메뉴 건너뛰기




Volumn 109, Issue 11, 1996, Pages 2727-2735

Dual functions of transglutaminase in novel cell adhesion

Author keywords

Blood coagulation factor XIIIa; Cell adhesion; Integrin; Transglutaminase

Indexed keywords

BLOOD CLOTTING FACTOR 13A; CYSTEINE; INTEGRIN; IODOACETAMIDE; POLYCLONAL ANTIBODY; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE;

EID: 0029859391     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (58)

References (37)
  • 1
    • 0028322985 scopus 로고
    • Transglutaminases: Protein cross-linking enzymes in tissues and body fluids
    • Aeschlimann, D. and Paulsson, M. (1994). Transglutaminases: Protein cross-linking enzymes in tissues and body fluids. Thromb. Haemost. 71, 402-415.
    • (1994) Thromb. Haemost. , vol.71 , pp. 402-415
    • Aeschlimann, D.1    Paulsson, M.2
  • 3
    • 0025328948 scopus 로고
    • Binding and degradation of blood coagulation factor XIII by cultured fibroblasts
    • Barry, E. L. and Mosher, D. F. (1990). Binding and degradation of blood coagulation factor XIII by cultured fibroblasts. J. Biol. Chem. 265, 9302-9307.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9302-9307
    • Barry, E.L.1    Mosher, D.F.2
  • 4
    • 0015951526 scopus 로고
    • Relationships of the catalytic properties of human plasma and platelet transglutaminases (activated blood coagulation factor FXIII) to their subunit structures
    • Chung, S. I., Lewis, M. S. and Folk, J. E. (1974). Relationships of the catalytic properties of human plasma and platelet transglutaminases (activated blood coagulation factor FXIII) to their subunit structures. J. Biol. Chem. 249, 940-950.
    • (1974) J. Biol. Chem. , vol.249 , pp. 940-950
    • Chung, S.I.1    Lewis, M.S.2    Folk, J.E.3
  • 5
    • 0024321318 scopus 로고
    • Collagen-platelet interaction; evidence for a direct interaction of collagen with platelet GPIIbIIIa and an indirect interaction with platelet GPIIbIIIa mediated by adhesion protein
    • Collar, B. S., Beer, J. H., Scudder, L. E. and Steingberg, M. H. (1989). Collagen-platelet interaction; evidence for a direct interaction of collagen with platelet GPIIbIIIa and an indirect interaction with platelet GPIIbIIIa mediated by adhesion protein. Blood 74, 182-192.
    • (1989) Blood , vol.74 , pp. 182-192
    • Collar, B.S.1    Beer, J.H.2    Scudder, L.E.3    Steingberg, M.H.4
  • 6
    • 0028085243 scopus 로고
    • Factor XIIIa binding to activated platelets is mediated through activation of glycoprotein IIb-IIIa
    • Cox, A. D. and Devine, V. D. (1994). Factor XIIIa binding to activated platelets is mediated through activation of glycoprotein IIb-IIIa. Blood 83, 1006-1016.
    • (1994) Blood , vol.83 , pp. 1006-1016
    • Cox, A.D.1    Devine, V.D.2
  • 7
    • 0016267498 scopus 로고
    • Calcium-dependent unmasking of active center cysteine during activation of fibrin stabilizing factor
    • Curtis, C. G., Brown, K. L., Credo, R. B., Domanik, R. A., Gray, A., Stenberg, P. and Lorand, L. (1974). Calcium-dependent unmasking of active center cysteine during activation of fibrin stabilizing factor. Biochemistry 13, 3774-3780.
    • (1974) Biochemistry , vol.13 , pp. 3774-3780
    • Curtis, C.G.1    Brown, K.L.2    Credo, R.B.3    Domanik, R.A.4    Gray, A.5    Stenberg, P.6    Lorand, L.7
  • 8
    • 0015498627 scopus 로고
    • Documentation of the plasma factor XIII deficiency in man
    • Duckert, F. (1972). Documentation of the plasma factor XIII deficiency in man. Ann. NY Acad. Sci. 202, 190-199.
