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Volumn 20, Issue 9, 2006, Pages

Maspin is physically associated with β1 integrin regulating cell adhesion in mammary epithelial cells

Author keywords

1 integrin; Cell adhesion; ECM; Maspin; RSL

Indexed keywords

BETA1 INTEGRIN; CYTOSKELETON PROTEIN; MASPIN; TRITON X 100; PRIMER DNA; RECOMBINANT PROTEIN; SERINE PROTEINASE INHIBITOR;

EID: 33845608469     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fj.05-5500fje     Document Type: Article
Times cited : (61)

References (47)
  • 2
    • 0028208912 scopus 로고
    • Maspin, a serpin with tumor-suppressing activity in human mammary epithelial cells
    • [see comments]
    • Zou, Z., Anisowicz, A., Hendrix, M. J., Thor, A., Neveu, M., Sheng, S., Rafidi, K., Seftor, E., and Sager, R. (1994) Maspin, a serpin with tumor-suppressing activity in human mammary epithelial cells [see comments]. Science 263, 526-529
    • (1994) Science , vol.263 , pp. 526-529
    • Zou, Z.1    Anisowicz, A.2    Hendrix, M.J.3    Thor, A.4    Neveu, M.5    Sheng, S.6    Rafidi, K.7    Seftor, E.8    Sager, R.9
  • 3
    • 0035884506 scopus 로고    scopus 로고
    • Blocking tumor growth, invasion, and metastasis by maspin in a syngeneic breast cancer model
    • Shi, H. Y., Zhang, W., Liang, R., Abraham, S., Kittrell, F. S., Medina, D., and Zhang, M. (2001) Blocking tumor growth, invasion, and metastasis by maspin in a syngeneic breast cancer model. Cancer Res. 61, 6945-6951
    • (2001) Cancer Res. , vol.61 , pp. 6945-6951
    • Shi, H.Y.1    Zhang, W.2    Liang, R.3    Abraham, S.4    Kittrell, F.S.5    Medina, D.6    Zhang, M.7
  • 5
    • 0033974302 scopus 로고    scopus 로고
    • Maspin is an angiogenesis inhibitor
    • Zhang, M., Volpert, O., Shi, Y. H., and Bouck, N. (2000) Maspin is an angiogenesis inhibitor. Nat. Med. 6, 196-199
    • (2000) Nat. Med. , vol.6 , pp. 196-199
    • Zhang, M.1    Volpert, O.2    Shi, Y.H.3    Bouck, N.4
  • 6
    • 0037362833 scopus 로고    scopus 로고
    • Maspin functions as tumor suppressor by increasing cell adhesion to extracellular matrix in prostate tumor cells
    • Abraham, S., Zhang, W., Greenberg, N., and Zhang, M. (2003) Maspin functions as tumor suppressor by increasing cell adhesion to extracellular matrix in prostate tumor cells. J. Urol. 169, 1157-1161
    • (2003) J. Urol. , vol.169 , pp. 1157-1161
    • Abraham, S.1    Zhang, W.2    Greenberg, N.3    Zhang, M.4
  • 7
    • 0041856173 scopus 로고    scopus 로고
    • Sufficiency of the reactive site loop of maspin for Induction of cell-matrix adhesion and inhibition of cell Invasion: Conversion of ovalbumin to a maspin-like molecule
    • Ngamkitidechakul, C., Warejcka, D. J., Burke, J. M., O'Brien, W. J., and Twining, S. S. (2003) Sufficiency of the reactive site loop of maspin for Induction of cell-matrix adhesion and inhibition of cell Invasion: Conversion of ovalbumin to a maspin-like molecule. J. Biol. Chem.
    • (2003) J. Biol. Chem.
