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Volumn 11, Issue 1 P.889-1198, 2006, Pages 1057-1076

The role of tissue transglutaminase in cell-matrix interactions

Author keywords

Cell Adhesion; Cell Migration; Fibronectin; Integrin; Matrix Assembly; Protein Cross Linking; Review; Transglutaminase

Indexed keywords


EID: 32844466022     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/1863     Document Type: Review
Times cited : (149)

References (129)
  • 1
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: Crosslinking enzymes with pleiotropic functions
    • Lorand, L. & R.M. Graham. Transglutaminases: crosslinking enzymes with pleiotropic functions. Nat. Rev. Mol. Cell. Biol., 4, 140-156 (2003)
    • (2003) Nat. Rev. Mol. Cell. Biol. , vol.4 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 2
    • 0034093354 scopus 로고    scopus 로고
    • Protein crosslinking in assembly and remodelling of extracellular matrices: The role of transglutaminases
    • Aeschlimann, D. & V. Thomazy. Protein crosslinking in assembly and remodelling of extracellular matrices: The role of transglutaminases. Connective Tissue Res., 41, 1-26 (2000)
    • (2000) Connective Tissue Res. , vol.41 , pp. 1-26
    • Aeschlimann, D.1    Thomazy, V.2
  • 3
    • 0036901574 scopus 로고    scopus 로고
    • Transglutaminases: Nature's biological glues
    • Griffin, M., R. Casadio & C.M. Bergamini. Transglutaminases: Nature's biological glues. Biochem. J., 368, 377-396 (2002)
    • (2002) Biochem. J. , vol.368 , pp. 377-396
    • Griffin, M.1    Casadio, R.2    Bergamini, C.M.3
  • 4
    • 0036804796 scopus 로고    scopus 로고
    • Transglutaminase 2: An enigmatic enzyme with diverse functions
    • Fesus, L. & M. Piacentini. Transglutaminase 2: an enigmatic enzyme with diverse functions. Trends Biochem. Sci., 27, 534-539 (2002)
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 534-539
    • Fesus, L.1    Piacentini, M.2
  • 5
    • 0032866851 scopus 로고    scopus 로고
    • Tissue transglutaminase: An enzyme with a split personality
    • Chen J.S. & K. Mehta. Tissue transglutaminase: an enzyme with a split personality. Int. J. Biochem. Cell. Biol., 31, 817-836 (1999)
    • (1999) Int. J. Biochem. Cell. Biol. , vol.31 , pp. 817-836
    • Chen, J.S.1    Mehta, K.2
  • 6
    • 0030863635 scopus 로고    scopus 로고
    • Tissue transglutaminase-dependent posttranslational modification of the retinoblastoma gene product in promonocytic cells undergoing apoptosis
    • Oliverio, S., A. Amendola, F. Di Sano, M.G. Farrace, L. Fesus, Z. Nemes, L. Piredda, A. Spinedi, & M. Piacentini. Tissue transglutaminase-dependent posttranslational modification of the retinoblastoma gene product in promonocytic cells undergoing apoptosis. Mol. Cell. Biol., 17, 6040-6048 (1997)
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6040-6048
    • Oliverio, S.1    Amendola, A.2    Di Sano, F.3    Farrace, M.G.4    Fesus, L.5    Nemes, Z.6    Piredda, L.7    Spinedi, A.8    Piacentini, M.9
  • 7
    • 0037036409 scopus 로고    scopus 로고
    • Tissue transglutaminase protects against apoptosis by modifying the tumor suppressor protein p110 Rb
    • Boehm, J.E., U. Singh, C. Combs, M.A. Antonyak & R.A Cerione. Tissue transglutaminase protects against apoptosis by modifying the tumor suppressor protein p110 Rb. J. Biol. Chem., 277, 20127-20130 (2002)
    • (2002) J. Biol. Chem. , vol.277 , pp. 20127-20130
    • Boehm, J.E.1    Singh, U.2    Combs, C.3    Antonyak, M.A.4    Cerione, R.A.5
  • 8
    • 0029745606 scopus 로고    scopus 로고
    • Core histones are glutaminyl substrates for tissue transglutaminase
    • Ballestar, E., C. Abad & L. Franco. Core histones are glutaminyl substrates for tissue transglutaminase. J. Biol. Chem., 271, 18817-18824 (1996)
    • (1996) J. Biol. Chem. , vol.271 , pp. 18817-18824
    • Ballestar, E.1    Abad, C.2    Franco, L.3
  • 9
    • 0035872859 scopus 로고    scopus 로고
    • Role of transglutaminase II in retinoic acid-induced activation of RhoA-associated kinase-2
    • Singh, U.S., M.T. Kunar, Y.L. Kao & K.M. Baker. Role of transglutaminase II in retinoic acid-induced activation of RhoA-associated kinase-2. EMBO J., 20, 2413-2423 (2001)
    • (2001) EMBO J. , vol.20 , pp. 2413-2423
    • Singh, U.S.1    Kunar, M.T.2    Kao, Y.L.3    Baker, K.M.4
  • 10
    • 0031890377 scopus 로고    scopus 로고
    • Identification of the eukaryotic initiation factor 5A as a retinoic acid-stimulated cellular binding partner for tissue transglutaminase II
    • Singh, U.S., Q. Li & R. Cerione. Identification of the eukaryotic initiation factor 5A as a retinoic acid-stimulated cellular binding partner for tissue transglutaminase II. J. Biol. Chem., 273, 1946-1950 (1998)
    • (1998) J. Biol. Chem. , vol.273 , pp. 1946-1950
    • Singh, U.S.1    Li, Q.2    Cerione, R.3
  • 12
    • 0029096258 scopus 로고
    • Transglutaminase crosslinking of the tau protein
    • Miller, M.L. & G.V. Johnson. Transglutaminase crosslinking of the tau protein. J. Neurochem., 65, 1760-1770 (1995)
    • (1995) J. Neurochem. , vol.65 , pp. 1760-1770
    • Miller, M.L.1    Johnson, G.V.2
  • 14
    • 1842332757 scopus 로고    scopus 로고
    • Identification of cytoplasmic actin as an abundant glutaminyl substrate for tissue transglutaminase in HL-60 and U937 cells undergoing apoptosis
    • Nemes Z. Jr., R. Adany, M. Balazs, P. Boross & L. Fesus. Identification of cytoplasmic actin as an abundant glutaminyl substrate for tissue transglutaminase in HL-60 and U937 cells undergoing apoptosis. J. Biol. Chem., 272, 20577-20583 (1997)
    • (1997) J. Biol. Chem. , vol.272 , pp. 20577-20583
    • Nemes Jr., Z.1    Adany, R.2    Balazs, M.3    Boross, P.4    Fesus, L.5
  • 15
    • 0032549637 scopus 로고    scopus 로고
    • The cell adhesion molecule C-CAM is a substrate for tissue transglutaminase
    • Hunter, I., K. Sigmundsson, N. Beauchemin & B. Obrink. The cell adhesion molecule C-CAM is a substrate for tissue transglutaminase. FEBS Lett., 425, 141-144 (1998)
    • (1998) FEBS Lett. , vol.425 , pp. 141-144
    • Hunter, I.1    Sigmundsson, K.2    Beauchemin, N.3    Obrink, B.4
  • 16
    • 0028231735 scopus 로고
    • Transglutaminase-mediated processing of fibronectin by endothelial cell monolayers
    • Martinez, J., D.G. Chalupowicz, R.K. Roush, A. Sheth, & C. Barsigian. Transglutaminase-mediated processing of fibronectin by endothelial cell monolayers. Biochemistry 33, 2538-2545 (1994)