    • (1972) Ann. NY Acad. Sci. , vol.202 , pp. 190-199
    • Duckert, F.1
  • 9
    • 0028455060 scopus 로고
    • Recovery of visual response of injured adult rat optic nerves treated with transglutamirase
    • Eitan, S., Solomon, A., Lavie, V., Voles, E., Hirschberg, D. L., Belkin, M. and Schwartz, M. (1994). Recovery of visual response of injured adult rat optic nerves treated with transglutamirase. Science 264, 1764-1768.
    • (1994) Science , vol.264 , pp. 1764-1768
    • Eitan, S.1    Solomon, A.2    Lavie, V.3    Voles, E.4    Hirschberg, D.L.5    Belkin, M.6    Schwartz, M.7
  • 10
    • 0026020583 scopus 로고
    • Receptor function for the integrin VLA-3. Fibronectin, collagen, and limitation binding are differentially influenced by Arg-GLY-ASP peptide and by divalent actions
    • Elices, M. J., Urry, L. A. and Helmer, M. E. (1991). Receptor function for the integrin VLA-3. Fibronectin, collagen, and limitation binding are differentially influenced by Arg-GLY-ASP peptide and by divalent actions. J. Cell Biol. 112, 168-181.
    • (1991) J. Cell Biol. , vol.112 , pp. 168-181
    • Elices, M.J.1    Urry, L.A.2    Helmer, M.E.3
  • 11
    • 0023048837 scopus 로고
    • Transglutaminase-sensitive glutamine residues of human plasma fibronectin revealed by studying its proteolytic fragment
    • Fesus, L., Metsis, M. L., Muszbek, L. and Koteliansky, V. E. (1986). Transglutaminase-sensitive glutamine residues of human plasma fibronectin revealed by studying its proteolytic fragment. Eur. J. Biochem. 154, 371-374.
    • (1986) Eur. J. Biochem. , vol.154 , pp. 371-374
    • Fesus, L.1    Metsis, M.L.2    Muszbek, L.3    Koteliansky, V.E.4
  • 12
    • 0017680149 scopus 로고
    • ε-(γ-glutamyl)lysine cross-link and the catalytic role of transglutaminases
    • Folk, J. E. and Finlayson, J. S. (1977). ε-(γ-glutamyl)lysine cross-link and the catalytic role of transglutaminases. Advan. Prot. Chem. 31, 1-133.
    • (1977) Advan. Prot. Chem. , vol.31 , pp. 1-133
    • Folk, J.E.1    Finlayson, J.S.2
  • 13
    • 0042524714 scopus 로고
    • Methods for investigating the essential groups for enzyme activity
    • Fraenkel-Conrat, H. (1957). Methods for investigating the essential groups for enzyme activity. Meth. Enzymol. 4, 247-269.
    • (1957) Meth. Enzymol. , vol.4 , pp. 247-269
    • Fraenkel-Conrat, H.1
  • 14
    • 0026338017 scopus 로고
    • Transglutaminases: Multifunctional cross-linking enzymes that stabilize tissues
    • Greenberg, C. S., Birckbichler, P. J. and Rice, R. H. (1991). Transglutaminases: multifunctional cross-linking enzymes that stabilize tissues. FASEB J. 5, 3071-3077.
    • (1991) FASEB J. , vol.5 , pp. 3071-3077
    • Greenberg, C.S.1    Birckbichler, P.J.2    Rice, R.H.3
  • 15
    • 0026770377 scopus 로고
    • Integrin: Versatility, modulation, and signaling in cell adhesion
    • Hynes, R. O. (1992). Integrin: Versatility, modulation, and signaling in cell adhesion. Cell 69, 11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 16
    • 0023803842 scopus 로고
    • Primary structure of human coagulation factor XIII
    • Ichinose, A. and Davie, E. W. (1988). Primary structure of human coagulation factor XIII. Advan. Exp. Med. Biol. 231, 15-27.
    • (1988) Advan. Exp. Med. Biol. , vol.231 , pp. 15-27
    • Ichinose, A.1    Davie, E.W.2
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0027972994 scopus 로고
    • Integrin-mediated cell adhesion: The extracellular face
