메뉴 건너뛰기




Volumn 4, Issue 4, 1999, Pages 367-376

Integrin Function in Breast Carcinoma Progression

Author keywords

Breast carcinoma; Extracellular matrix; Integrin receptors; Invasion; Phosphoinositide 3 OH kinase

Indexed keywords

INTEGRIN;

EID: 0033201938     PISSN: 10833021     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1018766317055     Document Type: Article
Times cited : (52)

References (70)
  • 1
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • R. O. Hynes (1992). Integrins: versatility, modulation, and signaling in cell adhesion. Cell 69:11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 2
    • 17344362877 scopus 로고    scopus 로고
    • Signaling by integrin receptors
    • C. C. Kumar (1998). Signaling by integrin receptors. Oncogene 17:1365-1373.
    • (1998) Oncogene , vol.17 , pp. 1365-1373
    • Kumar, C.C.1
  • 3
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • E. A. Clark and J. S. Brugge (1995). Integrins and signal transduction pathways: The road taken. Science 268:233-239.
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 4
    • 0032189153 scopus 로고    scopus 로고
    • Integrins take partners: Cross-talk between integrins and other membrane receptors
    • J. C. Porter and N. Hogg (1998). Integrins take partners: Cross-talk between integrins and other membrane receptors. Trends in Cell Biol. 8:390-396.
    • (1998) Trends in Cell Biol. , vol.8 , pp. 390-396
    • Porter, J.C.1    Hogg, N.2
  • 5
    • 0027413896 scopus 로고
    • Signaling by integrins: Implications for tumorigenesis
    • M. A. Schwartz (1993). Signaling by integrins: Implications for tumorigenesis. Cancer Res. 53:1503-1506.
    • (1993) Cancer Res. , vol.53 , pp. 1503-1506
    • Schwartz, M.A.1
  • 6
    • 0027682591 scopus 로고
    • Adhesion molecules in cancer: The role of integrins
    • R. L. Juliano and J. A. Varner (1993). Adhesion molecules in cancer: The role of integrins. Curr. Opin. Cell Biol. 5:812-818.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 812-818
    • Juliano, R.L.1    Varner, J.A.2
  • 7
    • 0025688587 scopus 로고
    • Extracellular matrix proteins and their receptors in the normal, hyperplastic and neoplastic breast
    • V. E. Gould, G. K. Koukoulis, and I. Virtanen (1990). Extracellular matrix proteins and their receptors in the normal, hyperplastic and neoplastic breast. Cell Differ. Dev. 32:409-416.
    • (1990) Cell Differ. Dev. , vol.32 , pp. 409-416
    • Gould, V.E.1    Koukoulis, G.K.2    Virtanen, I.3
  • 8
    • 0026040340 scopus 로고
    • Immunohistochemical localization of integrins in the normal, hyperplastic, and neoplastic breast. Correlations with their functions as receptors and cell adhesion molecules
    • G. K. Koukoulis, I. Virtanen, M. Korhonen, L. Laitinen, V. Quaranta, and V. E. Gould (1991). Immunohistochemical localization of integrins in the normal, hyperplastic, and neoplastic breast. Correlations with their functions as receptors and cell adhesion molecules. Am. J. Pathol. 139:787-799.
    • (1991) Am. J. Pathol. , vol.139 , pp. 787-799
    • Koukoulis, G.K.1    Virtanen, I.2    Korhonen, M.3    Laitinen, L.4    Quaranta, V.5    Gould, V.E.6
  • 9
    • 0026644051 scopus 로고
    • Integrins and their accessory adhesion molecules in mammary carcinomas: Loss of polarization in poorly differentiated tumors
    • M. Pignatelli, M. R. Cardillo, A. Hanby, and G. W. Stamp (1992). Integrins and their accessory adhesion molecules in mammary carcinomas: Loss of polarization in poorly differentiated tumors. Human Pathol. 23:1159-1166.