    • Ngamkitidechakul, C.1    Warejcka, D.J.2    Burke, J.M.3    O'Brien, W.J.4    Twining, S.S.5
  • 8
    • 0034282726 scopus 로고    scopus 로고
    • The surface of prostate carcinoma DU145 cells mediates the inhibition of urokinase-type plasminogen activator by maspin
    • McGowen, R., Biliran, H., Jr., Sager, R., and Sheng, S. (2000) The surface of prostate carcinoma DU145 cells mediates the inhibition of urokinase-type plasminogen activator by maspin. Cancer Res. 60, 4771-4778
    • (2000) Cancer Res. , vol.60 , pp. 4771-4778
    • McGowen, R.1    Biliran Jr., H.2    Sager, R.3    Sheng, S.4
  • 9
    • 0035893565 scopus 로고    scopus 로고
    • Pleiotrophic inhibition of pericellular urokinase-type plasminogen activator system by endogenous tumor suppressive maspin
    • Biliran, H., Jr., and Sheng, S. (2001) Pleiotrophic inhibition of pericellular urokinase-type plasminogen activator system by endogenous tumor suppressive maspin. Cancer Res. 61, 8676-8682
    • (2001) Cancer Res. , vol.61 , pp. 8676-8682
    • Biliran Jr., H.1    Sheng, S.2
  • 10
    • 0029058971 scopus 로고
    • The tumor suppressor maspin does not undergo the stressed to relaxed transition or inhibit trypsin-like serine proteases. Evidence that maspin is not a protease inhibitory serpin
    • Pemberton, P. A., Wong, D. T., Gibson, H. L., Kiefer, M. C., Fitzpatrick, P. A., Sager, R., and Barr, P. J. (1995) The tumor suppressor maspin does not undergo the stressed to relaxed transition or inhibit trypsin-like serine proteases. Evidence that maspin is not a protease inhibitory serpin. J. Biol. Chem. 270, 15832-15837
    • (1995) J. Biol. Chem. , vol.270 , pp. 15832-15837
    • Pemberton, P.A.1    Wong, D.T.2    Gibson, H.L.3    Kiefer, M.C.4    Fitzpatrick, P.A.5    Sager, R.6    Barr, P.J.7
  • 11
    • 0037032993 scopus 로고    scopus 로고
    • Maspin inhibits cell migration in the absence of protease inhibitory activity
    • Bass, R., Fernandez, A. M., and Ellis, V. (2002) Maspin inhibits cell migration in the absence of protease inhibitory activity. J. Biol. Chem. 277, 46845-46848
    • (2002) J. Biol. Chem. , vol.277 , pp. 46845-46848
    • Bass, R.1    Fernandez, A.M.2    Ellis, V.3
  • 13
    • 14044269508 scopus 로고    scopus 로고
    • Maspin mediates increased tumor cell apoptosis upon induction of the mitochondrial permeability transition
    • Latha, K., Zhang, W., Cella, N., Shi, H. Y., and Zhang, M. (2005) Maspin mediates increased tumor cell apoptosis upon induction of the mitochondrial permeability transition. Mol. Cell. Biol. 25, 1737-1748
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 1737-1748
    • Latha, K.1    Zhang, W.2    Cella, N.3    Shi, H.Y.4    Zhang, M.5
  • 15
    • 0027242415 scopus 로고
    • The matrix secreted by 804G cells contains laminin-related components that participate in hemidesmosome assembly in vitro. J
    • Langhofer, M., Hopkinson, S. B., and Jones, J. C. (1993) The matrix secreted by 804G cells contains laminin-related components that participate in hemidesmosome assembly in vitro. J. Cell Sci. 105(Pt 3), 753-764
    • (1993) Cell Sci. , vol.105 , Issue.PART 3 , pp. 753-764
    • Langhofer, M.1    Hopkinson, S.B.2    Jones, J.C.3
  • 16
    • 0034638829 scopus 로고    scopus 로고
    • Induction of terminal differentiation in epithelial cells requires polymerization of hensin by galectin 3
