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Volumn 78 1, Issue , 2011, Pages 197-246

Transglutaminase 2 at the crossroads between cell death and survival

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 2;

EID: 84856623167     PISSN: 0065258X     EISSN: None     Source Type: Book Series    
DOI: 10.1002/9781118105771.ch5     Document Type: Article
Times cited : (18)

References (274)
  • 1
    • 0017680149 scopus 로고
    • The epsilon-(gamma-glutamyl)lysine crosslink and the catalytic role of transglutaminases
    • Folk, J. E. and Finlayson, J. S. (1977) The epsilon-(gamma-glutamyl)lysine crosslink and the catalytic role of transglutaminases, Adv. Protein Chem. 31, 1.
    • (1977) Adv. Protein Chem. , vol.31 , pp. 1
    • Folk, J.E.1    Finlayson, J.S.2
  • 3
    • 0035980007 scopus 로고    scopus 로고
    • Evolution of transglutaminase genes: identification of a transglutaminase gene cluster on human chromosome 15q15. Structure of the gene encoding transglutaminase X and a novel gene family member, transglutaminase Z
    • Grenard, P., Bates, M. K., and Aeschlimann, D. (2001) Evolution of transglutaminase genes: identification of a transglutaminase gene cluster on human chromosome 15q15. Structure of the gene encoding transglutaminase X and a novel gene family member, transglutaminase Z, J. Biol. Chem. 276, 33066.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33066
    • Grenard, P.1    Bates, M.K.2    Aeschlimann, D.3
  • 4
    • 0032800014 scopus 로고    scopus 로고
    • A superfamily of archaeal, bacterial, and eukaryotic proteins homologous to animal transglutaminases
    • Makarova, K. S., Aravind, L., and Koonin, E. V. (1999) A superfamily of archaeal, bacterial, and eukaryotic proteins homologous to animal transglutaminases, Protein Sci. 8, 1714.
    • (1999) Protein Sci , vol.8 , pp. 1714
    • Makarova, K.S.1    Aravind, L.2    Koonin, E.V.3
  • 5
    • 0018574683 scopus 로고
    • Inhibition of blood coagulation factor XIIIa-mediated cross-linking between fibronectin and collagen by polyamines
    • Mosher, D. F., Schad, P. E., and Kleinman, H. K. (1979) Inhibition of blood coagulation factor XIIIa-mediated cross-linking between fibronectin and collagen by polyamines, J. Supramol. Struct. 11, 227.
    • (1979) J. Supramol. Struct. , vol.11 , pp. 227
    • Mosher, D.F.1    Schad, P.E.2    Kleinman, H.K.3
  • 6
    • 0028126640 scopus 로고
    • The structure of the transglutaminase 1 enzyme. Deletion cloning reveals domains that regulate its specific activity and substrate specificity
    • Kim, S. Y., Kim, I. G., Chung, S. I., and Steinert, P. M. (1994) The structure of the transglutaminase 1 enzyme. Deletion cloning reveals domains that regulate its specific activity and substrate specificity, J. Biol. Chem. 269, 27979.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27979
    • Kim, S.Y.1    Kim, I.G.2    Chung, S.I.3    Steinert, P.M.4
  • 7
    • 0017811219 scopus 로고
    • Relation of protein synthesis and transglutaminase activity to formation of the cross-linked envelope during terminal differentiation of the cultured human epidermal keratinocyte
    • Rice, R. H. and Green, H. (1978) Relation of protein synthesis and transglutaminase activity to formation of the cross-linked envelope during terminal differentiation of the cultured human epidermal keratinocyte, J. Cell Biol. 76, 705.