    • (1994) Biochemistry , vol.33 , pp. 2538-2545
    • Martinez, J.1    Chalupowicz, D.G.2    Roush, R.K.3    Sheth, A.4    Barsigian, C.5
  • 17
    • 0025607863 scopus 로고
    • Cross-linked Aα-γ chain hybrids serve as unique markers fro fibrinogen polymerized by tissue transglutaminase
    • Murthy, S.N. & L. Lorand. Cross-linked Aα-γ chain hybrids serve as unique markers fro fibrinogen polymerized by tissue transglutaminase. Proc. Natl. Acad. Sci. USA, 87, 9679-9682 (1990)
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9679-9682
    • Murthy, S.N.1    Lorand, L.2
  • 18
    • 0023139866 scopus 로고
    • Identification of a substrate site for liver transglutaminase on the aminopeptide of type III collagen
    • Bowness, J.M., I.E. Folk & R. Timpl. Identification of a substrate site for liver transglutaminase on the aminopeptide of type III collagen. J. Biol. Chem., 262, 1022-1024 (1987)
    • (1987) J. Biol. Chem. , vol.262 , pp. 1022-1024
    • Bowness, J.M.1    Folk, I.E.2    Timpl, R.3
  • 20
    • 0025823541 scopus 로고
    • Cross-linking of laminin-nidogen complexes by tissue transglutaminase. A novel mechanism for basement membrane stabilization
    • Aeschlimann, D. & M. Paulsson. Cross-linking of laminin-nidogen complexes by tissue transglutaminase. A novel mechanism for basement membrane stabilization. J. Biol. Chem. 266, 15308-15317 (1991)
    • (1991) J. Biol. Chem. , vol.266 , pp. 15308-15317
    • Aeschlimann, D.1    Paulsson, M.2
  • 21
    • 0030983922 scopus 로고    scopus 로고
    • Transglutaminase-catalyzed cross-linking of osteopontin is inhibited by osteocalcin
    • Kaartinen, M.T., A. Pirhonen, A. Linnala-Kankunen, & P.H. Maenpaa. Transglutaminase-catalyzed cross-linking of osteopontin is inhibited by osteocalcin. J. Biol. Chem., 272, 22736-22741 (1997)
    • (1997) J. Biol. Chem. , vol.272 , pp. 22736-22741
    • Kaartinen, M.T.1    Pirhonen, A.2    Linnala-Kankunen, A.3    Maenpaa, P.H.4
  • 22
    • 0030974902 scopus 로고    scopus 로고
    • Latent transforming growth factor-beta binding protein domains involved in activation and transglutaminase-dependent cross-linking of latent transforming growth factor-beta
    • Nunes, I., P.E. Gleizes, C.N. Metz & D.B. Rifkin. Latent transforming growth factor-beta binding protein domains involved in activation and transglutaminase-dependent cross-linking of latent transforming growth factor-beta. J. Cell Biol., 136, 1151-1163 (1997)
    • (1997) J. Cell Biol. , vol.136 , pp. 1151-1163
    • Nunes, I.1    Gleizes, P.E.2    Metz, C.N.3    Rifkin, D.B.4
  • 23
    • 0028176166 scopus 로고
    • Gh: A GTP-binding protein with transglutaminase activity and receptor signaling function
    • Nakaoka, H., D.M. Perez, K.J. Baek, T. Das, A. Husain, K. Misono, M.J. Im, & R.M. Graham. Gh: a GTP-binding protein with transglutaminase activity and receptor signaling function. Science, 264, 1593-1596 (1994)
    • (1994) Science , vol.264 , pp. 1593-1596
    • Nakaoka, H.1    Perez, D.M.2    Baek, K.J.3    Das, T.4    Husain, A.5    Misono, K.6    Im, M.J.7    Graham, R.M.8
  • 24
    • 0032718477 scopus 로고    scopus 로고
    • Interactions of G(h)/transglutaminase with phospholipase Cdelta1 and with GTP
    • Murthy, S.N., J.W. Lomasney, E.G. Mak, & L. Lorand. Interactions of G(h)/transglutaminase with phospholipase Cdelta1 and with GTP. Proc. Natl. Acad. Sci. USA, 96, 11815-11819 (1999)
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11815-11819
    • Murthy, S.N.1    Lomasney, J.W.2    Mak, E.G.3    Lorand, L.4
  • 25
    • 0032475924 scopus 로고    scopus 로고
    • GTP-dependent conformational changes associated with the functional switch between Galpha and cross-linking activities in brain-derived tissue transglutaminase
    • Monsonego, A., I. Friedmann, Y. Shani, M. Eisenstein & M. Schwartz. GTP-dependent conformational changes associated with the functional switch between Galpha and cross-linking activities in brain-derived tissue transglutaminase. J. Mol. Biol., 282, 713-720 (1998)
    • (1998) J. Mol. Biol. , vol.282 , pp. 713-720
    • Monsonego, A.1    Friedmann, I.2    Shani, Y.3    Eisenstein, M.4    Schwartz, M.5
  • 27
    • 2642536093 scopus 로고    scopus 로고
    • Tissue transglutaminase has intrinsic kinase activity: Identification of transglutaminase 2 as an insulin-like growth factor-binding protein-3 kinase
    • Mishra, S. & L.J. Murphy. Tissue transglutaminase has intrinsic kinase activity: identification of transglutaminase 2 as an insulin-like growth factor-binding protein-3 kinase. J. Biol. Chem., 279, 23863-23868 (2004)
    • (2004) J. Biol. Chem. , vol.279 , pp. 23863-23868
    • Mishra, S.1    Murphy, L.J.2
  • 28
    • 0037022619 scopus 로고    scopus 로고
    • Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity
    • Liu, S., R.A. Cerione & J. Clardy. Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity. Proc. Natl. Acad. Sci. U S A., 99, 2743-2747 (2002)
    • (2002) Proc. Natl. Acad. Sci. U S A. , vol.99 , pp. 2743-2747
    • Liu, S.1    Cerione, R.A.2    Clardy, J.3
  • 29
    • 0034674770 scopus 로고    scopus 로고
    • GTP binding and signaling by Gh/transglutaminase II involves distinct residues in a unique GTP-binding pocket
    • Iismaa, S.E., M.J. Wu, N. Nanda, W.B. Church & R.M. Graham. GTP binding and signaling by Gh/transglutaminase II involves distinct residues in a unique GTP-binding pocket. J. Biol. Chem., 275, 18259-18265 (2000)
    • (2000) J. Biol. Chem. , vol.275 , pp. 18259-18265
    • Iismaa, S.E.1    Wu, M.J.2    Nanda, N.3    Church, W.B.4    Graham, R.M.5
  • 30
    • 0024597647 scopus 로고
    • Differential expression of tissue transglutaminase in human cells. An immunohistochemical study
    • Thomazy, V. & L. Fesus. Differential expression of tissue transglutaminase in human cells. An immunohistochemical study. Cell Tissue Res., 255, 215-224 (1989)
    • (1989) Cell Tissue Res. , vol.255 , pp. 215-224
    • Thomazy, V.1    Fesus, L.2
  • 31
    • 0032557461 scopus 로고    scopus 로고
    • Identification of a transforming growth factor-beta1/bone morphogenetic protein 4 (TGF-beta1/BMP4) response element within the mouse tissue transglutaminase gene promoter
    • Ritter, S.J. & P.J. Davies. Identification of a transforming growth factor-beta1/bone morphogenetic protein 4 (TGF-beta1/BMP4) response element within the mouse tissue transglutaminase gene promoter. J. Biol. Chem., 273, 12798-12806 (1998)
    • (1998) J. Biol. Chem. , vol.273 , pp. 12798-12806