    • Hikita, C., Vijayakumar, S., Takito, J., Erdjument-Bromage, H., Tempst, P., and Al-Awqati, Q. (2000) Induction of terminal differentiation in epithelial cells requires polymerization of hensin by galectin 3. J. Cell Biol. 151, 1235-1246
    • (2000) J. Cell Biol. , vol.151 , pp. 1235-1246
    • Hikita, C.1    Vijayakumar, S.2    Takito, J.3    Erdjument-Bromage, H.4    Tempst, P.5    Al-Awqati, Q.6
  • 17
    • 0027104001 scopus 로고
    • Dynamics of three-dimensional replication patterns during the S-phase, analysed by double labelling of DNA and confocal microscopy
    • Manders, E. M., Stap, J., Brakenhoff, G. J., van Driel, R., and Aten, J. A. (1992) Dynamics of three-dimensional replication patterns during the S-phase, analysed by double labelling of DNA and confocal microscopy. J. Cell Sci. 103(Pt 3), 857-862
    • (1992) J. Cell Sci. , vol.103 , Issue.PART 3 , pp. 857-862
    • Manders, E.M.1    Stap, J.2    Brakenhoff, G.J.3    Van Driel, R.4    Aten, J.A.5
  • 18
    • 2942642590 scopus 로고    scopus 로고
    • Automatic and quantitative measurement of protein-protein colocalization in live cells
    • Costes, S. V., Daelemans, D., Cho, E. H., Dobbin, Z., Pavlakis, G., and Lockett, S. (2004) Automatic and quantitative measurement of protein-protein colocalization in live cells. Biophys. J. 86, 3993-4003
    • (2004) Biophys. J. , vol.86 , pp. 3993-4003
    • Costes, S.V.1    Daelemans, D.2    Cho, E.H.3    Dobbin, Z.4    Pavlakis, G.5    Lockett, S.6
  • 19
    • 0032489876 scopus 로고    scopus 로고
    • Processing of laminin-5 and its functional consequences: Role of plasmin and tissue-type plasminogen activator
    • Goldfinger, L. E., Stack, M. S., and Jones, J. C. (1998) Processing of laminin-5 and its functional consequences: role of plasmin and tissue-type plasminogen activator. J. Cell Biol. 141, 255-265
    • (1998) J. Cell Biol. , vol.141 , pp. 255-265
    • Goldfinger, L.E.1    Stack, M.S.2    Jones, J.C.3
  • 20
    • 0032841440 scopus 로고    scopus 로고
    • The alpha3 laminin subunit, alpha6beta4 and alpha3beta1 integrin coordinately regulate wound healing in cultured epithelial cells and in the skin
    • Goldfinger, L. E., Hopkinson, S. B., deHart, G. W., Collawn, S., Couchman, J. R., and Jones, J. C. (1999) The alpha3 laminin subunit, alpha6beta4 and alpha3beta1 integrin coordinately regulate wound healing in cultured epithelial cells and in the skin. J. Cell Sci. 112(Pt 16), 2615-2629
    • (1999) J. Cell Sci. , vol.112 , Issue.PART 16 , pp. 2615-2629
    • Goldfinger, L.E.1    Hopkinson, S.B.2    DeHart, G.W.3    Collawn, S.4    Couchman, J.R.5    Jones, J.C.6
  • 21
    • 0037020196 scopus 로고    scopus 로고
    • The role of apoptosis in creating and maintaining luminal space within normal and oncogene-expressing mammary acini
    • Debnath, J., Mills, K. R., Collins, N. L., Reginato, M. J., Muthuswamy, S. K., and Brugge, J. S. (2002) The role of apoptosis in creating and maintaining luminal space within normal and oncogene-expressing mammary acini. Cell 111, 29-40
    • (2002) Cell , vol.111 , pp. 29-40
    • Debnath, J.1    Mills, K.R.2    Collins, N.L.3    Reginato, M.J.4    Muthuswamy, S.K.5    Brugge, J.S.6
  • 23
    • 0027945083 scopus 로고
    • Production, purification, and characterization of recombinant maspin proteins