    • Luftus, J. C., Smith, J. W. and Ginsberg, M. H. (1994). Integrin-mediated cell adhesion: the extracellular face. J. Biol. Chem. 269, 25235-25238.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25235-25238
    • Luftus, J.C.1    Smith, J.W.2    Ginsberg, M.H.3
  • 21
    • 0017168643 scopus 로고
    • Affinity chromatography of human plasma and platelet Factor XIII on organomercurial agarose
    • McDonagh, J., Waggonar, W. G., Hamilton, E. G., Hindenach, B. and McDonagh, R. P. (1976). Affinity chromatography of human plasma and platelet Factor XIII on organomercurial agarose. Biochim. Biophys. Acta 446, 345-357.
    • (1976) Biochim. Biophys. Acta , vol.446 , pp. 345-357
    • McDonagh, J.1    Waggonar, W.G.2    Hamilton, E.G.3    Hindenach, B.4    McDonagh, R.P.5
  • 22
    • 0026730043 scopus 로고
    • Requirement for VLA-4 and VLA-5 integrins in lymphoma cells binding to and migration beneath stromal cells in culture
    • Miyake, K., Hasunuma, Y., Yagata, H. and Kimoto, M. (1992). Requirement for VLA-4 and VLA-5 integrins in lymphoma cells binding to and migration beneath stromal cells in culture. J. Cell Biol. 119, 653-662.
    • (1992) J. Cell Biol. , vol.119 , pp. 653-662
    • Miyake, K.1    Hasunuma, Y.2    Yagata, H.3    Kimoto, M.4
  • 24
    • 0021331433 scopus 로고
    • Cross-linking of fibronectin to collagenous proteins
    • Mosher, D. F. (1984). Cross-linking of fibronectin to collagenous proteins. Mol. Cell. Biochem. 58, 63-68.
    • (1984) Mol. Cell. Biochem. , vol.58 , pp. 63-68
    • Mosher, D.F.1
  • 26
    • 0022408228 scopus 로고
    • Purification of the catalytically active phosphorylated form of insulin receptor kinase by affinity chromatography with o-phosphotyrosyl-binding antibodies
    • Pang, D.T., Sharma, B.R. and Shafer, J.A. (1985). Purification of the catalytically active phosphorylated form of insulin receptor kinase by affinity chromatography with o-phosphotyrosyl-binding antibodies. Arch. Biochem. Biophys. 242, 176-186.
    • (1985) Arch. Biochem. Biophys. , vol.242 , pp. 176-186
    • Pang, D.T.1    Sharma, B.R.2    Shafer, J.A.3
  • 27
    • 0025895928 scopus 로고
    • Osteopontin, a substrate for transglutaminase and factor XIII activity
    • Prince, C. W., Dickie, D. and Krumdieck, C. L. (1991). Osteopontin, a substrate for transglutaminase and factor XIII activity. Biochem. Biophys. Res. Commun. 177, 1205-1210.
    • (1991) Biochem. Biophys. Res. Commun. , vol.177 , pp. 1205-1210
    • Prince, C.W.1    Dickie, D.2    Krumdieck, C.L.3
  • 29
    • 0025735355 scopus 로고
    • Immunoelectrophoretic characterizations of the cross-linking of fibrinogen and fibrin by factor XIIIa and tissue transglutaminase. Identification of a rapid mode of hybrid α-γ-chain cross-linking that is promoted by the γ-chain cross-linking
    • Shainoff, J. R., Urbanic, D. A. and DiBello, P. M. (1991). Immunoelectrophoretic characterizations of the cross-linking of fibrinogen and fibrin by factor XIIIa and tissue transglutaminase. Identification of a rapid mode of hybrid α-γ-chain cross-linking that is promoted by the γ-chain cross-linking. J. Biol. Chem. 266, 6429-6437.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6429-6437
    • Shainoff, J.R.1    Urbanic, D.A.2    DiBello, P.M.3
  • 30
    • 0023664709 scopus 로고
    • A complex of platelet glycoprotein Ic and IIa identified by a rat monoclonal antibody
    • Sonnenberg, A., Janssen, H., Hogernorit, F., Calafat, J. and Hilgers, J. (1987). A complex of platelet glycoprotein Ic and IIa identified by a rat monoclonal antibody. J. Biol. Chem. 262, 10376-10383.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10376-10383