    • Ritter, S.J.1    Davies, P.J.2
  • 32
    • 0037019816 scopus 로고    scopus 로고
    • Specific methylation of the CpG-rich domains in the promoter of the human tissue transglutaminase gene
    • Cacciamani, T., S. Virgili, M. Centurelli, E. Bertoli, T. Eremenko & P. Volpe. Specific methylation of the CpG-rich domains in the promoter of the human tissue transglutaminase gene. Gene, 297, 103-112 (2002)
    • (2002) Gene , vol.297 , pp. 103-112
    • Cacciamani, T.1    Virgili, S.2    Centurelli, M.3    Bertoli, E.4    Eremenko, T.5    Volpe, P.6
  • 33
    • 0030894829 scopus 로고    scopus 로고
    • Regulation of the expression of the tissue transglutaminase gene by DNA methylation
    • Lu, S. & P.J. Davies. Regulation of the expression of the tissue transglutaminase gene by DNA methylation. Proc. Natl. Acad. Sci. USA, 94, 4692-4697 (1997)
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4692-4697
    • Lu, S.1    Davies, P.J.2
  • 34
    • 0032524312 scopus 로고    scopus 로고
    • Distinct nuclear localization and activity of tissue transglutaminase
    • Lesort, M., K. Attanavanich, J. Zhang & G.V. Johnson. Distinct nuclear localization and activity of tissue transglutaminase. J. Biol Chem., 273, 11991-11994 (1998)
    • (1998) J. Biol Chem. , vol.273 , pp. 11991-11994
    • Lesort, M.1    Attanavanich, K.2    Zhang, J.3    Johnson, G.V.4
  • 35
    • 1542335670 scopus 로고    scopus 로고
    • Intracellular localization and activity state of tissue transglutaminase differentially impacts cell death
    • Milakovic, T., J. Tucholski, E. McCoy & G.V. Johnson. Intracellular localization and activity state of tissue transglutaminase differentially impacts cell death. J. Biol. Chem., 279, 8715-8722 (2004)
    • (2004) J. Biol. Chem. , vol.279 , pp. 8715-8722
    • Milakovic, T.1    Tucholski, J.2    McCoy, E.3    Johnson, G.V.4
  • 36
    • 0032988045 scopus 로고    scopus 로고
    • Interaction of tissue transglutaminase with nuclear transport protein importin-alpha3
    • Peng, X., Y. Zhang, H. Zhang, S. Graner, J.F. Williams, M.L. Levitt & A. Lokshin. Interaction of tissue transglutaminase with nuclear transport protein importin-alpha3. FEBS Lett., 446, 35-39 (1999)
    • (1999) FEBS Lett. , vol.446 , pp. 35-39
    • Peng, X.1    Zhang, Y.2    Zhang, H.3    Graner, S.4    Williams, J.F.5    Levitt, M.L.6    Lokshin, A.7
  • 37
    • 0033573849 scopus 로고    scopus 로고
    • Alpha 1B-adrenoceptor interacts with multiple sites of transglutaminase II: Characteristics of the interaction in binding and activation
    • Feng, J.F., C.D. Gray & M.J. Im. Alpha 1B-adrenoceptor interacts with multiple sites of transglutaminase II: characteristics of the interaction in binding and activation. Biochemistry, 38, 2224-2232 (1999)
    • (1999) Biochemistry , vol.38 , pp. 2224-2232
    • Feng, J.F.1    Gray, C.D.2    Im, M.J.3
  • 38
    • 0034695929 scopus 로고    scopus 로고
    • Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin
    • Akimov, S.S., D. Krylov, L.F. Fleischman & A.M. Belkin. Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin. J. Cell Biol., 148, 825-838 (2000)
    • (2000) J. Cell Biol. , vol.148 , pp. 825-838
    • Akimov, S.S.1    Krylov, D.2    Fleischman, L.F.3    Belkin, A.M.4
  • 39
    • 0021093255 scopus 로고
    • Interaction between tissue transglutaminase and phospholipid vesicles
    • Fesus L., A. Horvath & J. Harsfalvi. Interaction between tissue transglutaminase and phospholipid vesicles. FEBS Lett., 155, 1-5 (1983)
    • (1983) FEBS Lett. , vol.155 , pp. 1-5
    • Fesus, L.1    Horvath, A.2    Harsfalvi, J.3
  • 40
  • 41
    • 0025885719 scopus 로고
    • Localization of cellular transglutaminase on the extracellular matrix after wounding: Characteristics of the matrix-bound enzyme
    • Upchurch, H.F., E. Conway & M.D. Maxwell. Localization of cellular transglutaminase on the extracellular matrix after wounding: characteristics of the matrix-bound enzyme. J. Cell. Physiol., 149, 375-382 (1991)
    • (1991) J. Cell. Physiol. , vol.149 , pp. 375-382
    • Upchurch, H.F.1    Conway, E.2    Maxwell, M.D.3
  • 42
    • 0025837326 scopus 로고
    • Tissue (type II) transglutaminase covalently incorporates itself, fibrinogen, or fibronectin into high molecular weight complexes on the extracellular surface of isolated hepatocytes. Use of 2-[(2-oxopropyl)thio] imidazolium derivatives as cellular transglutaminase inactivators
    • Barsigian, C., A.M. Stern & J. Martinez. Tissue (type II) transglutaminase covalently incorporates itself, fibrinogen, or fibronectin into high molecular weight complexes on the extracellular surface of isolated hepatocytes. Use of 2-[(2-oxopropyl)thio] imidazolium derivatives as cellular transglutaminase inactivators. J. Biol. Chem., 266, 22501-22509 (1991)
    • (1991) J. Biol. Chem. , vol.266 , pp. 22501-22509
    • Barsigian, C.1    Stern, A.M.2    Martinez, J.3
  • 43
    • 0033544020 scopus 로고    scopus 로고
    • Tissue transglutaminase is an important player at the surface of human endothelial cells: Evidence for its externalization and its colocalization with the beta(1) integrin
    • Gaudry, C.A., E. Verderio, R.A. Jones, C. Smith & M. Griffin. Tissue transglutaminase is an important player at the surface of human endothelial cells: evidence for its externalization and its colocalization with the beta(1) integrin. Exp. Cell Res., 252, 104-113 (1999)
    • (1999) Exp. Cell Res. , vol.252 , pp. 104-113
    • Gaudry, C.A.1    Verderio, E.2    Jones, R.A.3    Smith, C.4    Griffin, M.5
  • 45
    • 0026705663 scopus 로고
    • Expression of tissue trans-glutaminase in Balb-C 3T3 fibroblasts: Effects on cell morphology and adhesion
    • Gentile, V., V. Thomazy, M. Piacentini, L. Fesus & P.J. Davies. Expression of tissue trans-glutaminase in Balb-C 3T3 fibroblasts: effects on cell morphology and adhesion. J. Cell Biol., 119, 463-474 (1992)
    • (1992) J. Cell Biol. , vol.119 , pp. 463-474
    • Gentile, V.1    Thomazy, V.2    Piacentini, M.3    Fesus, L.4    Davies, P.J.5
  • 46
    • 0010115712 scopus 로고    scopus 로고
    • Reduced expression of tissue transglutaminase in a human endothelial cell line leads to changes in cell spreading, cell adhesion and reduced polymerisation of fibronectin
    • Jones, R.A., B. Nicholas, S. Mian, P.J. Davies & M. Griffin. Reduced expression of tissue transglutaminase in a human endothelial cell line leads to changes in cell spreading, cell adhesion and reduced polymerisation of fibronectin. J. Cell Sci., 110, 2461-2472 (1997)