    • Sheng, S., Pemberton, P. A., and Sager, R. (1994) Production, purification, and characterization of recombinant maspin proteins. J. Biol. Chem. 269, 30988-30993
    • (1994) J. Biol. Chem. , vol.269 , pp. 30988-30993
    • Sheng, S.1    Pemberton, P.A.2    Sager, R.3
  • 24
    • 11244315121 scopus 로고    scopus 로고
    • Crystal structure of human maspin, a serpin with antitumor properties: Reactive center loop of maspin is exposed but constrained
    • Al-Ayyoubi, M., Gettins, P. G., and Volz, K. (2004) Crystal structure of human maspin, a serpin with antitumor properties: reactive center loop of maspin is exposed but constrained. J. Biol. Chem. 279, 55540-55544
    • (2004) J. Biol. Chem. , vol.279 , pp. 55540-55544
    • Al-Ayyoubi, M.1    Gettins, P.G.2    Volz, K.3
  • 25
    • 0035823595 scopus 로고    scopus 로고
    • The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature
    • Silverman, G. A., Bird, P. I., Carrell, R. W., Church, F. C., Coughlin, P. B., Gettins, P. G., Irving, J. A., Lomas, D. A., Luke, C. J., Moyer, R. W., et al. (2001) The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature. J. Biol. Chem. 276, 33293-33296
    • (2001) J. Biol. Chem. , vol.276 , pp. 33293-33296
    • Silverman, G.A.1    Bird, P.I.2    Carrell, R.W.3    Church, F.C.4    Coughlin, P.B.5    Gettins, P.G.6    Irving, J.A.7    Lomas, D.A.8    Luke, C.J.9    Moyer, R.W.10
  • 26
    • 0029907962 scopus 로고    scopus 로고
    • Maspin acts at the cell membrane to inhibit invasion and motility of mammary and prostatic cancer cells
    • Sheng, S., Carey, J., Seftor, E. A., Dias, L., Hendrix, M. J., and Sager, R. (1996) Maspin acts at the cell membrane to inhibit invasion and motility of mammary and prostatic cancer cells. Proc. Natl. Acad. Sci. U. S. A. 93, 11669-11674
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 11669-11674
    • Sheng, S.1    Carey, J.2    Seftor, E.A.3    Dias, L.4    Hendrix, M.J.5    Sager, R.6
  • 27
    • 0031794915 scopus 로고    scopus 로고
    • Migration of breast epithelial cells on Laminin-5: Differential role of integrins in normal and transformed cell types
    • Plopper, G. E., Domanico, S. Z., Cirulli, V., Kiosses, W. B., and Quaranta, V. (1998) Migration of breast epithelial cells on Laminin-5: differential role of integrins in normal and transformed cell types. Breast Cancer Res. Treat 51, 57-69
    • (1998) Breast Cancer Res. Treat , vol.51 , pp. 57-69
    • Plopper, G.E.1    Domanico, S.Z.2    Cirulli, V.3    Kiosses, W.B.4    Quaranta, V.5
  • 28
    • 0025887362 scopus 로고
    • Epiligrin, a new cell adhesion ligand for integrin alpha 3 beta 1 in epithelial basement membranes
    • Carter, W. G., Ryan, M. C., and Gahr, P. J. (1991) Epiligrin, a new cell adhesion ligand for integrin alpha 3 beta 1 in epithelial basement membranes. Cell 65, 599-610
    • (1991) Cell , vol.65 , pp. 599-610
    • Carter, W.G.1    Ryan, M.C.2    Gahr, P.J.3
  • 29
    • 0028863558 scopus 로고
    • Control of integrin expression by extracellular matrix
    • Delcommenne, M., and Streuli, C. H. (1995) Control of integrin expression by extracellular matrix. J. Biol. Chem. 270, 26794-26801
    • (1995) J. Biol. Chem. , vol.270 , pp. 26794-26801
    • Delcommenne, M.1    Streuli, C.H.2
  • 30
    • 0032217084 scopus 로고    scopus 로고