    • Sonnenberg, A.1    Janssen, H.2    Hogernorit, F.3    Calafat, J.4    Hilgers, J.5
  • 31
    • 0022469265 scopus 로고
    • Modification of transglutaminase assay: Use of ammonium sulfate to stop the reaction
    • Takagi, J., Saito, Y., Kikuchi, T. and Inada, Y. (1986). Modification of transglutaminase assay: Use of ammonium sulfate to stop the reaction. Analyt. Biochem. 153, 295-298.
    • (1986) Analyt. Biochem. , vol.153 , pp. 295-298
    • Takagi, J.1    Saito, Y.2    Kikuchi, T.3    Inada, Y.4
  • 32
    • 0028177372 scopus 로고
    • β1-integrin-mediated adhesion of melanoma cells to the propolypeptide of von Willebrand factor
    • Takagi, J., Sudo, Y., Saito, T. and Saito, Y. (1994). β1-integrin-mediated adhesion of melanoma cells to the propolypeptide of von Willebrand factor. Eur. J. Biochem. 222, 861-867.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 861-867
    • Takagi, J.1    Sudo, Y.2    Saito, T.3    Saito, Y.4
  • 33
    • 0344053910 scopus 로고
    • Primary structure of blood coagulation factor FXIIIa (fibrinoligase, transglutaminase) from human placenta
    • Takahashi, N., Takahashi, Y. and Putnum, F. W. (1986). Primary structure of blood coagulation factor FXIIIa (fibrinoligase, transglutaminase) from human placenta. Proc. Nat. Acad. Sci. USA 83, 8019-8023.
    • (1986) Proc. Nat. Acad. Sci. USA , vol.83 , pp. 8019-8023
    • Takahashi, N.1    Takahashi, Y.2    Putnum, F.W.3
  • 34
    • 0025885719 scopus 로고
    • Localization of cellular transglutaminase on the extracellular matrix after wounding: Characteristics of the matrix bound enzyme
    • Upchurch, H. F., Conway, E., Patterson, M. K. J. and Maxwell, M. D. (1991). Localization of cellular transglutaminase on the extracellular matrix after wounding: characteristics of the matrix bound enzyme. J. Cell Physiol. 149, 375-382.
    • (1991) J. Cell Physiol. , vol.149 , pp. 375-382
    • Upchurch, H.F.1    Conway, E.2    Patterson, M.K.J.3    Maxwell, M.D.4
  • 35
    • 0027254197 scopus 로고
    • Propolypeptide of von Willebrand factor serves as a substrate for factor XIIIa and is cross-linked to laminin
    • Usui, T., Takagi, J. and Saito, Y. (1993). Propolypeptide of von Willebrand factor serves as a substrate for factor XIIIa and is cross-linked to laminin. J. Biol. Chem. 268, 12311-12316.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12311-12316
    • Usui, T.1    Takagi, J.2    Saito, Y.3
  • 36
    • 0023555151 scopus 로고
    • Identification of multiple cell adhesion receptors for collagen and fibronectin in human fibrosarcoma cells possessing unique and common β subunits
    • Wayner, E. A. and Carter, W. G. (1988). Identification of multiple cell adhesion receptors for collagen and fibronectin in human fibrosarcoma cells possessing unique and common β subunits. J. Cell Biol. 105, 1873-1884.
    • (1988) J. Cell Biol. , vol.105 , pp. 1873-1884
    • Wayner, E.A.1    Carter, W.G.2
  • 37
    • 0024335963 scopus 로고
    • Signal transduction through the fibronectin receptor induces collagenase and stromelysin gene expression
    • Werb, Z., Tremble, P. M., Behrendtsen, O., Cronley, E. and Damsky, C. H. (1989). Signal transduction through the fibronectin receptor induces collagenase and stromelysin gene expression. J. Cell Biol. 109, 877-889.
    • (1989) J. Cell Biol. , vol.109 , pp. 877-889
    • Werb, Z.1    Tremble, P.M.2    Behrendtsen, O.3    Cronley, E.4    Damsky, C.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.