    • (1992) Human Pathol. , vol.23 , pp. 1159-1166
    • Pignatelli, M.1    Cardillo, M.R.2    Hanby, A.3    Stamp, G.W.4
  • 10
    • 0025037292 scopus 로고
    • Decreased expression of integrin adhesive protein receptors in adenocarcinoma of the breast
    • M. M. Zutter, G. Mazoujian, and S. A. Santoro (1990). Decreased expression of integrin adhesive protein receptors in adenocarcinoma of the breast. Am. J. Pathol. 137:863-870.
    • (1990) Am. J. Pathol. , vol.137 , pp. 863-870
    • Zutter, M.M.1    Mazoujian, G.2    Santoro, S.A.3
  • 11
    • 0028864468 scopus 로고
    • Myoepithelial cell differentiation in the developing mammary gland: Progressive acquisition of smooth muscle phenotype
    • M. A. Deugnier, E. P. Moiseyeva, J. P. Thiery, and M. Glukhova (1995). Myoepithelial cell differentiation in the developing mammary gland: Progressive acquisition of smooth muscle phenotype. Dev. Dynam. 204:107-117.
    • (1995) Dev. Dynam. , vol.204 , pp. 107-117
    • Deugnier, M.A.1    Moiseyeva, E.P.2    Thiery, J.P.3    Glukhova, M.4
  • 12
    • 0024539022 scopus 로고
    • Association of the VLA α6 subunit with a novel protein. A possible alternative to the common VLA β 1 subunit on certain cell lines
    • M. E. Hemler, C. Crouse, and A. Sonnenberg (1989). Association of the VLA α6 subunit with a novel protein. A possible alternative to the common VLA β 1 subunit on certain cell lines. J. Biol. Chem. 264:6529-6535.
    • (1989) J. Biol. Chem. , vol.264 , pp. 6529-6535
    • Hemler, M.E.1    Crouse, C.2    Sonnenberg, A.3
  • 13
    • 0024430105 scopus 로고
    • A novel integrin (α e β 4) from human epithelial cells suggests a fourth family of integrin adhesion receptors
    • S. Kajiji, R. N. Tamura, and V. Quaranta (1989). A novel integrin (α E β 4) from human epithelial cells suggests a fourth family of integrin adhesion receptors. EMBO J. 8:673-680.
    • (1989) EMBO J. , vol.8 , pp. 673-680
    • Kajiji, S.1    Tamura, R.N.2    Quaranta, V.3
  • 14
    • 0024453530 scopus 로고
    • Analysis of the tumor-associated antigen TSP-180. Identity with α 6 β 4 in the integrin superfamily
    • S. J. Kennel, L. J. Foote, R. Falcioni, A. Sonnenberg, C. D. Stringer, C. Crouse, and M. E. Hemler (1989). Analysis of the tumor-associated antigen TSP-180. Identity with α 6 β 4 in the integrin superfamily. J. Biol. Chem. 264:15515-15521.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15515-15521
    • Kennel, S.J.1    Foote, L.J.2    Falcioni, R.3    Sonnenberg, A.4    Stringer, C.D.5    Crouse, C.6    Hemler, M.E.7
  • 15
    • 0030006606 scopus 로고    scopus 로고
    • Desmosomes and hemidesmosomes - Structure and function of molecular components
    • K. J. Green, and J. C. R. Jones (1996). Desmosomes and hemidesmosomes - structure and function of molecular components. FASEB J. 10:871-881.
    • (1996) FASEB J. , vol.10 , pp. 871-881
    • Green, K.J.1    Jones, J.C.R.2
  • 16
    • 0030272476 scopus 로고    scopus 로고
    • Hemidesmosomes - Roles in adhesion, signaling and human diseases
    • L. Borradori and A. Sonnenberg (1996). Hemidesmosomes - Roles in adhesion, signaling and human diseases. Curr. Opin. Cell Biol. 8:647-656.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 647-656
    • Borradori, L.1    Sonnenberg, A.2
  • 17
    • 0028806271 scopus 로고
    • Expression of hemidesmosomes and component proteins is lost by invasive breast cancer cells
    • L. M. Bergstraesser, G. Srinivasan, J. C. Jones, S. Stahl, and S. A. Weitzman (1995). Expression of hemidesmosomes and component proteins is lost by invasive breast cancer cells. Amer. J. Pathol. 147:1823-1839.