    • Reciprocal interactions between beta1-integrin and epidermal growth factor receptor in three-dimensional basement membrane breast cultures: A different perspective in epithelial biology
    • Wang, F., Weaver, V. M., Petersen, O. W., Larabell, C. A., Dedhar, S., Briand, P., Lupu, R., and Bissell, M. J. (1998) Reciprocal interactions between beta1-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
  • 31
    • 0035516140 scopus 로고    scopus 로고
    • Transmembrane crosstalk between the extracellular matrix-cytoskeleton crosstalk
    • Geiger, B., Bershadsky, A., Pankov, R., and Yamada, K. M. (2001) Transmembrane crosstalk between the extracellular matrix-cytoskeleton crosstalk. Nat. Rev. Mol. Cell. Biol. 2, 793-805
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 793-805
    • Geiger, B.1    Bershadsky, A.2    Pankov, R.3    Yamada, K.M.4
  • 32
    • 0035654634 scopus 로고    scopus 로고
    • Maspin: Synthesis by human cornea and regulation of in vitro stromal cell adhesion to extracellular matrix
    • Ngamkitidechakul, C., Burke, J. M., O'Brien, W. J., and Twining, S. S. (2001) Maspin: synthesis by human cornea and regulation of in vitro stromal cell adhesion to extracellular matrix. Invest. Ophthalmol. Vis. Sci. 42, 3135-3141
    • (2001) Invest. Ophthalmol. Vis. Sci. , vol.42 , pp. 3135-3141
    • Ngamkitidechakul, C.1    Burke, J.M.2    O'Brien, W.J.3    Twining, S.S.4
  • 33
    • 0037192782 scopus 로고    scopus 로고
    • Evidence for a direct interaction between the tumour suppressor serpin maspin, and types I and III collagen
    • Blacque, O. E., and Worrall, D. M. (2002) Evidence for a direct interaction between the tumour suppressor serpin maspin, and types I and III collagen. J. Biol. Chem.
    • (2002) J. Biol. Chem.
    • Blacque, O.E.1    Worrall, D.M.2
  • 35
    • 0027248518 scopus 로고
    • Identification of a regulatory region of integrin beta 1 subunit using activating and inhibiting antibodies
    • Takada, Y., and Puzon, W. (1993) Identification of a regulatory region of integrin beta 1 subunit using activating and inhibiting antibodies. J. Biol. Chem. 268, 17597-17601
    • (1993) J. Biol. Chem. , vol.268 , pp. 17597-17601
    • Takada, Y.1    Puzon, W.2
  • 36
    • 0033570087 scopus 로고    scopus 로고
    • Three-state unfolding and self-association of maspin, a tumor-suppressing serpin
    • Liu, T., Pemberton, P. A., and Robertson, A. D. (1999) Three-state unfolding and self-association of maspin, a tumor-suppressing serpin. J. Biol. Chem. 274, 29628-29632
    • (1999) J. Biol. Chem. , vol.274 , pp. 29628-29632
    • Liu, T.1    Pemberton, P.A.2    Robertson, A.D.3
  • 37
    • 0018608687 scopus 로고
    • The outer boundary of the cytoskeleton: A lamina derived from plasma membrane proteins
    • Ben-Ze'ev, A., Duerr, A., Solomon, F., and Penman, S. (1979) The outer boundary of the cytoskeleton: a lamina derived from plasma membrane proteins. Cell 17, 859-865
    • (1979) Cell , vol.17 , pp. 859-865
    • Ben-Ze'ev, A.1    Duerr, A.2    Solomon, F.3    Penman, S.4
  • 38
    • 0017699553 scopus 로고
    • Surface distribution of LETS protein in relation to the cytoskeleton of normal and transformed cells
    • Mautner, V., and Hynes, R. O. (1977) Surface distribution of LETS protein in relation to the cytoskeleton of normal and transformed cells. J. Cell Biol. 75, 743-768
