in adherent and nonadherent neutrophils
    • Graham, I. L., Anderson, D. C., Holers, M., and Brown, E. J. Complement receptor 3 (CR3, Mac-1, integrin αMβ2, CD11b/CD18) is required for tyrosine pnosphorylation of paxillin in adherent and nonadherent neutrophils. J. Cell Biol., 127: 1139-1147, 1994.
    • (1994) J. Cell Biol. , vol.127 , pp. 1139-1147
    • Graham, I.L.1    Anderson, D.C.2    Holers, M.3    Brown, E.J.4
  • 26
    • 0025946283 scopus 로고
    • Signal transduction by integrins: Increased protein tyrosine phosphorylation caused by clustering of β1 integrins
    • Kornberg, L., Earp, H. S., Turner, C. E., Prockop, C., and Juliano, R. L. Signal transduction by integrins: increased protein tyrosine phosphorylation caused by clustering of β1 integrins. Proc. Natl. Acad. Sci. USA, 88: 8392-8396, 1991.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8392-8396
    • Kornberg, L.1    Earp, H.S.2    Turner, C.E.3    Prockop, C.4    Juliano, R.L.5
  • 27
    • 0029078096 scopus 로고
    • Specialized functional properties of the integrin α4 cytoplasmic domain
    • Kassner, P. D., Alon, R., Springer, T. A., and Hemler, M. E. Specialized functional properties of the integrin α4 cytoplasmic domain. Mol. Biol. Cell., 6: 661-674, 1995.
    • (1995) Mol. Biol. Cell. , vol.6 , pp. 661-674
    • Kassner, P.D.1    Alon, R.2    Springer, T.A.3    Hemler, M.E.4
  • 28
    • 0028356999 scopus 로고
    • Regulation of cellular interactions with laminin by integrin cytoplasmic domains: The A and B structural variants of the α6β1 integrin differentially modulate the adhesive strength, morphology, and migration of macrophages
    • Shaw, L., and Mercurio, A. M. Regulation of cellular interactions with laminin by integrin cytoplasmic domains: the A and B structural variants of the α6β1 integrin differentially modulate the adhesive strength, morphology, and migration of macrophages. Mol. Biol. Cell., 5: 679-690, 1994.
    • (1994) Mol. Biol. Cell. , vol.5 , pp. 679-690
    • Shaw, L.1    Mercurio, A.M.2
  • 29
    • 0026061509 scopus 로고
    • The major laminin receptor of mouse embryonic stem cells is a novel isoform of the α6β1 integrin
    • Cooper, H. M., Tamura, R. N., and Quaranta, V. The major laminin receptor of mouse embryonic stem cells is a novel isoform of the α6β1 integrin. J. Cell Biol., 115: 843-850, 1991.
    • (1991) J. Cell Biol. , vol.115 , pp. 843-850
    • Cooper, H.M.1    Tamura, R.N.2    Quaranta, V.3
  • 30
    • 0025908468 scopus 로고
    • Molecular cloning of the human α6 integrin subunit: Alternative splicing of α6 mRNA and chromosomal localization of the α6 and β4 genes
    • Hogervorst, F., Kuikman, I., van Kessel, A. G., and Sonnenberg, A. Molecular cloning of the human α6 integrin subunit: alternative splicing of α6 mRNA and chromosomal localization of the α6 and β4 genes. Eur. J. Biochem., 199: 425-433, 1991.
    • (1991) Eur. J. Biochem. , vol.199 , pp. 425-433
    • Hogervorst, F.1    Kuikman, I.2    Van Kessel, A.G.3    Sonnenberg, A.4
  • 31
    • 0027371830 scopus 로고
    • Expression and function of the cytoplasmic variants of the integrin α6 subunit in transfected K562 cells
    • Delwel, G. O., Hogervorst, F., Kuikman, I., Paulsson, M., Timpl, R., and Sonnenberg, A. Expression and function of the cytoplasmic variants of the integrin α6 subunit in transfected K562 cells. J. Biol. Chem., 268: 25865-25875, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25865-25875
    • Delwel, G.O.1    Hogervorst, F.2    Kuikman, I.3    Paulsson, M.4    Timpl, R.5    Sonnenberg, A.6
  • 32
    • 0026596337 scopus 로고
    • Distinct cellular functions mediated by different VLA integrin α subunit cytoplasmic domains
    • Chan, B. M. C., Kassner, P. D., Schiro, J. A., Byers, H. R., Kupper, T. S., and Hemler, M. E. Distinct cellular functions mediated by different VLA integrin α subunit cytoplasmic domains. Cell, 68: 1051-1060, 1992.