    • (1978) J. Cell Biol. , vol.76 , pp. 705
    • Rice, R.H.1    Green, H.2
  • 8
    • 0036804796 scopus 로고    scopus 로고
    • Transglutaminase 2 an enigmatic enzyme with diverse functions
    • Fesus, L. and Piacentini, M. (2002) Transglutaminase 2: an enigmatic enzyme with diverse functions, Trends Biochem. Sci. 27, 534.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 534
    • Fesus, L.1    Piacentini, M.2
  • 9
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: crosslinking enzymes with pleiotropic functions
    • Lorand, L. and Graham, R. M. (2003) Transglutaminases: crosslinking enzymes with pleiotropic functions, Nat. Rev. Mol. Cell Biol. 4, 140.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 140
    • Lorand, L.1    Graham, R.M.2
  • 10
    • 0030068095 scopus 로고    scopus 로고
    • The proximal promoter of the human transglutaminase 3 gene. Stratified squamous epithelialspecific expression in cultured cells is mediated by binding of Sp1 and ets transcription factors to a proximal promoter element
    • Lee, J. H., Jang, S. I., Yang, J. M., Markova, N. G., and Steinert, P. M. (1996) The proximal promoter of the human transglutaminase 3 gene. Stratified squamous epithelialspecific expression in cultured cells is mediated by binding of Sp1 and ets transcription factors to a proximal promoter element, J. Biol. Chem. 271, 4561.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4561
    • Lee, J.H.1    Jang, S.I.2    Yang, J.M.3    Markova, N.G.4    Steinert, P.M.5
  • 11
    • 0032143453 scopus 로고    scopus 로고
    • The human prostate-specific transglutaminase gene (TGM4): genomic organization, tissue-specific expression, and promoter characterization
    • Dubbink, H. J., De Waal, L., Van Haperen, R., Verkaik, N. S., Trapman, J., and Romijn, J. C. (1998) The human prostate-specific transglutaminase gene (TGM4): genomic organization, tissue-specific expression, and promoter characterization, Genomics 51, 434.
    • (1998) Genomics , vol.51 , pp. 434
    • Dubbink, H.J.1    De Waal, L.2    Van Haperen, R.3    Verkaik, N.S.4    Trapman, J.5    Romijn, J.C.6
  • 13
    • 0042624865 scopus 로고    scopus 로고
    • Differential expression of tissue transglutaminase protein in mouse ovarian follicle
    • Lee, C. J., Do, B. R., Lee, J. M., Song, K. W., Kang, J. S., and Park, M. H. (2003) Differential expression of tissue transglutaminase protein in mouse ovarian follicle, In Vivo 17, 235.
    • (2003) In Vivo , vol.17 , pp. 235
    • Lee, C.J.1    Do, B.R.2    Lee, J.M.3    Song, K.W.4    Kang, J.S.5    Park, M.H.6
  • 14
    • 0033562768 scopus 로고    scopus 로고
    • Transcription regulatory elements of the first intron control human transglutaminase type I gene expression in epidermal keratinocytes
    • Polakowska, R. R., Graf, B. A., Falciano, V., and LaCelle, P. (1999) Transcription regulatory elements of the first intron control human transglutaminase type I gene expression in epidermal keratinocytes, J. Cell Biochem. 73, 355.
    • (1999) J. Cell Biochem. , vol.73 , pp. 355
    • Polakowska, R.R.1    Graf, B.A.2    Falciano, V.3    LaCelle, P.4
  • 15
    • 0025065288 scopus 로고
    • A novel guanine nucleotide-binding protein coupled to the alpha 1-adrenergic receptor. I. Identification by photolabeling or membrane and ternary complex preparation
    • Im,M. J. and Graham, R.M. (1990) A novel guanine nucleotide-binding protein coupled to the alpha 1-adrenergic receptor. I. Identification by photolabeling or membrane and ternary complex preparation, J. Biol. Chem. 265, 18944.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18944
    • Im, M.J.1    Graham, R.M.2
  • 16
    • 0025010874 scopus 로고
    • A novel guanine nucleotide-binding protein coupled to the alpha 1-adrenergic receptor. II. Purification, characterization, and reconstitution
    • Im, M. J., Riek, R. P., and Graham, R. M. (1990) A novel guanine nucleotide-binding protein coupled to the alpha 1-adrenergic receptor. II. Purification, characterization, and reconstitution, J. Biol. Chem. 265, 18952.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18952
    • Im, M.J.1    Riek, R.P.2    Graham, R.M.3
  • 19
    • 0037022619 scopus 로고    scopus 로고
    • Structural basis for the guanine nucleotidebinding activity of tissue transglutaminase and its regulation of transamidation activity
    • Liu, S., Cerione, R. A., and Clardy, J. (2002) Structural basis for the guanine nucleotidebinding activity of tissue transglutaminase and its regulation of transamidation activity, Proc. Natl. Acad. Sci. U.S.A. 99, 2743.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 2743
    • Liu, S.1    Cerione, R.A.2    Clardy, J.3
  • 20
    • 0028176166 scopus 로고
    • Gh: a GTP-binding protein with transglutaminase activity and receptor signaling function
    • Nakaoka, H., Perez, D. M., Baek, K. J., Das, T., Husain, A., Misono, K., Im, M. J., and Graham, R. M. (1994) Gh: a GTP-binding protein with transglutaminase activity and receptor signaling function, Science 264, 1593.