    • (1977) J. Cell Biol. , vol.75 , pp. 743-768
    • Mautner, V.1    Hynes, R.O.2
  • 39
    • 0018403475 scopus 로고
    • Cell adhesion and acquisition of detergent resistance by the cytoskeleton of cultured chick fibroblasts
    • Gonen, A., Weisman-Shomer, P., and Fry, M. (1979) Cell adhesion and acquisition of detergent resistance by the cytoskeleton of cultured chick fibroblasts. Biochim. Biophys. Acta 552, 307-321
    • (1979) Biochim. Biophys. Acta , vol.552 , pp. 307-321
    • Gonen, A.1    Weisman-Shomer, P.2    Fry, M.3
  • 40
    • 0037233234 scopus 로고    scopus 로고
    • Polarity determination in breast tissue: Desmosomal adhesion, myoepithelial cells, and laminin 1
    • Bissell, M. J., and Bilder, D. (2003) Polarity determination in breast tissue: desmosomal adhesion, myoepithelial cells, and laminin 1. Breast Cancer Res. 5, 117-119
    • (2003) Breast Cancer Res. , vol.5 , pp. 117-119
    • Bissell, M.J.1    Bilder, D.2
  • 41
    • 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
    • Streuli, C. H., Bailey, N., and Bissell, M. J. (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
  • 43
    • 0033594105 scopus 로고    scopus 로고
    • Extracellular matrix regulates apoptosis in mammary epithelium through a control on insulin signaling
    • Farrelly, N., Lee, Y. J., Oliver, J., Dive, C., and Streuli, C. H. (1999) Extracellular matrix regulates apoptosis in mammary epithelium through a control on insulin signaling. J. Cell Biol. 144, 1337-1348
    • (1999) J. Cell Biol. , vol.144 , pp. 1337-1348
    • Farrelly, N.1    Lee, Y.J.2    Oliver, J.3    Dive, C.4    Streuli, C.H.5
  • 44
    • 5144235557 scopus 로고    scopus 로고
    • Targeted disruption of beta1-integrin in a transgenic mouse model of human breast cancer reveals an essential role in mammary tumor induction
    • White, D. E., Kurpios, N. A., Zuo, D., Hassell, J. A., Blaess, S., Mueller, U., and Muller, W. J. (2004) Targeted disruption of beta1-integrin in a transgenic mouse model of human breast cancer reveals an essential role in mammary tumor induction. Cancer Cell 6, 159-170
    • (2004) Cancer Cell , vol.6 , pp. 159-170
    • White, D.E.1    Kurpios, N.A.2    Zuo, D.3    Hassell, J.A.4    Blaess, S.5    Mueller, U.6    Muller, W.J.7
  • 45
    • 0030936450 scopus 로고    scopus 로고
    • Reversion of the malignant phenotype of human breast cells in three-dimensional culture and in vivo by integrin blocking antibodies
    • Weaver, V. M., Petersen, O. W., Wang, F., Larabell, C. A., Briand, P., Damsky, C., and Bissell, M. J. (1997) Reversion of the malignant phenotype of human breast cells in three-dimensional culture and in vivo by integrin blocking antibodies. J. Cell Biol. 137, 231-245
    • (1997) J. Cell Biol. , vol.137 , pp. 231-245
    • Weaver, V.M.1    Petersen, O.W.2    Wang, F.3    Larabell, C.A.4    Briand, P.5    Damsky, C.6    Bissell, M.J.7
  • 47
    • 2342422643 scopus 로고    scopus 로고
    • Maspin plays an essential role in early embryonic development
    • Gao, F., Shi, H. Y., Daughty, C., Cella, N., and Zhang, M. (2004) Maspin plays an essential role in early embryonic development. Development 131, 1479-1489
    • (2004) Development , vol.131 , pp. 1479-1489
    • Gao, F.1    Shi, H.Y.2    Daughty, C.3    Cella, N.4    Zhang, M.5


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