    • (1992) Cell , vol.68 , pp. 1051-1060
    • Chan, B.M.C.1    Kassner, P.D.2    Schiro, J.A.3    Byers, H.R.4    Kupper, T.S.5    Hemler, M.E.6
  • 34
    • 0029157259 scopus 로고
    • Assembly and function of integrin receptors is dependent on opposing α and β cytoplasmic domains
    • Briesewitz, R., Kern, A., and Marcantonio, E. E. Assembly and function of integrin receptors is dependent on opposing α and β cytoplasmic domains. Mol. Biol. Cell, 6: 997-1010, 1995.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 997-1010
    • Briesewitz, R.1    Kern, A.2    Marcantonio, E.E.3
  • 35
    • 0026512171 scopus 로고
    • A monoclonal antibody to β1 integrin (CD29) stimulates VLA-dependent adherence of leukocytes to human umbilical vein endothelial cells and matrix components
    • Kovach, N. L., Carlos, T. M., Yee, E., and Harlan, J. M. A monoclonal antibody to β1 integrin (CD29) stimulates VLA-dependent adherence of leukocytes to human umbilical vein endothelial cells and matrix components. J. Cell Biol., 116: 499-509, 1992.
    • (1992) J. Cell Biol. , vol.116 , pp. 499-509
    • Kovach, N.L.1    Carlos, T.M.2    Yee, E.3    Harlan, J.M.4
  • 37
    • 0027497502 scopus 로고
    • Multiple functional forms of the integrin VLA-2 derived from a single α2 cDNA clone: Interconversion of forms induced by an anti-β1 antibody
    • Chan, B. M. C., and Hemler, M. E. Multiple functional forms of the integrin VLA-2 derived from a single α2 cDNA clone: interconversion of forms induced by an anti-β1 antibody. J. Cell Biol., 120: 537-543, 1993.
    • (1993) J. Cell Biol. , vol.120 , pp. 537-543
    • Chan, B.M.C.1    Hemler, M.E.2
  • 38
    • 0029758858 scopus 로고    scopus 로고
    • Integrin-associated protein immunoglobulin domain is necessary for efficient vitronectin bead binding
    • Lindberg, F. P., Gresham, H. D., Reinhold, M. I., and Brown, E. J. Integrin-associated protein immunoglobulin domain is necessary for efficient vitronectin bead binding. J. Cell Biol., 134: 1313-1322, 1996.
    • (1996) J. Cell Biol. , vol.134 , pp. 1313-1322
    • Lindberg, F.P.1    Gresham, H.D.2    Reinhold, M.I.3    Brown, E.J.4
  • 39
    • 0030239653 scopus 로고    scopus 로고
    • Transmembrane-4 superfamily proteins CD81 (TAPA-1), CD82, CD63, and CD53 specifically associate with integrin α4β1 (CD49a/CD29)
    • Mannion, B. A., Berditchevski, F., Kraeft, S-K., Chen, L. B., and Hemler, M. E. Transmembrane-4 superfamily proteins CD81 (TAPA-1), CD82, CD63, and CD53 specifically associate with integrin α4β1 (CD49a/CD29). J. Immunol., 157: 2039-2047, 1996.
    • (1996) J. Immunol. , vol.157 , pp. 2039-2047
    • Mannion, B.A.1    Berditchevski, F.2    Kraeft, S.-K.3    Chen, L.B.4    Hemler, M.E.5
  • 40
    • 0029005293 scopus 로고
    • The transendothelial migration of neutrophils involves integrin-associated protein (CD47)
    • Cooper, D., Lindberg, F. P., Ganble, J. R., Brown, E. J., and Vadas, M. A. The transendothelial migration of neutrophils involves integrin-associated protein (CD47). Proc. Natl. Acad. Sci. USA, 92: 3978-3982, 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3978-3982
    • Cooper, D.1    Lindberg, F.P.2    Ganble, J.R.3    Brown, E.J.4    Vadas, M.A.5
  • 41
    • 0030019862 scopus 로고    scopus 로고
    • CD47 mediates post-adhesive events required for neutrophil migration across polarized intestinal epithelia
    • Parkos, C. A., Colgan, S. P., Liang, T. W., Nusrat, A., Bacarra, A. E., Carnes, D. K., and Madara, J. L. CD47 mediates post-adhesive events required for neutrophil migration across polarized intestinal epithelia. J. Cell Biol., 132: 437-450, 1996.