    • (1995) Amer. J. Pathol. , vol.147 , pp. 1823-1839
    • Bergstraesser, L.M.1    Srinivasan, G.2    Jones, J.C.3    Stahl, S.4    Weitzman, S.A.5
  • 18
    • 0025928098 scopus 로고
    • Mammary epithelial cells, extracellular matrix, and gene expression
    • C. H. Streuli and M. J. Bissell (1991). Mammary epithelial cells, extracellular matrix, and gene expression. Cancer Treat. Res. 53:365-381.
    • (1991) Cancer Treat. Res. , vol.53 , pp. 365-381
    • Streuli, C.H.1    Bissell, M.J.2
  • 19
    • 0031713433 scopus 로고    scopus 로고
    • Extracellular matrix signaling: Integration of form and function in normal and malignant cells
    • N. Boudreau and M. J. Bissell (1998). Extracellular matrix signaling: Integration of form and function in normal and malignant cells. Curr. Opin. Cell Biol. 10:640-646.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 640-646
    • Boudreau, N.1    Bissell, M.J.2
  • 21
    • 0025786161 scopus 로고
    • Control of mammary epithelial differentiation: Basement membrane induces tissue-specific gene expression in the absence of cell-cell interaction and morphological polarity
    • C. H. Streuli, N. Bailey, and M. J. Bissell (1991). Control of mammary epithelial differentiation: basement membrane induces tissue-specific gene expression in the absence of cell-cell interaction and morphological polarity. J. Cell Biol. 115:1383-1395.
    • (1991) J. Cell Biol. , vol.115 , pp. 1383-1395
    • Streuli, C.H.1    Bailey, N.2    Bissell, M.J.3
  • 22
    • 0029056909 scopus 로고
    • Extracellular matrix regulates whey acidic protein gene expression by suppression of TGF-α in mouse mammary epithelial cells: Studies in culture and in transgenic mice
    • C. Q. Lin, P. J. Dempsey, R. J. Coffey, and M. J. Bissell (1995). Extracellular matrix regulates whey acidic protein gene expression by suppression of TGF-α in mouse mammary epithelial cells: Studies in culture and in transgenic mice. J. Cell Biol. 129:1115-1126.
    • (1995) J. Cell Biol. , vol.129 , pp. 1115-1126
    • Lin, C.Q.1    Dempsey, P.J.2    Coffey, R.J.3    Bissell, M.J.4
  • 25
    • 0032540383 scopus 로고    scopus 로고
    • Regulation of mammary differentiation by extracellular matrix involves protein-tyrosine phosphatases
    • G. M. Edwards, F. H. Wilford, X. Liu, L. Hennighausen, J. Djiane, and C. H. Streuli (1998). Regulation of mammary differentiation by extracellular matrix involves protein-tyrosine phosphatases. J. Biol. Chem. 273:9495-9500.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9495-9500
    • Edwards, G.M.1    Wilford, F.H.2    Liu, X.3    Hennighausen, L.4    Djiane, J.5    Streuli, C.H.6
  • 26
    • 0030933277 scopus 로고    scopus 로고
    • Oncoprotein networks
    • T. Hunter (1997). Oncoprotein networks. Cell 88:333-346.
    • (1997) Cell , vol.88 , pp. 333-346
    • Hunter, T.1
  • 27
    • 0019215188 scopus 로고
    • Ultrastructural analysis in the differential diagnosis of breast tumors. The significance of myoepithelial cells, basal lamina, intracytoplasmic lumina and secretory granules
    • V. E. Gould, W. Jao, and H. Battifora (1980). Ultrastructural analysis in the differential diagnosis of breast tumors. The significance of myoepithelial cells, basal lamina, intracytoplasmic lumina and secretory granules. Pathol. Res. Practice 167:45-70.
