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Volumn 38, Issue , 2005, Pages 19-36

Structure-function relationships of transglutaminases - A contemporary view

Author keywords

[No Author keywords available]

Indexed keywords

ISOENZYME; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE;

EID: 14544290552     PISSN: 00796263     EISSN: None     Source Type: Book Series    
DOI: 10.1159/000084231     Document Type: Review
Times cited : (12)

References (44)
  • 2
    • 0025195721 scopus 로고
    • Localization of ε-lysyl-γ-glutamyl cross-links in five human α2-macroglobulin-proteinase complexes. Nature of the high molecular weight cross-linked products
    • Sottrup-Jensen L, Hansen HF, Pedersen HS, Kristensen L: Localization of ε-lysyl-γ-glutamyl cross-links in five human α2-macroglobulin- proteinase complexes. Nature of the high molecular weight cross-linked products. J Biol Chem 1990;265:17727-17737.
    • (1990) J Biol Chem , vol.265 , pp. 17727-17737
    • Sottrup-Jensen, L.1    Hansen, H.F.2    Pedersen, H.S.3    Kristensen, L.4
  • 4
    • 0345505270 scopus 로고    scopus 로고
    • Thioredoxin motif of Caenorhabditis elegans PDI-3 provides Cys and His catalytic residues for transglutaminase activity
    • Blaskó B, Mádi A, Fésüs L: Thioredoxin motif of Caenorhabditis elegans PDI-3 provides Cys and His catalytic residues for transglutaminase activity. Biochem Biophys Res Commun 2003; 303:1142-1147.
    • (2003) Biochem Biophys Res Commun , vol.303 , pp. 1142-1147
    • Blaskó, B.1    Mádi, A.2    Fésüs, L.3
  • 5
    • 0036134815 scopus 로고    scopus 로고
    • Transglutaminase: Remembering Heinrich Waelsch
    • Lorand L: Transglutaminase: Remembering Heinrich Waelsch. Neurochem Int 2002;40:7-12.
    • (2002) Neurochem Int , vol.40 , pp. 7-12
    • Lorand, L.1
  • 6
    • 0017680149 scopus 로고
    • The ε-(-γ-glutamyl)lysine crosslink and the catalytic role of transglutaminases
    • Folk JE, Finlayson JS: The ε-(-γ-glutamyl)lysine crosslink and the catalytic role of transglutaminases. Adv Protein Chem 1977;31:1-133.
    • (1977) Adv Protein Chem , vol.31 , pp. 1-133
    • Folk, J.E.1    Finlayson, J.S.2
  • 7
    • 0014940829 scopus 로고
    • Mechanism of action of guinea pig liver transglutaminase. VII. Chemical and stereochemical aspects of substrate binding and catalysis
    • Chung SI, Shrager RI, Folk JE: Mechanism of action of guinea pig liver transglutaminase. VII. Chemical and stereochemical aspects of substrate binding and catalysis. J Biol Chem 1970;245: 6424-6435.
    • (1970) J Biol Chem , vol.245 , pp. 6424-6435
    • Chung, S.I.1    Shrager, R.I.2    Folk, J.E.3
  • 8
    • 0033256583 scopus 로고    scopus 로고
    • Human prostate-specific transglutaminase gene: Promoter cloning, tissue-specific expression, and down-regulation in metastatic prostate cancer
    • An G, Meka CS, Bright SP, Veltri RW: Human prostate-specific transglutaminase gene: Promoter cloning, tissue-specific expression, and down-regulation in metastatic prostate cancer. Urology 1999;54:1105-1111.
    • (1999) Urology , vol.54 , pp. 1105-1111
    • An, G.1    Meka, C.S.2    Bright, S.P.3    Veltri, R.W.4
  • 11
    • 1342304083 scopus 로고    scopus 로고
    • Structural basis for the coordinated regulation of transglutaminase 3 by guanine nucleotides and calcium/magnesium
    • Ahvazi B, Boeshans KM, Idler W, Baxa U, Steinert PM, Rastinejad F: Structural basis for the coordinated regulation of transglutaminase 3 by guanine nucleotides and calcium/magnesium. J Biol Chem 2004;279:7180-7192.
    • (2004) J Biol Chem , vol.279 , pp. 7180-7192
    • Ahvazi, B.1    Boeshans, K.M.2    Idler, W.3    Baxa, U.4    Steinert, P.M.5    Rastinejad, F.6
  • 12
    • 0037411143 scopus 로고    scopus 로고
    • N-terminus end of rat prostate transglutaminase is responsible for its catalytic activity and GTP binding
    • Mariniello L, Esposito C, Caputo I, Sorrentino A, Porta R: N-terminus end of rat prostate transglutaminase is responsible for its catalytic activity and GTP binding. Int J Biochem Cell Biol 2003;35:1098-1108.
    • (2003) Int J Biochem Cell Biol , vol.35 , pp. 1098-1108
    • Mariniello, L.1    Esposito, C.2    Caputo, I.3    Sorrentino, A.4    Porta, R.5
  • 13
    • 0038606434 scopus 로고    scopus 로고