    • (1996) J. Cell Biol. , vol.132 , pp. 437-450
    • Parkos, C.A.1    Colgan, S.P.2    Liang, T.W.3    Nusrat, A.4    Bacarra, A.E.5    Carnes, D.K.6    Madara, J.L.7
  • 42
    • 0025837201 scopus 로고
    • Identification of the motility-related protein (MRP-1), recognized by monoclonal antibody M31-15, which inhibits cell motility
    • Miyake, M., Koyama, M., Seno, M., and Ikeyama, S. Identification of the motility-related protein (MRP-1), recognized by monoclonal antibody M31-15, which inhibits cell motility. J. Exp. Med., 174: 1347-1354, 1991.
    • (1991) J. Exp. Med. , vol.174 , pp. 1347-1354
    • Miyake, M.1    Koyama, M.2    Seno, M.3    Ikeyama, S.4
  • 43
    • 0027406455 scopus 로고
    • Suppression of cell motility and metastasis by transfection with human motility-related protein (MRP-1/CD9) DNA
    • Ikeyama, S., Koyama, M., Yamaoko, M., Sasada, R., and Miyake, M. Suppression of cell motility and metastasis by transfection with human motility-related protein (MRP-1/CD9) DNA. J. Exp. Med., 177: 1231-1237, 1993.
    • (1993) J. Exp. Med. , vol.177 , pp. 1231-1237
    • Ikeyama, S.1    Koyama, M.2    Yamaoko, M.3    Sasada, R.4    Miyake, M.5
  • 45
    • 0027534578 scopus 로고
    • Peptides derived from a sequence within β3 integrin bind to platelet αIIbβ3 (GPIIb-IIIa) and inhibit ligand binding
    • Steiner, B., Trzeciak, A., Pfenninger, G., and Kouns, W. C. Peptides derived from a sequence within β3 integrin bind to platelet αIIbβ3 (GPIIb-IIIa) and inhibit ligand binding. J. Biol. Chem., 268: 6870-6873, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6870-6873
    • Steiner, B.1    Trzeciak, A.2    Pfenninger, G.3    Kouns, W.C.4
  • 46
    • 0025216612 scopus 로고
    • The ligand binding site of the platelet integrin receptor GPIIb-IIIa is proximal to the second calcium binding domain of its α subunit
    • D'Souza, S. E., Ginsberg, M. H., Burke, T. A., and Plow, E. F. The ligand binding site of the platelet integrin receptor GPIIb-IIIa is proximal to the second calcium binding domain of its α subunit. J. Biol. Chem., 265: 3440-3446, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3440-3446
    • D'Souza, S.E.1    Ginsberg, M.H.2    Burke, T.A.3    Plow, E.F.4
  • 47
    • 0026625737 scopus 로고
    • Localization of the cross-linking sites of RGD and KQAGDV peptides to the isolated fibrinogen receptor, the human platelet integrin glycoprotein IIb/IIIa: Influence of peptide length
    • Calvete, J. J., Schafer, W., Mann, K., Henschen, A., and Gonzalez-Rodriguez, J. Localization of the cross-linking sites of RGD and KQAGDV peptides to the isolated fibrinogen receptor, the human platelet integrin glycoprotein IIb/IIIa: influence of peptide length. Eur. J. Biochem., 206: 759-765, 1992.
    • (1992) Eur. J. Biochem. , vol.206 , pp. 759-765
    • Calvete, J.J.1    Schafer, W.2    Mann, K.3    Henschen, A.4    Gonzalez-Rodriguez, J.5
  • 49
    • 0028179102 scopus 로고
    • Involvement of very late activation antigen 4 (VLA-4) and vascular cell adhesion molecule-1 (VCAM-1) in tumor necrosis factor α enhancement of experimental metastasis
    • Okahara, H., Yagita, H., Miyake, K., and Okumura, K. Involvement of very late activation antigen 4 (VLA-4) and vascular cell adhesion molecule-1 (VCAM-1) in tumor necrosis factor α enhancement of experimental metastasis. Cancer Res., 54: 3233-3236, 1994.
    • (1994) Cancer Res. , vol.54 , pp. 3233-3236
    • Okahara, H.1    Yagita, H.2    Miyake, K.3    Okumura, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.