    • (1980) Pathol. Res. Practice , vol.167 , pp. 45-70
    • Gould, V.E.1    Jao, W.2    Battifora, H.3
  • 28
    • 0027582308 scopus 로고
    • Distribution of tenascin, cellular fibronectins and integrins in the normal, hyperplastic and neoplastic breast
    • G. K. Koukoulis, A. A. Howeedy, M. Korhonen, I. Virtanen, and V. E. Gould (1993). Distribution of tenascin, cellular fibronectins and integrins in the normal, hyperplastic and neoplastic breast. J. Submicroscopic Cytol. Pathol. 25:285-295.
    • (1993) J. Submicroscopic Cytol. Pathol. , vol.25 , pp. 285-295
    • Koukoulis, G.K.1    Howeedy, A.A.2    Korhonen, M.3    Virtanen, I.4    Gould, V.E.5
  • 29
    • 0027535633 scopus 로고
    • Interaction of integrins α3β1 and α2β1: Potential role in keratinocyte intercellular adhesion
    • B. E. Symington, Y. Takada, and W. G. Carter (1993). Interaction of integrins α3β1 and α2β1: Potential role in keratinocyte intercellular adhesion. J. Cell Biol. 120:523-535.
    • (1993) J. Cell Biol. , vol.120 , pp. 523-535
    • Symington, B.E.1    Takada, Y.2    Carter, W.G.3
  • 30
    • 0027772194 scopus 로고
    • Altered integrin expression in adenocarcinoma of the breast. Analysis by in situ hybridization
    • M. M. Zutter, H. R. Krigman, and S. A. Santoro (1993). Altered integrin expression in adenocarcinoma of the breast. Analysis by in situ hybridization. Am. J. Pathol. 142:1439-1448.
    • (1993) Am. J. Pathol. , vol.142 , pp. 1439-1448
    • Zutter, M.M.1    Krigman, H.R.2    Santoro, S.A.3
  • 31
    • 0028918625 scopus 로고
    • Alteration of collagen-dependent adhesion, motility, and morphogenesis by the expression of antisense α 2 integrin mRNA in mammary cells
    • P. J. Keely, A. M. Fong, M. M. Zutter, and S. A. Santoro (1995). Alteration of collagen-dependent adhesion, motility, and morphogenesis by the expression of antisense α 2 integrin mRNA in mammary cells. J. Cell Sci. 108:595-607.
    • (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
  • 32
    • 0028978457 scopus 로고
    • Re-expression of the α2β1 integrin abrogates the malignant phenotype of breast carcinoma cells
    • M. M. Zutter, S. A. Santoro, W. D. Staatz, and Y. L. Tsung (1995). Re-expression of the α2β1 integrin abrogates the malignant phenotype of breast carcinoma cells. Proc. Natl. Acad. Sci. U.S.A. 92:7411-7415.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 7411-7415
    • Zutter, M.M.1    Santoro, S.A.2    Staatz, W.D.3    Tsung, Y.L.4
  • 33
    • 0032523825 scopus 로고    scopus 로고
    • Downstream events in mammary gland morphogenesis mediated by reexpression of the α2β1 integrin: The role of the α6 and β4 integrin subunits
    • H. Sun, S. A. Santoro, and M. M. Zutter (1998). Downstream events in mammary gland morphogenesis mediated by reexpression of the α2β1 integrin: The role of the α6 and β4 integrin subunits. Cancer Res. 58:2224-2233.
    • (1998) Cancer Res. , vol.58 , pp. 2224-2233
    • Sun, H.1    Santoro, S.A.2    Zutter, M.M.3
  • 34
    • 0027177948 scopus 로고
    • Identification by differential display of α6 integrin as a candidate tumor suppressor gene
    • R. Sager, A. Anisowicz, M. Neveu, P. Liang, and G. Sotiropoulou (1993). Identification by differential display of α6 integrin as a candidate tumor suppressor gene. FASEB J. 7:964-970.
    • (1993) FASEB J. , vol.7 , pp. 964-970
    • Sager, R.1    Anisowicz, A.2    Neveu, M.3    Liang, P.4    Sotiropoulou, G.5
  • 35
    • 0026635875 scopus 로고
    • Changes in expression of α6β4 integrin heterodimer in primary and metastatic breast cancer
    • P. G. Natali, M. R. Nicotra, C. Botti, M. Mottolese, A. Bigotti, and O. Segatto (1992). Changes in expression of α6β4 integrin heterodimer in primary and metastatic breast cancer. Brit. J. Cancer 66:318-322.