    • (1997) J. Cell Sci. , vol.110 , pp. 2461-2472
    • Jones, R.A.1    Nicholas, B.2    Mian, S.3    Davies, P.J.4    Griffin, M.5
  • 47
    • 0031869591 scopus 로고    scopus 로고
    • Regulated expression of tissue transglutaminase in Swiss 3T3 fibroblasts: Effects on the processing of fibronectin, cell attachment, and cell death
    • Verderio, E., B. Nicholas, S. Gross & M. Griffin. Regulated expression of tissue transglutaminase in Swiss 3T3 fibroblasts: effects on the processing of fibronectin, cell attachment, and cell death. Exp. Cell Res., 239, 119-138 (1998)
    • (1998) Exp. Cell Res. , vol.239 , pp. 119-138
    • Verderio, E.1    Nicholas, B.2    Gross, S.3    Griffin, M.4
  • 49
    • 0035947675 scopus 로고    scopus 로고
    • Matrix-dependent proteolysis of surface transglutaminase by membrane-type metalloproteinase regulates cancer cell adhesion and locomotion
    • Belkin, A.M., S.S. Akimov, L.S. Zaritskaya, B.I. Ratnikov, E.I. Deryugina & A.Y. Strongin. Matrix-dependent proteolysis of surface transglutaminase by membrane-type metalloproteinase regulates cancer cell adhesion and locomotion. J. Biol. Chem., 276, 18415-18422 (2001)
    • (2001) J. Biol. Chem. , vol.276 , pp. 18415-18422
    • Belkin, A.M.1    Akimov, S.S.2    Zaritskaya, L.S.3    Ratnikov, B.I.4    Deryugina, E.I.5    Strongin, A.Y.6
  • 50
    • 0035469864 scopus 로고    scopus 로고
    • Cell surface tissue transglutaminase is involved in adhesion and migration of monocytic cells on fibronectin
    • Akimov, S.S. & A.M. Belkin. Cell surface tissue transglutaminase is involved in adhesion and migration of monocytic cells on fibronectin. Blood, 98, 1567-1576 (2001)
    • (2001) Blood , vol.98 , pp. 1567-1576
    • Akimov, S.S.1    Belkin, A.M.2
  • 51
    • 1542742158 scopus 로고    scopus 로고
    • TGF-beta2-induced cell surface tissue transglutaminase increases adhesion and migration of RPE cells on fibronectin through the gelatin-binding domain
    • Priglinger, S.G., C.S. Alge, A.S. Neubauer, N. Kristin, C. Hirneiss, K. Eibl, A. Kampik & U. Welge-Lussen. TGF-beta2-induced cell surface tissue transglutaminase increases adhesion and migration of RPE cells on fibronectin through the gelatin-binding domain. Invest. Ophthalmol. Vis. Sci., 45, 955-963 (2004)
    • (2004) Invest. Ophthalmol. Vis. Sci. , vol.45 , pp. 955-963
    • Priglinger, S.G.1    Alge, C.S.2    Neubauer, A.S.3    Kristin, N.4    Hirneiss, C.5    Eibl, K.6    Kampik, A.7    Welge-Lussen, U.8
  • 53
    • 0004043397 scopus 로고
    • Springer-Verlag, New York
    • Hynes, R.O. Fibronectins. Springer-Verlag, New York. 1-284 (1990)
    • (1990) Fibronectins , pp. 1-284
    • Hynes, R.O.1
  • 54
    • 0031713365 scopus 로고    scopus 로고
    • Fibronectin: Structure, assembly, and cardiovascular implications
    • Magnusson, M.K. & D.F. Mosher. Fibronectin: structure, assembly, and cardiovascular implications. Arterioscler. Thromb. Vasc. Biol., 18, 1363-1370 (1998)
    • (1998) Arterioscler. Thromb. Vasc. Biol. , vol.18 , pp. 1363-1370
    • Magnusson, M.K.1    Mosher, D.F.2
  • 55
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional allosteric signaling machines
    • Hynes, R.O. Integrins: bidirectional allosteric signaling machines. Cell 110, 673-687 (2002)
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 56
    • 8544283045 scopus 로고    scopus 로고
    • Cell biology: Adhesion articulated
    • Mould, A.P. & M.J. Humphries. Cell biology: adhesion articulated. Nature, 432, 27-28 (2004)
    • (2004) Nature , vol.432 , pp. 27-28
    • Mould, A.P.1    Humphries, M.J.2
  • 57
    • 8744228282 scopus 로고    scopus 로고
    • Mechanisms of integration of cells and extracellular matrices by integrins
    • Humphries, M.J., M.A. Travis, K. Clark & A.P. Mould. Mechanisms of integration of cells and extracellular matrices by integrins. Biochem. Soc. Trans., 32, 822-825 (2004)
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 822-825
    • Humphries, M.J.1    Travis, M.A.2    Clark, K.3    Mould, A.P.4
  • 58
    • 0028088291 scopus 로고
    • Genetic analyses of cell-matrix interactions in development
    • Hynes, R.O. Genetic analyses of cell-matrix interactions in development. Curr. Opin. Genet. Dev., 4, 569-574 (1994)
    • (1994) Curr. Opin. Genet. Dev. , vol.4 , pp. 569-574
    • Hynes, R.O.1
  • 61
    • 0036473019 scopus 로고    scopus 로고
    • The incorporation of fibrinogen into extracellular matrix is dependent on active assembly of a fibronectin matrix
    • Pereira, M., B.J. Rybarczyk, T.M. Odrljin, D.C. Hocking, J. Sottile & P.J. Simpson-Haidaris. The incorporation of fibrinogen into extracellular matrix is dependent on active assembly of a fibronectin matrix. J. Cell Sci., 115, 609-617 (2002)
    • (2002) J. Cell Sci. , vol.115 , pp. 609-617
    • Pereira, M.1    Rybarczyk, B.J.2    Odrljin, T.M.3    Hocking, D.C.4    Sottile, J.5    Simpson-Haidaris, P.J.6
  • 62
    • 0036796746 scopus 로고    scopus 로고
    • Fibronectin polymerization regulates the composition and stability of extracellular matrix fibrils and cell-matrix adhesions
    • Sottile, J. & D.C. Hocking. Fibronectin polymerization regulates the composition and stability of extracellular matrix fibrils and cell-matrix adhesions. Mol. Biol. Cell, 13, 3546-3559 (2002)
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3546-3559
    • Sottile, J.1    Hocking, D.C.2
  • 63
    • 0034534561 scopus 로고    scopus 로고
    • Fibronectin polymerization stimulates cell growth by RGD-dependent and -independent mechanisms
    • Sottile, J., D.C. Hocking & K.J. Langenbach. Fibronectin polymerization stimulates cell growth by RGD-dependent and -independent mechanisms. J. Cell Sci., 113, 4287-4299 (2000)
    • (2000) J. Cell Sci. , vol.113 , pp. 4287-4299
    • Sottile, J.1    Hocking, D.C.2    Langenbach, K.J.3
  • 64
    • 0023845995 scopus 로고
    • Fibronectin as a carrier for the transglutaminase from human erythrocytes
    • Lorand, L., J.E. Dailey & P.M. Turner. Fibronectin as a carrier for the transglutaminase from human erythrocytes. Proc. Natl. Acad. Sci. U S A, 85, 1057-1059 (1988)
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 1057-1059
    • Lorand, L.1    Dailey, J.E.2    Turner, P.M.3
  • 65
    • 0024585067 scopus 로고
    • Complexation of fibronectin with tissue transglutaminase
    • Turner, P.M. & L. Lorand. Complexation of fibronectin with tissue transglutaminase. Biochemistry, 28, 628-635 (1989)