    • Roles of calcium ions in the activation and activity of the transglutaminase 3 enzyme
    • Ahvazi B, Boeshans KM, Idler W, Baxa U, Steinert PM: Roles of calcium ions in the activation and activity of the transglutaminase 3 enzyme. J Biol Chem 2003;278:23834-23841.
    • (2003) J Biol Chem , vol.278 , pp. 23834-23841
    • Ahvazi, B.1    Boeshans, K.M.2    Idler, W.3    Baxa, U.4    Steinert, P.M.5
  • 14
    • 0033620472 scopus 로고    scopus 로고
    • Bricks and mortar of the epidermal barrier
    • Nemes Z, Steinert PM: Bricks and mortar of the epidermal barrier. Exp Mol Med 1999;31:5-19.
    • (1999) Exp Mol Med , vol.31 , pp. 5-19
    • Nemes, Z.1    Steinert, P.M.2
  • 15
    • 0033587684 scopus 로고    scopus 로고
    • A novel function for transglutaminase 1: Attachment of long-chain ω-hydroxyceramides to involucrin by ester bond formation
    • USA
    • Nemes Z, Marekov LN, Fésüs L, Steinert PM: A novel function for transglutaminase 1: Attachment of long-chain ω-hydroxyceramides to involucrin by ester bond formation. Proc Natl Acad Sci USA 1999;96:8402-8407.
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 8402-8407
    • Nemes, Z.1    Marekov, L.N.2    Fésüs, L.3    Steinert, P.M.4
  • 16
    • 0037022619 scopus 로고    scopus 로고
    • Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity
    • USA
    • Liu S, Cerione RA, Clardy J: Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity. Proc Natl Acad Sci USA 2002; 99:2743-2747.
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 2743-2747
    • Liu, S.1    Cerione, R.A.2    Clardy, J.3
  • 18
    • 18744421735 scopus 로고    scopus 로고
    • Two non-proline cis peptide bonds may be important for factor XIII function
    • Weiss MS, Metzner HJ, Hilgenfeld R: Two non-proline cis peptide bonds may be important for factor XIII function. FEBS Lett 1998;423:291-296.
    • (1998) FEBS Lett , vol.423 , pp. 291-296
    • Weiss, M.S.1    Metzner, H.J.2    Hilgenfeld, R.3
  • 19
    • 0036565662 scopus 로고    scopus 로고
    • Three-dimensional structure of the human transglutaminase 3 enzyme: Binding of calcium ions changes structure for activation
    • Ahvazi B, Kim HC, Kee SH, Nemes Z, Steinert PM: Three-dimensional structure of the human transglutaminase 3 enzyme: Binding of calcium ions changes structure for activation. EMBO J 2002;21:2055-2067.
    • (2002) EMBO J , vol.21 , pp. 2055-2067
    • Ahvazi, B.1    Kim, H.C.2    Kee, S.H.3    Nemes, Z.4    Steinert, P.M.5
  • 20
    • 2942705910 scopus 로고    scopus 로고
    • Crystal structure of transglutaminase 3 in complex with GMP: Structural basis for nucleotide specificity
    • Ahvazi B, Boeshans KM, Steinert PM: Crystal structure of transglutaminase 3 in complex with GMP: Structural basis for nucleotide specificity. J Biol Chem 2004;279:26716-26725.
    • (2004) J Biol Chem , vol.279 , pp. 26716-26725
    • Ahvazi, B.1    Boeshans, K.M.2    Steinert, P.M.3
  • 22
    • 0029856983 scopus 로고    scopus 로고
    • C-terminal deletion of human tissue transglutaminase enhances magnesium-dependent GTP/ATPase activity
    • Lai TS, Slaughter TF, Koropchak CM, Haroon ZA, Greenberg CS: C-terminal deletion of human tissue transglutaminase enhances magnesium-dependent GTP/ATPase activity. J Biol Chem 1996;271:31191-31195.
    • (1996) J Biol Chem , vol.271 , pp. 31191-31195
    • Lai, T.S.1    Slaughter, T.F.2    Koropchak, C.M.3    Haroon, Z.A.4    Greenberg, C.S.5
  • 23
    • 0037022557 scopus 로고    scopus 로고
    • Conserved tryptophan in the core domain of transglutaminase is essential for catalytic activity
    • USA
    • Murthy SN, Iismaa S, Begg G, Freymann DM, Graham RM, Lorand L: Conserved tryptophan in the core domain of transglutaminase is essential for catalytic activity. Proc Natl Acad Sci USA 2002;99:2738-2742.
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 2738-2742
    • Murthy, S.N.1    Iismaa, S.2    Begg, G.3    Freymann, D.M.4    Graham, R.M.5    Lorand, L.6
  • 24
    • 0141850279 scopus 로고    scopus 로고
    • A model for the reaction mechanism of the transglutaminase 3 enzyme
    • Ahvazi B, Steinert PM: A model for the reaction mechanism of the transglutaminase 3 enzyme. Exp Mol Med 2003;35:228-242.
    • (2003) Exp Mol Med , vol.35 , pp. 228-242
    • Ahvazi, B.1    Steinert, P.M.2
  • 26
  • 27