    • (1992) Brit. J. Cancer , vol.66 , pp. 318-322
    • Natali, P.G.1    Nicotra, M.R.2    Botti, C.3    Mottolese, M.4    Bigotti, A.5    Segatto, O.6
  • 36
    • 0027383908 scopus 로고
    • Expression of β 1 integrins on tumor cells of invasive ductal breast carcinoma
    • N. Jonjic, K. Lucin, M. Krstulja, Z. Iternicka, and E. Mustac (1993). Expression of β 1 integrins on tumor cells of invasive ductal breast carcinoma. Pathol. Res. Practice 189:979-984.
    • (1993) Pathol. Res. Practice , vol.189 , pp. 979-984
    • Jonjic, N.1    Lucin, K.2    Krstulja, M.3    Iternicka, Z.4    Mustac, E.5
  • 37
    • 0028813315 scopus 로고
    • High expression level of α6 integrin in human breast carcinoma is correlated with reduced survival
    • K. Friedrichs, P. Ruiz, F. Franke, I. Gille, H.-J. Terpe, and B. A. Imhof (1995). High expression level of α6 integrin in human breast carcinoma is correlated with reduced survival. Cancer Res. 55:901-906.
    • (1995) Cancer Res. , vol.55 , pp. 901-906
    • Friedrichs, K.1    Ruiz, P.2    Franke, F.3    Gille, I.4    Terpe, H.-J.5    Imhof, B.A.6
  • 38
    • 0031914189 scopus 로고    scopus 로고
    • Prognostic value of α6β4 integrin expression in breast carcinomas is affected by laminin production from tumor cells
    • E. Tagliabue, C. Ghirelli, P. Squicciarini, P. Aiello, M. I. Colnaghi, and S. Menard (1998). Prognostic value of α6β4 integrin expression in breast carcinomas is affected by laminin production from tumor cells. Clinical Cancer Res. 4:407-410.
    • (1998) Clinical Cancer Res. , vol.4 , pp. 407-410
    • Tagliabue, E.1    Ghirelli, C.2    Squicciarini, P.3    Aiello, P.4    Colnaghi, M.I.5    Menard, S.6
  • 39
    • 0030063313 scopus 로고    scopus 로고
    • Function of the integrin α6β1 in metastatic breast carcinoma cells assessed by expression of a dominant-negative receptor
    • L. M. Shaw, C. Chao, U. M. Wewer, and A. M. Mercurio (1996). Function of the integrin α6β1 in metastatic breast carcinoma cells assessed by expression of a dominant-negative receptor. Cancer Res. 56:959-963.
    • (1996) Cancer Res. , vol.56 , pp. 959-963
    • Shaw, L.M.1    Chao, C.2    Wewer, U.M.3    Mercurio, A.M.4
  • 40
    • 0030695152 scopus 로고    scopus 로고
    • The integrin α 6 β 1 promotes the survival of metastatic human breast carcinoma cells in mice
    • U. M. Wewer, L. M. Shaw, R. Albrechtsen, and A. M. Mercurio (1997). The integrin α 6 β 1 promotes the survival of metastatic human breast carcinoma cells in mice. Am. J. Pathol. 151:1191-1198.
    • (1997) Am. J. Pathol. , vol.151 , pp. 1191-1198
    • Wewer, U.M.1    Shaw, L.M.2    Albrechtsen, R.3    Mercurio, A.M.4
  • 41
    • 0028989179 scopus 로고
    • The role of β 1 integrins in adhesion of two breast carcinoma cell lines to a model endothelium
    • R. D. Bliss, J. A. Kirby, D. A. Browell, and T. W. Lennard (1995). The role of β 1 integrins in adhesion of two breast carcinoma cell lines to a model endothelium. Clin. Exp. Metastasis 13:173-183.