    • (1989) Biochemistry , vol.28 , pp. 628-635
    • Turner, P.M.1    Lorand, L.2
  • 67
    • 0034839336 scopus 로고    scopus 로고
    • Cell-surface transglutaminase promotes fibronectin assembly via interaction with the gelatin-binding domain of fibronectin: A role in TGFbeta-dependent matrix deposition
    • Akimov, S.S. & A.M. Belkin. Cell-surface transglutaminase promotes fibronectin assembly via interaction with the gelatin-binding domain of fibronectin: a role in TGFbeta-dependent matrix deposition. J. Cell Sci., 114, 2989-3000 (2001)
    • (2001) J. Cell Sci. , vol.114 , pp. 2989-3000
    • Akimov, S.S.1    Belkin, A.M.2
  • 68
    • 0142242157 scopus 로고    scopus 로고
    • A novel RGD-independent cell adhesion pathway mediated by fibronectin-bound tissue transglutaminase rescues cells from anoikis
    • Verderio, E.A.M., D. Telci, A. Okoye, G. Melino & M. Griffin. A novel RGD-independent cell adhesion pathway mediated by fibronectin-bound tissue transglutaminase rescues cells from anoikis. J. Biol. Chem., 278, 42604-42614 (2003)
    • (2003) J. Biol. Chem. , vol.278 , pp. 42604-42614
    • Verderio, E.A.M.1    Telci, D.2    Okoye, A.3    Melino, G.4    Griffin, M.5
  • 69
    • 0027416842 scopus 로고
    • Affinity of human erythrocyte transglutaminase for a 42-kDa gelatin-binding fragment of human plasma fibronectin
    • Radek, J.T., J.M. Jeong, S.N. Murthy, K.C. Ingham & L. Lorand. Affinity of human erythrocyte transglutaminase for a 42-kDa gelatin-binding fragment of human plasma fibronectin. Proc. Natl. Acad. Sci. USA, 90, 3152-3156 (1993)
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3152-3156
    • Radek, J.T.1    Jeong, J.M.2    Murthy, S.N.3    Ingham, K.C.4    Lorand, L.5
  • 71
    • 0028928017 scopus 로고
    • The fibronectin-binding domain of transglutaminase
    • Jeong, J.M., S.N. Murthy, J.T. Radek & L. Lorand. The fibronectin-binding domain of transglutaminase. J. Biol. Chem., 270, 5654-5658 (1995)
    • (1995) J. Biol. Chem. , vol.270 , pp. 5654-5658
    • Jeong, J.M.1    Murthy, S.N.2    Radek, J.T.3    Lorand, L.4
  • 73
    • 0029859391 scopus 로고    scopus 로고
    • Dual functions of transglutaminase in novel cell adhesion
    • Ueki, S., J. Takagi & Y. Saito. Dual functions of transglutaminase in novel cell adhesion. J. Cell Sci., 109, 2727-2735 (1996)
    • (1996) J. Cell Sci. , vol.109 , pp. 2727-2735
    • Ueki, S.1    Takagi, J.2    Saito, Y.3
  • 74
    • 0033402619 scopus 로고    scopus 로고
    • Activity-independent cell adhesion to tissue-type transglutaminase is mediated by alpha4beta1 integrin
    • Isobe, T., H. Takahashi, S. Ueki, J. Takagi & Y. Saito. Activity-independent cell adhesion to tissue-type transglutaminase is mediated by alpha4beta1 integrin. Eur. J. Cell Biol., 78, 876-883 (1999)
    • (1999) Eur. J. Cell Biol. , vol.78 , pp. 876-883
    • Isobe, T.1    Takahashi, H.2    Ueki, S.3    Takagi, J.4    Saito, Y.5
  • 75
    • 0034604565 scopus 로고    scopus 로고
    • Tissue transglutaminase, coagulation factor XIII, and the pro-polypeptide of von Willebrand factor are all ligands for the integrins alpha9beta 1 and alpha 4beta 1
    • Takahashi H., T. Isobe, S. Horibe, J. Takagi, Y. Yokosaki, D. Sheppard & Y. Saito. Tissue transglutaminase, coagulation factor XIII, and the pro-polypeptide of von Willebrand factor are all ligands for the integrins alpha9beta 1 and alpha 4beta 1. J. Biol. Chem., 275, 23589-23595 (2000)
    • (2000) J. Biol. Chem. , vol.275 , pp. 23589-23595
    • Takahashi, H.1    Isobe, T.2    Horibe, S.3    Takagi, J.4    Yokosaki, Y.5    Sheppard, D.6    Saito, Y.7
  • 76
    • 4644335421 scopus 로고    scopus 로고
    • Cell-surface-associated tissue transglutaminase is a target of MMP-2 proteolysis
    • Belkin, A.M., E.A. Zemskov, J. Hang, S.S. Akimov, S. Sikora & A.Y. Strongin. Cell-surface-associated tissue transglutaminase is a target of MMP-2 proteolysis. Biochemistry, 43, 11760-11769 (2004)
    • (2004) Biochemistry , vol.43 , pp. 11760-11769
    • Belkin, A.M.1    Zemskov, E.A.2    Hang, J.3    Akimov, S.S.4    Sikora, S.5    Strongin, A.Y.6
  • 78
    • 0033578417 scopus 로고    scopus 로고
    • Calreticulin down-regulates both GTP binding and transglutaminase activities of transglutaminase II
    • Feng, J.F., M. Readon, S.P. Yadav & M.J. Im. Calreticulin down-regulates both GTP binding and transglutaminase activities of transglutaminase II. Biochemistry, 38, 10743-10749 (1999)
    • (1999) Biochemistry , vol.38 , pp. 10743-10749
    • Feng, J.F.1    Readon, M.2    Yadav, S.P.3    Im, M.J.4
  • 79
    • 0033591411 scopus 로고    scopus 로고
    • Calreticulin affects focal contact-dependent but not close contact-dependent cell-substratum adhesion
    • Fadel, M.P., E. Dziak, C.M. Lo, J. Ferrier, N. Mesaeli, M. Michalak & M. Opas. Calreticulin affects focal contact-dependent but not close contact-dependent cell-substratum adhesion. J. Biol. Chem., 274, 15085-15094 (1999)
    • (1999) J. Biol. Chem. , vol.274 , pp. 15085-15094
    • Fadel, M.P.1    Dziak, E.2    Lo, C.M.3    Ferrier, J.4    Mesaeli, N.5    Michalak, M.6    Opas, M.7
  • 80
    • 0034680794 scopus 로고    scopus 로고
    • Thrombospondin mediates focal adhesion disassembly through interactions with cell surface calreticulin
    • Goicoechea, S., A.W. Orr, M.A. Pallero, P. Eggleton & I.E. Murphy-Ullrich. Thrombospondin mediates focal adhesion disassembly through interactions with cell surface calreticulin. J. Biol. Chem., 275, 36358-36368 (2000)
    • (2000) J. Biol. Chem. , vol.275 , pp. 36358-36368
    • Goicoechea, S.1    Orr, A.W.2    Pallero, M.A.3    Eggleton, P.4    Murphy-Ullrich, I.E.5
  • 82
    • 0034836428 scopus 로고    scopus 로고
    • LRP: A multifunctional scavenger and signaling receptor
    • Herz, J. & D.K. Strickland. LRP: a multifunctional scavenger and signaling receptor. J. Clin. Invest., 108, 779-784 (2001)
    • (2001) J. Clin. Invest. , vol.108 , pp. 779-784
    • Herz, J.1    Strickland, D.K.2
  • 83
    • 0037432766 scopus 로고    scopus 로고
    • LRP: Role in vascular wall integrity and protection from atherosclerosis
    • Boucher, P., M. Gotthardt, W.P. Li, R.G. Anderson & J. Herz. LRP: role in vascular wall integrity and protection from atherosclerosis. Science, 300, 329-332 (2003)
    • (2003) Science , vol.300 , pp. 329-332
    • Boucher, P.1    Gotthardt, M.2    Li, W.P.3    Anderson, R.G.4    Herz, J.5
  • 84