    • (1994) Science , vol.264 , pp. 1593
    • 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
  • 21
    • 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. and Murphy, L. J. (2004) 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.
    • (2004) J. Biol. Chem. , vol.279 , pp. 23863
    • Mishra, S.1    Murphy, L.J.2
  • 22
    • 28444488402 scopus 로고    scopus 로고
    • The p53 oncoprotein is a substrate for tissue transglutaminase kinase activity
    • Mishra, S. and Murphy, L. J. (2006) The p53 oncoprotein is a substrate for tissue transglutaminase kinase activity, Biochem. Biophys. Res. Commun. 339, 726.
    • (2006) Biochem. Biophys. Res. Commun. , vol.339 , pp. 726
    • Mishra, S.1    Murphy, L.J.2
  • 26
    • 0029859391 scopus 로고    scopus 로고
    • Dual functions of transglutaminase in novel cell adhesion
    • Ueki, S., Takagi, J., and Saito, Y. (1996) Dual functions of transglutaminase in novel cell adhesion, J. Cell Sci. 109(Pt 11), 2727.
    • (1996) J. Cell Sci. , vol.109 , Issue.PT 11 , pp. 2727
    • Ueki, S.1    Takagi, J.2    Saito, Y.3
  • 27
    • 0023704687 scopus 로고
    • Transglutaminase-mediated cross-linking of proteins and cell ageing: the erythrocyte and lens models
    • Lorand, L. (1988) Transglutaminase-mediated cross-linking of proteins and cell ageing: the erythrocyte and lens models, Adv. Exp. Med. Biol. 231, 79.
    • (1988) Adv. Exp. Med. Biol. , vol.231 , pp. 79
    • Lorand, L.1
  • 29
    • 0033046453 scopus 로고    scopus 로고
    • Mapping and sequencing of the murine 'tissue' transglutaminase (Tgm2) gene: absence of mutations in MRLlpr/lpr mice
    • D'Amato, M., Iannicola, C., Monteriu, G., and Piacentini, M. (1999), Mapping and sequencing of the murine 'tissue' transglutaminase (Tgm2) gene: absence of mutations in MRLlpr/lpr mice, Cell Death Differ. 6, 216.
    • (1999) Cell Death Differ , vol.6 , pp. 216
    • D'Amato, M.1    Iannicola, C.2    Monteriu, G.3    Piacentini, M.4
  • 30
    • 0028220758 scopus 로고
    • The human tissue transglutaminase gene maps on chromosome 20q12 by in situ fluorescence hybridization
    • Gentile, V., Davies, P. J., and Baldini, A. (1994), The human tissue transglutaminase gene maps on chromosome 20q12 by in situ fluorescence hybridization, Genomics 20, 295.
    • (1994) Genomics , vol.20 , pp. 295
    • Gentile, V.1    Davies, P.J.2    Baldini, A.3
  • 31
    • 0030690093 scopus 로고    scopus 로고
    • Organization and structure of the human tissue transglutaminase gene
    • Fraij, B. M. and Gonzales, R. A. (1997), Organization and structure of the human tissue transglutaminase gene, Biochim. Biophys. Acta 1354, 65.
    • (1997) Biochim. Biophys. Acta , vol.1354 , pp. 65
    • Fraij, B.M.1    Gonzales, R.A.2
  • 32
    • 0026018479 scopus 로고
    • Isolation and characterization of cDNA clones to mouse macrophage and human endothelial cell tissue transglutaminases
    • Gentile, V., Saydak, M., Chiocca, E. A., Akande, O., Birckbichler, P. J., Lee, K. N., Stein, J. P., and Davies, P. J. (1991) Isolation and characterization of cDNA clones to mouse macrophage and human endothelial cell tissue transglutaminases, J. Biol. Chem. 266, 478.