    • (1995) Clin. Exp. Metastasis , vol.13 , pp. 173-183
    • Bliss, R.D.1    Kirby, J.A.2    Browell, D.A.3    Lennard, T.W.4
  • 42
    • 0033594105 scopus 로고    scopus 로고
    • Extracellular matrix regulates apoptosis in mammary epithelium through a control on insulin signaling
    • N. Farrelly, Y.-J. Lee, J. Oliver, C. Dive, and C. H. Streuli (1999). Extracellular matrix regulates apoptosis in mammary epithelium through a control on insulin signaling. J. Cell Biol. 144:1337-1347.
    • (1999) J. Cell Biol. , vol.144 , pp. 1337-1347
    • Farrelly, N.1    Lee, Y.-J.2    Oliver, J.3    Dive, C.4    Streuli, C.H.5
  • 43
    • 0030913673 scopus 로고    scopus 로고
    • Matrix adhesion and Ras transformation both activate a phosphoinositide 3-OH kinase and protein kinase B/Akt cellular survival pathway
    • A. Khwaja, P. Rodriguez-Viciana, S. Wennstrom, P. H. Warne, and J. Downward (1997). Matrix adhesion and Ras transformation both activate a phosphoinositide 3-OH kinase and protein kinase B/Akt cellular survival pathway. EMBO J. 16:2783-2793.
    • (1997) EMBO J. , vol.16 , pp. 2783-2793
    • Khwaja, A.1    Rodriguez-Viciana, P.2    Wennstrom, S.3    Warne, P.H.4    Downward, J.5
  • 46
    • 0031196705 scopus 로고    scopus 로고
    • The IGF-I receptor and cancer
    • R. Baserga, M. Resnicoff, and M. Dews (1997). The IGF-I receptor and cancer. Endocrine 7:99-102.
    • (1997) Endocrine , vol.7 , pp. 99-102
    • Baserga, R.1    Resnicoff, M.2    Dews, M.3
  • 48
    • 0029666420 scopus 로고    scopus 로고
    • β 4 integrin is required for hemidesmosome formation, cell adhesion and cell survival
    • J. Dowling, Q. C. Yu, and E. Fuchs (1996). β 4 integrin is required for hemidesmosome formation, cell adhesion and cell survival. J. Cell Biol. 134:559-572.
    • (1996) J. Cell Biol. , vol.134 , pp. 559-572
    • Dowling, J.1    Yu, Q.C.2    Fuchs, E.3
  • 49
    • 0030325051 scopus 로고    scopus 로고
    • The integrin α 6 β 4 and the biology of carcinoma
    • I. Rabinovitz and A. M. Mercurio (1996). The integrin α 6 β 4 and the biology of carcinoma. Biochem. Cell Biol. 74:811-821.
    • (1996) Biochem. Cell Biol. , vol.74 , pp. 811-821
    • Rabinovitz, I.1    Mercurio, A.M.2
  • 50
    • 0031456065 scopus 로고    scopus 로고
    • Activation of phosphoinositide 3-Oh kinase by the α 6 β 4 integrin promotes carcinoma invasion
    • L. M. Shaw, I. Rabinovitz, H. H. F. Wang, A. Toker, and A. M. Mercurio (1997). Activation of phosphoinositide 3-Oh kinase by the α 6 β 4 integrin promotes carcinoma invasion. Cell 91:949-960.
    • (1997) Cell , vol.91 , pp. 949-960
    • Shaw, L.M.1    Rabinovitz, I.2    Wang, H.H.F.3    Toker, A.4    Mercurio, A.M.5
  • 51
    • 0029661897 scopus 로고    scopus 로고
    • A function for the integrin α 6 β 4 in the invasive properties of colorectal carcinoma cells
    • C. Chao, M. M. Lotz, A. C. Clarke, and A. M. Mercurio (1996). A function for the integrin α 6 β 4 in the invasive properties of colorectal carcinoma cells. Cancer Res. 56:4811-4819.