    • 0028907482 scopus 로고
    • Isolation and characterization of the human tissue transglutaminase gene promoter
    • Lu, S., M. Saydak, V. Gentile, J.P. Stein & P.J. Davies. Isolation and characterization of the human tissue transglutaminase gene promoter. J. Biol. Chem., 270, 9748-9756 (1995)
    • (1995) J. Biol. Chem. , vol.270 , pp. 9748-9756
    • Lu, S.1    Saydak, M.2    Gentile, V.3    Stein, J.P.4    Davies, P.J.5
  • 85
    • 0021750326 scopus 로고
    • Retinoic acid-induced expression of tissue transglutaminase in mouse peritoneal macrophages
    • Moore, W.T. Jr., M.P. Murtaugh & P.J. Davies. Retinoic acid-induced expression of tissue transglutaminase in mouse peritoneal macrophages. J. Biol. Chem., 259, 12794-12802 (1984)
    • (1984) J. Biol. Chem. , vol.259 , pp. 12794-12802
    • Moore Jr., W.T.1    Murtaugh, M.P.2    Davies, P.J.3
  • 86
    • 0030051022 scopus 로고    scopus 로고
    • Identification and characterization of a versatile retinoid response element (retinoic acid receptor response element-retinoid X receptor response element) in the mouse tissue transglutaminase gene promoter
    • Nagy, L., M. Saydak, N. Shipley, S. Lu, J.P. Basilion, Z.H. Yan, P. Syka, R.A. Chandraratna, J.P. Stein, R.A. Heyman & P.J. Davies. Identification and characterization of a versatile retinoid response element (retinoic acid receptor response element-retinoid X receptor response element) in the mouse tissue transglutaminase gene promoter. J. Biol. Chem., 271, 4355-4365 (1996)
    • (1996) J. Biol. Chem. , vol.271 , pp. 4355-4365
    • Nagy, L.1    Saydak, M.2    Shipley, N.3    Lu, S.4    Basilion, J.P.5    Yan, Z.H.6    Syka, P.7    Chandraratna, R.A.8    Stein, J.P.9    Heyman, R.A.10    Davies, P.J.11
  • 87
    • 0025293021 scopus 로고
    • Regulation of transglutaminase type II by transforming growth factor-beta 1 in normal and transformed human epidermal keratinocytes
    • George, M.D., T.M. Vollberg, E.E. Floyd, J.P. Stein & A.M. Jetten. Regulation of transglutaminase type II by transforming growth factor-beta 1 in normal and transformed human epidermal keratinocytes. J. Biol. Chem., 265, 11098-11104 (1990)
    • (1990) J. Biol. Chem. , vol.265 , pp. 11098-11104
    • George, M.D.1    Vollberg, T.M.2    Floyd, E.E.3    Stein, J.P.4    Jetten, A.M.5
  • 88
    • 32844462359 scopus 로고    scopus 로고
    • TGF-beta1 up-regulates transglutaminase two and fibronectin in dermal fibroblasts: A possible mechanism for the stabilization of tissue inflammation
    • Quan, G., J.Y. Choi, D.S. Lee & S.C. Lee. TGF-beta1 up-regulates transglutaminase two and fibronectin in dermal fibroblasts: a possible mechanism for the stabilization of tissue inflammation. Arch. Dermatol. Res., 26, 1-7 (2005)
    • (2005) Arch. Dermatol. Res. , vol.26 , pp. 1-7
    • Quan, G.1    Choi, J.Y.2    Lee, D.S.3    Lee, S.C.4
  • 89
    • 0027405028 scopus 로고
    • Expression induced by interleukin-6 of tissue-type transglutaminase in human hepatoblastoma HepG2 cells
    • Suto, N., K. Ikura & R. Sasaki. Expression induced by interleukin-6 of tissue-type transglutaminase in human hepatoblastoma HepG2 cells. J. Biol. Chem., 268, 7469-7473 (1993)
    • (1993) J. Biol. Chem. , vol.268 , pp. 7469-7473
    • Suto, N.1    Ikura, K.2    Sasaki, R.3
  • 90
    • 0035403504 scopus 로고    scopus 로고
    • Interleukin-1 induces pro-mineralizing activity of cartilage tissue transglutaminase and factor XIIIa
    • Johnson, K., S. Hashimoto, M. Lotz, K. Pritzker & R. Terkeltaub. Interleukin-1 induces pro-mineralizing activity of cartilage tissue transglutaminase and factor XIIIa. Am. J. Pathol., 159, 149-163 (2001)
    • (2001) Am. J. Pathol. , vol.159 , pp. 149-163
    • Johnson, K.1    Hashimoto, S.2    Lotz, M.3    Pritzker, K.4    Terkeltaub, R.5
  • 92
    • 0033862956 scopus 로고    scopus 로고
    • Trans-glutaminase-mediated fibronectin multimerization in lung endothelial matrix in response to TNF-alpha
    • Chen, R., B. Gao, C. Huang, B. Olsen, R.F. Rotundo, F. Blumenstock & T.M. Saba. Trans-glutaminase-mediated fibronectin multimerization in lung endothelial matrix in response to TNF-alpha. Am. J. Physiol., 279, L161-L174 (2000)
    • (2000) Am. J. Physiol. , vol.279
    • Chen, R.1    Gao, B.2    Huang, C.3    Olsen, B.4    Rotundo, R.F.5    Blumenstock, F.6    Saba, T.M.7
  • 94
    • 0041816056 scopus 로고    scopus 로고
    • Opposing roles of Ras/Raf oncogenes and the MEK1/ERK signaling module in regulation of expression and adhesive function of surface transglutaminase
    • Akimov, S.S. & A.M. Belkin. Opposing roles of Ras/Raf oncogenes and the MEK1/ERK signaling module in regulation of expression and adhesive function of surface transglutaminase. J. Biol. Chem., 278, 35609-35619 (2003)
    • (2003) J. Biol. Chem. , vol.278 , pp. 35609-35619
    • Akimov, S.S.1    Belkin, A.M.2
  • 95
    • 0029088221 scopus 로고
    • The importance of the GTP-binding protein tissue transglutaminase in the regulation of cell cycle progression
    • Mian S., S. el Alaoui, J. Lawry, V. Gentile, P.J. Davies & M. Griffin. The importance of the GTP-binding protein tissue transglutaminase in the regulation of cell cycle progression. FEBS Lett., 370, 27-31 (1995)
    • (1995) FEBS Lett. , vol.370 , pp. 27-31
    • Mian, S.1    El Alaoui, S.2    Lawry, J.3    Gentile, V.4    Davies, P.J.5    Griffin, M.6
  • 96
    • 14544298333 scopus 로고    scopus 로고
    • Tissue transglutaminase (TG2) in cancer biology
    • Mangala, L.S. & K. Mehta. Tissue transglutaminase (TG2) in cancer biology. Prog. Exp. Tumor Res., 38, 125-138 (2005)
    • (2005) Prog. Exp. Tumor Res. , vol.38 , pp. 125-138
    • Mangala, L.S.1    Mehta, K.2
  • 97
    • 9744274000 scopus 로고    scopus 로고
    • Prognostic significance of tissue trans-glutaminase in drug resistant and metastatic breast cancer
    • Mehta, K., J. Fok, F.R. Miller, D. Koul & A.A. Sahin. Prognostic significance of tissue trans-glutaminase in drug resistant and metastatic breast cancer. Clin. Cancer Res., 10, 8068-8076 (2004)
    • (2004) Clin. Cancer Res. , vol.10 , pp. 8068-8076
    • Mehta, K.1    Fok, J.2    Miller, F.R.3    Koul, D.4    Sahin, A.A.5
  • 98
    • 0031760698 scopus 로고    scopus 로고
    • Extracellular matrix remodeling during morphogenesis
    • Werb, Z. & J.R. Chin. Extracellular matrix remodeling during morphogenesis. Ann. N. Y. Acad. Sci., 857, 110-118 (1998)
    • (1998) Ann. N. Y. Acad. Sci. , vol.857 , pp. 110-118
    • Werb, Z.1    Chin, J.R.2