    • (1991) J. Biol. Chem. , vol.266 , pp. 478
    • Gentile, V.1    Saydak, M.2    Chiocca, E.A.3    Akande, O.4    Birckbichler, P.J.5    Lee, K.N.6    Stein, J.P.7    Davies, P.J.8
  • 33
    • 0022976312 scopus 로고
    • Quantitation of tissue transglutaminase by a sandwich ELISA system
    • Fesus, L. and Arato, G. (1986), Quantitation of tissue transglutaminase by a sandwich ELISA system, J. Immunol. Methods 94, 131.
    • (1986) J. Immunol. Methods , vol.94 , pp. 131
    • Fesus, L.1    Arato, G.2
  • 34
    • 0024597647 scopus 로고
    • Differential expression of tissue transglutaminase in human cells. An immunohistochemical study
    • Thomazy, V. and Fesus, L. (1989) Differential expression of tissue transglutaminase in human cells. An immunohistochemical study, Cell Tissue Res. 255, 215.
    • (1989) Cell Tissue Res , vol.255 , pp. 215
    • Thomazy, V.1    Fesus, L.2
  • 35
    • 0034635503 scopus 로고    scopus 로고
    • Opposite effects of Ca(2+) and GTP binding on tissue transglutaminase tertiary structure
    • Di Venere, A., Rossi, A., De Matteis, F., Rosato, N., Agro, A. F., andMei, G. (2000) Opposite effects of Ca(2+) and GTP binding on tissue transglutaminase tertiary structure, J. Biol. Chem. 275, 3915.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3915
    • Di Venere, A.1    Rossi, A.2    De Matteis, F.3    Rosato, N.4    Agro, A.F.5    Mei, G.6
  • 36
    • 0028291204 scopus 로고
    • Transglutaminase factor XIII uses proteinase-like catalytic triad to crosslink macromolecules
    • Pedersen, L. C., Yee, V. C., Bishop, P. D., Le Trong, I., Teller, D. C., and Stenkamp, R. E. (1994) Transglutaminase factor XIII uses proteinase-like catalytic triad to crosslink macromolecules, Protein Sci. 3, 1131.
    • (1994) Protein Sci , vol.3 , pp. 1131
    • Pedersen, L.C.1    Yee, V.C.2    Bishop, P.D.3    Le Trong, I.4    Teller, D.C.5    Stenkamp, R.E.6
  • 39
    • 0028828698 scopus 로고
    • Identification and biochemical characterization of an 80 kilodalton GTP-binding/transglutaminase from rabbit liver nuclei
    • Singh, U. S., Erickson, J. W., and Cerione, R. A. (1995) Identification and biochemical characterization of an 80 kilodalton GTP-binding/transglutaminase from rabbit liver nuclei, Biochemistry 34, 15863.
    • (1995) Biochemistry , vol.34 , pp. 15863
    • Singh, U.S.1    Erickson, J.W.2    Cerione, R.A.3
  • 42
    • 0032747129 scopus 로고    scopus 로고
    • Cell surface localization of tissue transglutaminase is dependent on a fibronectin-binding site in its N-terminal beta-sandwich domain
    • Gaudry, C. A., Verderio, E., Aeschlimann, D., Cox, A., Smith, C., and Griffin, M. (1999) Cell surface localization of tissue transglutaminase is dependent on a fibronectin-binding site in its N-terminal beta-sandwich domain, J. Biol. Chem. 274, 30707.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30707
    • Gaudry, C.A.1    Verderio, E.2    Aeschlimann, D.3    Cox, A.4    Smith, C.5    Griffin, M.6
  • 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., Verderio, E., Jones, R. A., Smith, C., and Griffin, M. (1999) 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.
    • (1999) Exp. Cell Res. , vol.252 , pp. 104
    • Gaudry, C.A.1    Verderio, E.2    Jones, R.A.3    Smith, C.4    Griffin, M.5
  • 44
    • 0034114379 scopus 로고    scopus 로고
    • Bcl-2, tissue transglutaminase and p53 protein expression in the apoptotic cascade in ribs of premature infants
    • Stevens, H. Y., Reeve, J., and Noble, B. S. (2000) Bcl-2, tissue transglutaminase and p53 protein expression in the apoptotic cascade in ribs of premature infants, J. Anat. 196(Pt 2), 181.