    • (1996) Cancer Res. , vol.56 , pp. 4811-4819
    • Chao, C.1    Lotz, M.M.2    Clarke, A.C.3    Mercurio, A.M.4
  • 52
    • 0031283128 scopus 로고    scopus 로고
    • The integrin α6β4 functions in carcinoma cell migration on laminin-1 by mediating the formation and stabilization of actin-containing motility structures
    • I. Rabinovitz and A. M. Mercurio (1997). The integrin α6β4 functions in carcinoma cell migration on laminin-1 by mediating the formation and stabilization of actin-containing motility structures. J. Cell Biol. 139:1873-1884.
    • (1997) J. Cell Biol. , vol.139 , pp. 1873-1884
    • Rabinovitz, I.1    Mercurio, A.M.2
  • 53
    • 0029092648 scopus 로고
    • Activation of the p21 pathway of growth arrest and apoptosis by the β4 integrin cytoplasmic domain
    • A. S. Clarke, M. M. Lotz, C. Chao, and A. M. Mercurio (1995). Activation of the p21 pathway of growth arrest and apoptosis by the β4 integrin cytoplasmic domain. J. Biol. Chem. 270:22673-22676.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22673-22676
    • Clarke, A.S.1    Lotz, M.M.2    Chao, C.3    Mercurio, A.M.4
  • 55
    • 0029103231 scopus 로고
    • Systemic gene therapy with p53 reduces growth and metastases of a malignant human breast cancer in nude mice
    • L. A. Lesoon-Wood, W. H. Kim, H. K. Kleinman, B. D. Weintraub, and A. J. Mixson (1995). Systemic gene therapy with p53 reduces growth and metastases of a malignant human breast cancer in nude mice. Human Gene Therapy 6:395-405.
    • (1995) Human Gene Therapy , vol.6 , pp. 395-405
    • Lesoon-Wood, L.A.1    Kim, W.H.2    Kleinman, H.K.3    Weintraub, B.D.4    Mixson, A.J.5
  • 56
    • 0031459917 scopus 로고    scopus 로고
    • Cdc42 and rac1 induce integrin-mediated cell motility and invasiveness through Pi(3)K
    • P. J. Keely, J. K. Westwick, I. P. Whitehead, C. J. Der, and L. V. Parise (1997). Cdc42 and rac1 induce integrin-mediated cell motility and invasiveness through Pi(3)K. Nature 390:632-636.
    • (1997) Nature , vol.390 , pp. 632-636
    • Keely, P.J.1    Westwick, J.K.2    Whitehead, I.P.3    Der, C.J.4    Parise, L.V.5
  • 57
    • 0028961293 scopus 로고
    • Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • C. D. Nobes and A. Hall (1995). Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81:53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 59
    • 0032583205 scopus 로고    scopus 로고
    • Matrix-dependent Tiam1/Rac signaling in epithelial cells promotes either cell-cell adhesion or cell migration and is regulated by phosphatidylinositol 3-kinase
    • E. E. Sander, S. van Delft, J. P. ten Klooster, T. Reid, R. A. van der Kammen, F. Michiels, and J. G. Collard (1998). Matrix-dependent Tiam1/Rac signaling in epithelial cells promotes either cell-cell adhesion or cell migration and is regulated by phosphatidylinositol 3-kinase. J. Cell Biol. 143:1385-1398.
    • (1998) J. Cell Biol. , vol.143 , pp. 1385-1398
    • Sander, E.E.1    Van Delft, S.2    Ten Klooster, J.P.3    Reid, T.4    Van Der Kammen, R.A.5    Michiels, F.6    Collard, J.G.7
  • 61
    • 0027685701 scopus 로고
    • Cadherins in cancer: Implications for invasion and metastasis
    • M. Takeichi (1993). Cadherins in cancer: Implications for invasion and metastasis. Curr. Opin. Cell Biol. 5:806-811.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 806-811
    • Takeichi, M.1
  • 62
    • 0032517857 scopus 로고    scopus 로고
    • Release of cAMP gating by the α6β4 integrin stimulates lamellae formation and the chemotactic migration of invasive carcinoma cells
    • K. L. O'Connor, L. M. Shaw, and A. M. Mercurio (1998). Release of cAMP gating by the α6β4 integrin stimulates lamellae formation and the chemotactic migration of invasive carcinoma cells. J. Cell Biol. 143:1749-1760.