    • 0034046724 scopus 로고    scopus 로고
    • Ligand-induced conformational changes in tissue transglutaminase: Monte Carlo analysis of small-angle scattering data
    • Mariani P, Carsughi F, Spinozzi F, Romanzetti S, Meier G, Casadio R, Bergamini CM: Ligand-induced conformational changes in tissue transglutaminase: Monte Carlo analysis of small-angle scattering data. Biophys J 2000;78:3240-3251.
    • (2000) Biophys J , vol.78 , pp. 3240-3251
    • Mariani, P.1    Carsughi, F.2    Spinozzi, F.3    Romanzetti, S.4    Meier, G.5    Casadio, R.6    Bergamini, C.M.7
  • 28
    • 0023733194 scopus 로고
    • GTP modulates calcium binding and cation-induced conformational changes in erythrocyte transglutaminase
    • Bergamini CM: GTP modulates calcium binding and cation-induced conformational changes in erythrocyte transglutaminase. FEBS Lett 1988;239:255-258.
    • (1988) FEBS Lett , vol.239 , pp. 255-258
    • Bergamini, C.M.1
  • 30
    • 0028964517 scopus 로고
    • Site-directed mutation in conserved anionic regions of guinea pig liver transglutaminase
    • Ikura K, Yu C, Nagao M, Sasaki R, Furuyoshi S, Kawabata N: Site-directed mutation in conserved anionic regions of guinea pig liver transglutaminase. Arch Biochem Biophys 1995;318:307-313.
    • (1995) Arch Biochem Biophys , vol.318 , pp. 307-313
    • Ikura, K.1    Yu, C.2    Nagao, M.3    Sasaki, R.4    Furuyoshi, S.5    Kawabata, N.6
  • 32
    • 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, Verderio E, Collighan R, Gross S, Adams J, Griffin M: 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 2002;277: 16567-16575.
    • (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
  • 33
    • 2942575057 scopus 로고    scopus 로고
    • The emerging structural understanding of transglutaminase 3
    • Ahvazi B, Boeshans KM, Rastinejad F: The emerging structural understanding of transglutaminase 3. J Struct Biol 2004;147:200-207.
    • (2004) J Struct Biol , vol.147 , pp. 200-207
    • Ahvazi, B.1    Boeshans, K.M.2    Rastinejad, F.3
  • 37
    • 0033578417 scopus 로고    scopus 로고
    • Calreticulin down-regulates both GTP binding and transglutaminase activities of transglutaminase II
    • Feng JF, Readon M, Yadav SP, Im MJ: Calreticulin down-regulates both GTP binding and transglutaminase activities of transglutaminase II. Biochemistry 1999;38:10743-10749.
    • (1999) Biochemistry , vol.38 , pp. 10743-10749
    • Feng, J.F.1    Readon, M.2    Yadav, S.P.3    Im, M.J.4
  • 39
    • 0033573849 scopus 로고    scopus 로고
    • 1B-adrenoceptor interacts with multiple sites of transglutaminase II: Characteristics of the interaction in binding and activation
    • 1B-adrenoceptor interacts with multiple sites of transglutaminase II: Characteristics of the interaction in binding and activation. Biochemistry 1999;38:2224-2232.
    • (1999) Biochemistry , vol.38 , pp. 2224-2232
    • Feng, J.F.1    Gray, C.D.2    Im, M.J.3
  • 40
    • 0034674770 scopus 로고    scopus 로고
    • GTP binding and signaling by Gh/ transglutaminase II involves distinct residues in a unique GTP-binding pocket
    • Iismaa SE, Wu MJ, Nanda N, Church WB, Graham RM: GTP binding and signaling by Gh/ transglutaminase II involves distinct residues in a unique GTP-binding pocket. J Biol Chem 2000;275:18259-18265.
    • (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
  • 42
    • 0034695929 scopus 로고    scopus 로고
    • Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin
    • Akimov SS, Krylov D, Fleischman LF, Belkin AM: Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin. J Cell Biol 2000;148:825-838.
    • (2000) J Cell Biol , vol.148 , pp. 825-838
    • Akimov, S.S.1    Krylov, D.2    Fleischman, L.F.3    Belkin, A.M.4
  • 43
    • 0034839336 scopus 로고    scopus 로고
    • Cell-surface transglutaminase promotes fibronectin assembly via interaction with the gelatin-binding domain of fibronectin: A role in TGFβ-dependent matrix deposition
    • Akimov SS, Belkin AM: Cell-surface transglutaminase promotes fibronectin assembly via interaction with the gelatin-binding domain of fibronectin: A role in TGFβ-dependent matrix deposition. J Cell Sci 2001;114:2989-3000.
    • (2001) J Cell Sci , vol.114 , pp. 2989-3000
    • Akimov, S.S.1    Belkin, A.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.