  • 99
    • 21244446693 scopus 로고    scopus 로고
    • Proteolysis of cell-surface tissue transglutaminase by matrix metalloproteinase-2 contributes to the adhesive defect and matrix abnormalities in thrombospondin-2-null fibroblasts and mice
    • Agah, A., T.R. Kyriakides & P. Bornstein. Proteolysis of cell-surface tissue transglutaminase by matrix metalloproteinase-2 contributes to the adhesive defect and matrix abnormalities in thrombospondin-2-null fibroblasts and mice. Am. J. Pathol., 167, 81-88 (2005)
    • (2005) Am. J. Pathol. , vol.167 , pp. 81-88
    • Agah, A.1    Kyriakides, T.R.2    Bornstein, P.3
  • 101
  • 102
    • 0037107551 scopus 로고    scopus 로고
    • Fibronectin at a glance
    • Pankov, R. & K.M. Yamada. Fibronectin at a glance. J. Cell Sci., 115, 3861-3863 (2002)
    • (2002) J. Cell Sci. , vol.115 , pp. 3861-3863
    • Pankov, R.1    Yamada, K.M.2
  • 103
    • 0028978237 scopus 로고
    • A novel role for alpha3beta1 integrin in extracellular matrix assembly
    • Wu, C., A.E. Chung & J.A. McDonald. A novel role for alpha3beta1 integrin in extracellular matrix assembly. J. Cell Sci., 108, 2511-2523 (1995)
    • (1995) J. Cell Sci. , vol.108 , pp. 2511-2523
    • Wu, C.1    Chung, A.E.2    McDonald, J.A.3
  • 104
    • 0034092910 scopus 로고    scopus 로고
    • A novel RGD-independent fibronectin assembly pathway initiated by alpha4beta1 integrin binding to the alternatively spliced V region
    • Sechler, J.L., A.M. Cumiskey, D.M. Gazzola & J.E. Schwarzbauer. A novel RGD-independent fibronectin assembly pathway initiated by alpha4beta1 integrin binding to the alternatively spliced V region. J. Cell Sci., 113, 1491-1498 (2000)
    • (2000) J. Cell Sci. , vol.113 , pp. 1491-1498
    • Sechler, J.L.1    Cumiskey, A.M.2    Gazzola, D.M.3    Schwarzbauer, J.E.4
  • 105
    • 0028786294 scopus 로고
    • Integrin activation and cytoskeletal interaction are essential for the assembly of a fibronectin matrix
    • Wu, C., V.M. Keivens, T.E. O'Toole, J.A. McDonald & M.H. Ginsberg. Integrin activation and cytoskeletal interaction are essential for the assembly of a fibronectin matrix. Cell, 83, 715-724 1995.
    • (1995) Cell , vol.83 , pp. 715-724
    • Wu, C.1    Keivens, V.M.2    O'Toole, T.E.3    McDonald, J.A.4    Ginsberg, M.H.5
  • 106
    • 0024292679 scopus 로고
    • Site-directed mutagenesis of the cell-binding domain of human fibronectin: Separable, synergistic sites mediate adhesive function
    • Obara, M., M.S. Kang & K.M. Yamada. Site-directed mutagenesis of the cell-binding domain of human fibronectin: separable, synergistic sites mediate adhesive function. Cell, 53, 649-657 (1988)
    • (1988) Cell , vol.53 , pp. 649-657
    • Obara, M.1    Kang, M.S.2    Yamada, K.M.3
  • 107
    • 0028043949 scopus 로고
    • Fibronectin self-association is mediated by complementary sites within the amino-terminal one-third of the molecule
    • Aguirre, K.M., R.J. McCormick & J.E. Schwarzbauer. Fibronectin self-association is mediated by complementary sites within the amino-terminal one-third of the molecule. J. Biol. Chem., 269, 27863-27868 (1994)
    • (1994) J. Biol. Chem. , vol.269 , pp. 27863-27868
    • Aguirre, K.M.1    McCormick, R.J.2    Schwarzbauer, J.E.3
  • 108
    • 0037134508 scopus 로고    scopus 로고
    • Alternative splicing of the IIICS domain in fibronectin governs the role of the heparin II domain in fibrillogenesis and cell spreading
    • Santas, A.J., J.A. Peterson, J.L. Halbleib, S.E. Craig, M.J. Humphries & D.M. Peters. Alternative splicing of the IIICS domain in fibronectin governs the role of the heparin II domain in fibrillogenesis and cell spreading. J. Biol. Chem., 277, 13650-13658 (2002)
    • (2002) J. Biol. Chem. , vol.277 , pp. 13650-13658
    • Santas, A.J.1    Peterson, J.A.2    Halbleib, J.L.3    Craig, S.E.4    Humphries, M.J.5    Peters, D.M.6
  • 109
    • 0025730907 scopus 로고
    • Role of the I-9 and III-1 modules of fibronectin in formation of an extracellular matrix
    • Chernousov, M.A., F.J. Fogerty, V.E. Koteliansky & D.F. Mosher. Role of the I-9 and III-1 modules of fibronectin in formation of an extracellular matrix. J. Biol. Chem., 266, 10851-10858 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10851-10858
    • Chernousov, M.A.1    Fogerty, F.J.2    Koteliansky, V.E.3    Mosher, D.F.4
  • 110
    • 0026652898 scopus 로고
    • A fibronectin self-assembly site involved in fibronectin matrix assembly: Reconstruction with a synthetic peptide
    • Morla, A. & E. Ruoslahti. A fibronectin self-assembly site involved in fibronectin matrix assembly: reconstruction with a synthetic peptide. J. Cell Biol., 118, 421-433 (1992)
    • (1992) J. Cell Biol. , vol.118 , pp. 421-433
    • Morla, A.1    Ruoslahti, E.2
  • 111
    • 0029897753 scopus 로고    scopus 로고
    • A novel role for the integrin-binding III-10 module in fibronectin marix assembly
    • Hocking, D.C., R.K. Smith & P.J. McKeown-Longo. A novel role for the integrin-binding III-10 module in fibronectin marix assembly. J. Cell Biol., 133, 431-444 (1996)
    • (1996) J. Cell Biol. , vol.133 , pp. 431-444
    • Hocking, D.C.1    Smith, R.K.2    McKeown-Longo, P.J.3
  • 112
    • 0031036225 scopus 로고    scopus 로고
    • Cryptic self-association sites in type III modules of fibronectin
    • Ingham, K.C., S.A. Brew, S. Huff & S.V. Litvinovich. Cryptic self-association sites in type III modules of fibronectin. J. Biol. Chem., 272, 1718-1724 (1997)
    • (1997) J. Biol. Chem. , vol.272 , pp. 1718-1724
    • Ingham, K.C.1    Brew, S.A.2    Huff, S.3    Litvinovich, S.V.4
  • 113
    • 0028364087 scopus 로고
    • Fibronectin's III-1 module contains a conformation-dependent binding site for the amino-terminal region of fibronectin
    • Hocking, D.C., J. Sottile & P.J. McKeown-Longo. Fibronectin's III-1 module contains a conformation-dependent binding site for the amino-terminal region of fibronectin. J. Biol. Chem., 269, 19183-19191 (1994)
    • (1994) J. Biol. Chem. , vol.269 , pp. 19183-19191
    • Hocking, D.C.1    Sottile, J.2    McKeown-Longo, P.J.3
  • 114
    • 0032550177 scopus 로고    scopus 로고
    • Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly
    • Zhong, C., M. Chrzanowska-Wodnicka, J. Brown, A. Shaub, A.M. Belkin & K. Burridge. Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly. J. Cell Biol., 141, 539-551 (1998)
    • (1998) J. Cell Biol. , vol.141 , pp. 539-551