    • (1998) J. Cell Biol. , vol.143 , pp. 1749-1760
    • O'Connor, K.L.1    Shaw, L.M.2    Mercurio, A.M.3
  • 63
    • 0029115343 scopus 로고
    • Signal transduction by the α6β4 integrin: Distinct β4 subunit sites mediate recruitment of Shc/Grb2 and association with the cytoskeleton of hemidesmosomes
    • F. Mainiero, A. Pepe, K. K. Wary, L. Spinardi, M. Mohammadi, J. Schlessinger, and F. G. Giancotti (1995). Signal transduction by the α6β4 integrin: Distinct β4 subunit sites mediate recruitment of Shc/Grb2 and association with the cytoskeleton of hemidesmosomes. EMBO J. 14:4470-4481.
    • (1995) EMBO J. , vol.14 , pp. 4470-4481
    • Mainiero, F.1    Pepe, A.2    Wary, K.K.3    Spinardi, L.4    Mohammadi, M.5    Schlessinger, J.6    Giancotti, F.G.7
  • 64
    • 0028598744 scopus 로고
    • Specificity in recognition of phosphopeptides by src-homology 2 domains
    • L. C. Cantley, and Z. Songyang (1994). Specificity in recognition of phosphopeptides by src-homology 2 domains. J. Cell Sci. Supplement. 18:121-126.
    • (1994) J. Cell Sci. Supplement , vol.18 , pp. 121-126
    • Cantley, L.C.1    Songyang, Z.2
  • 66
    • 0028670125 scopus 로고
    • The biology of erbB-2/ neu/HER-2 and its role in cancer
    • N. E. Hynes and D. F. Stern (1994). The biology of erbB-2/ neu/HER-2 and its role in cancer. Biochim. Biophys. Acta. 1198:165-184.
    • (1994) Biochim. Biophys. Acta , vol.1198 , pp. 165-184
    • Hynes, N.E.1    Stern, D.F.2
  • 68
    • 0030901145 scopus 로고    scopus 로고
    • Insulin-like growth factor receptor cooperates with integrin αvβ5 to promote tumor cell dissemination in vivo
    • P. C. Brooks, R. L. Klemke, S. Schon, J. M. Lewis, M. A. Schwartz, and D. A. Cheresh (1997). Insulin-like growth factor receptor cooperates with integrin αvβ5 to promote tumor cell dissemination in vivo. J. Clin. Invest. 99:1390-1398.
    • (1997) J. Clin. Invest. , vol.99 , pp. 1390-1398
    • Brooks, P.C.1    Klemke, R.L.2    Schon, S.3    Lewis, J.M.4    Schwartz, M.A.5    Cheresh, D.A.6
  • 69
    • 0030028186 scopus 로고    scopus 로고
    • The roles of integrins and extracellular matrix proteins in the insulin-like growth factor I-stimulated chemotaxis of human breast cancer cells
    • M. E. Doerr and J. I. Jones (1996). The roles of integrins and extracellular matrix proteins in the insulin-like growth factor I-stimulated chemotaxis of human breast cancer cells. J. Biol. Chem. 271:2443-2447.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2443-2447
    • Doerr, M.E.1    Jones, J.I.2
  • 70
    • 0032217084 scopus 로고    scopus 로고
    • Reciprocal interactions between β1-integrin and epidermal growth factor receptor in three-dimensional basement membrane breast cultures: A different perspective in epithelial biology
    • F. Wang, V. M. Weaver, O. W. Petersen, C. A. Larabell, S. Dedhar, P. Briand, R. Lupu, and M. J. Bissell (1998). Reciprocal interactions between β1-integrin and epidermal growth factor receptor in three-dimensional basement membrane breast cultures: A different perspective in epithelial biology. Proc. Natl. Acad. Sci. U.S.A. 95:14821-14826.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 14821-14826
    • Wang, F.1    Weaver, V.M.2    Petersen, O.W.3    Larabell, C.A.4    Dedhar, S.5    Briand, P.6    Lupu, R.7    Bissell, M.J.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.