    • Zhong, C.1    Chrzanowska-Wodnicka, M.2    Brown, J.3    Shaub, A.4    Belkin, A.M.5    Burridge, K.6
  • 115
    • 0023791465 scopus 로고
    • Transforming growth factor beta increases cell surface binding and assembly of exogenous (plasma) fibronectin by normal human fibroblasts
    • Allen-Hoffmann, B.L., C.L. Crankshaw & D.F. Mosher. Transforming growth factor beta increases cell surface binding and assembly of exogenous (plasma) fibronectin by normal human fibroblasts. Mol. Cell. Biol., 8, 4234-4242 (1988)
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4234-4242
    • Allen-Hoffmann, B.L.1    Crankshaw, C.L.2    Mosher, D.F.3
  • 116
    • 0023926486 scopus 로고
    • Transforming growth factor beta stimulates the expression of fibronectin and both subunits of the human fibronectin receptor by cultured human lung fibroblasts
    • Roberts, C.J., T.M. Birkenmeier, J.J. McQuillan, S.K. Akiyama, S.S. Yamada, W.-T. Chen, K.M. Yamada & J.A. McDonald. Transforming growth factor beta stimulates the expression of fibronectin and both subunits of the human fibronectin receptor by cultured human lung fibroblasts. J. Biol. Chem., 263, 4586-4592 (1988)
    • (1988) J. Biol. Chem. , vol.263 , pp. 4586-4592
    • Roberts, C.J.1    Birkenmeier, T.M.2    McQuillan, J.J.3    Akiyama, S.K.4    Yamada, S.S.5    Chen, W.-T.6    Yamada, K.M.7    McDonald, J.A.8
  • 117
    • 1642506297 scopus 로고    scopus 로고
    • Down-regulation of Hox A7 is required for cell adhesion and migration on fibronectin during early HL-60 monocytic differentiation
    • Leroy, P., F. Berto, I. Bourget and B. Rossi. Down-regulation of Hox A7 is required for cell adhesion and migration on fibronectin during early HL-60 monocytic differentiation. J. Leukoc. Biol., 75, 680-688 (2004)
    • (2004) J. Leukoc. Biol. , vol.75 , pp. 680-688
    • Leroy, P.1    Berto, F.2    Bourget, I.3    Rossi, B.4
  • 118
    • 0037053359 scopus 로고    scopus 로고
    • Analysis of tissue transglutaminase function in the migration of Swiss 3T3 fibroblasts: The active-state conformation of the enzyme does not affect cell motility but is important for its secretion
    • Balklava, Z., E. Verderio, R. Collighan, S. Gross, J. Adams & M. Griffin. Analysis of tissue transglutaminase function in the migration of Swiss 3T3 fibroblasts: the active-state conformation of the enzyme does not affect cell motility but is important for its secretion. J. Biol. Chem., 277, 16567-16575 (2002)
    • (2002) J. Biol. Chem. , vol.277 , pp. 16567-16575
    • Balklava, Z.1    Verderio, E.2    Collighan, R.3    Gross, S.4    Adams, J.5    Griffin, M.6
  • 119
    • 0042834268 scopus 로고    scopus 로고
    • Identification of tissue transglutaminase as a novel molecule involved in human CD8(+) T cell transendothelial migration
    • Mohan, K., D. Pinto & T.B. Issekutz. Identification of tissue transglutaminase as a novel molecule involved in human CD8(+) T cell transendothelial migration. J. Immunol., 171, 3179-3186 (2003)
    • (2003) J. Immunol. , vol.171 , pp. 3179-3186
    • Mohan, K.1    Pinto, D.2    Issekutz, T.B.3
  • 120
    • 0030450884 scopus 로고    scopus 로고
    • Tissue transglutaminase and factor XIII in cartilage and bone remodeling
    • Aeschlimann, D., D. Mosher & M. Paulsson. Tissue transglutaminase and factor XIII in cartilage and bone remodeling. Semin. Thromb. Haemost., 22, 437-443 (1996)
    • (1996) Semin. Thromb. Haemost. , vol.22 , pp. 437-443
    • Aeschlimann, D.1    Mosher, D.2    Paulsson, M.3
  • 121
    • 17444392120 scopus 로고    scopus 로고
    • Fibrinogen and fibrin
    • Weisel, J.W. Fibrinogen and fibrin. Adv. Protein Chem., 70, 247-299 (2005)
    • (2005) Adv. Protein Chem. , vol.70 , pp. 247-299
    • Weisel, J.W.1
  • 122
    • 21444451809 scopus 로고    scopus 로고
    • The galectin family of proteins
    • Horie, H. The galectin family of proteins. Curr. Drug Targets, 6, 373-374 (2005)
    • (2005) Curr. Drug Targets , vol.6 , pp. 373-374
    • Horie, H.1
  • 123
    • 0031740228 scopus 로고    scopus 로고
    • Transglutaminase-mediated oligomerization of galectin-3 modulates human melanoma cell interactions with laminin
    • van der Brule, F.A., F.T. Liu and V. Castronovo. Transglutaminase- mediated oligomerization of galectin-3 modulates human melanoma cell interactions with laminin. Cell Adhes. Commun., 5, 425-435 (1998)
    • (1998) Cell Adhes. Commun. , vol.5 , pp. 425-435
    • Van Der Brule, F.A.1    Liu, F.T.2    Castronovo, V.3
  • 124
    • 18244399091 scopus 로고    scopus 로고
    • Transglutaminase-mediated oligomerization of the fibrin(ogen) {alpha}C-domains promotes integrin-dependent cell adhesion and signaling
    • Belkin, A.M., G. Tsurupa, E. Zemskov, Y. Veklich, J.W. Weisel & L. Medved. Transglutaminase-mediated oligomerization of the fibrin(ogen) {alpha}C-domains promotes integrin-dependent cell adhesion and signaling. Blood, 105, 3561-3568 (2005)
    • (2005) Blood , vol.105 , pp. 3561-3568
    • Belkin, A.M.1    Tsurupa, G.2    Zemskov, E.3    Veklich, Y.4    Weisel, J.W.5    Medved, L.6
  • 125
    • 4344669555 scopus 로고    scopus 로고
    • Alpha1B-adrenoceptor signaling and cell motility: GTPase function of Gh/transglutaminase 2 inhibits cell migration through interaction with cytoplasmic tail of integrin alpha subunits
    • Kang, S.K., K.S. Yi, N.S. Kwon, K.H. Park, U.H. Kim, K.J. Baek & M.J. Im. Alpha1B-adrenoceptor signaling and cell motility: GTPase function of Gh/transglutaminase 2 inhibits cell migration through interaction with cytoplasmic tail of integrin alpha subunits. J. Biol. Chem., 279, 36593-36600 (2004)
    • (2004) J. Biol. Chem. , vol.279 , pp. 36593-36600
    • Kang, S.K.1    Yi, K.S.2    Kwon, N.S.3    Park, K.H.4    Kim, U.H.5    Baek, K.J.6    Im, M.J.7
  • 128
    • 0034747685 scopus 로고    scopus 로고
    • Gene disruption of tissue transglutaminase
    • De Laurenzi, V., & G. Melino. Gene disruption of tissue transglutaminase. Mol. Cell. Biol., 21, 148-155 (2001)
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 148-155
    • De Laurenzi, V.1    Melino, G.2
  • 129
    • 4143089161 scopus 로고    scopus 로고
    • Tissue transglutaminase in normal and abnormal wound healing
    • Verderio, E.A., M.T. Johnson & M. Griffin. Tissue transglutaminase in normal and abnormal wound healing. Amino Acids, 26, 387-404 (2004)
    • (2004) Amino Acids , vol.26 , pp. 387-404
    • Verderio, E.A.1    Johnson, M.T.2    Griffin, M.3


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