    • (2000) J. Anat. , vol.196 , Issue.PT 2 , pp. 181
    • Stevens, H.Y.1    Reeve, J.2    Noble, B.S.3
  • 45
    • 0027416842 scopus 로고
    • Affinity of human erythrocyte transglutaminase for a 42-kDa gelatin-binding fragment of human plasma fibronectin
    • Radek, J. T., Jeong, J. M., Murthy, S. N., Ingham, K. C., and Lorand, L. (1993) Affinity of human erythrocyte transglutaminase for a 42-kDa gelatin-binding fragment of human plasma fibronectin, Proc. Natl. Acad. Sci. U.S.A. 90, 3152.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 3152
    • Radek, J.T.1    Jeong, J.M.2    Murthy, S.N.3    Ingham, K.C.4    Lorand, L.5
  • 46
    • 0034695929 scopus 로고    scopus 로고
    • Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin
    • Akimov, S. S., Krylov, D., Fleischman, L. F., and Belkin, A. M. (2000) Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin, J. Cell Biol. 148, 825.
    • (2000) J. Cell Biol. , vol.148 , pp. 825
    • Akimov, S.S.1    Krylov, D.2    Fleischman, L.F.3    Belkin, A.M.4
  • 47
    • 51049089580 scopus 로고    scopus 로고
    • Fibronectin-tissue transglutaminase matrix rescues RGDimpaired cell adhesion through syndecan-4 and beta1 integrin co-signaling
    • Telci, D., Wang, Z., Li, X., Verderio, E. A., Humphries, M. J., Baccarini, M., Basaga, H., and Griffin, M. (2008) Fibronectin-tissue transglutaminase matrix rescues RGDimpaired cell adhesion through syndecan-4 and beta1 integrin co-signaling, J. Biol. Chem. 283, 20937.
    • (2008) J. Biol. Chem. , vol.283 , pp. 20937
    • Telci, D.1    Wang, Z.2    Li, X.3    Verderio, E.A.4    Humphries, M.J.5    Baccarini, M.6    Basaga, H.7    Griffin, M.8
  • 48
    • 33745138517 scopus 로고    scopus 로고
    • GPR56, an atypical G proteincoupled receptor, binds tissue transglutaminase, TG2, and inhibits melanoma tumor growth and metastasis
    • Xu, L., Begum, S., Hearn, J. D., and Hynes, R. O. (2006) GPR56, an atypical G proteincoupled receptor, binds tissue transglutaminase, TG2, and inhibits melanoma tumor growth and metastasis, Proc. Natl. Acad. Sci. U.S.A. 103, 9023.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 9023
    • Xu, L.1    Begum, S.2    Hearn, J.D.3    Hynes, R.O.4
  • 49
    • 0033617199 scopus 로고    scopus 로고
    • Differential signaling by the thromboxane receptor isoforms via the novel GTP-binding protein, Gh
    • Vezza, R., Habib, A., and FitzGerald, G. A. (1999) Differential signaling by the thromboxane receptor isoforms via the novel GTP-binding protein, Gh, J. Biol. Chem. 274, 12774.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12774
    • Vezza, R.1    Habib, A.2    FitzGerald, G.A.3
  • 50
    • 0032055116 scopus 로고    scopus 로고
    • Phospholipase C-delta1 and oxytocin receptor signalling: evidence of its role as an effector
    • Park, E. S., Won, J. H., Han, K. J., Suh, P. G., Ryu, S. H., Lee, H. S., Yun, H. Y., Kwon, N. S., and Baek, K. J. (1998) Phospholipase C-delta1 and oxytocin receptor signalling: evidence of its role as an effector, Biochem. J. 331(Pt 1), 283.
    • (1998) Biochem. J. , vol.331 , Issue.PT 1 , pp. 283
    • Park, E.S.1    Won, J.H.2    Han, K.J.3    Suh, P.G.4    Ryu, S.H.5    Lee, H.S.6    Yun, H.Y.7    Kwon, N.S.8    Baek, K.J.9
  • 54
    • 0030756529 scopus 로고    scopus 로고
    • The core domain of the tissue transglutaminase Gh hydrolyzes GTP and ATP
    • Iismaa, S. E., Chung, L., Wu, M. J., Teller, D. C., Yee, V. C., and Graham, R. M. (1997) The core domain of the tissue transglutaminase Gh hydrolyzes GTP and ATP, Biochemistry 36, 11655.
    • (1997) Biochemistry , vol.36 , pp. 11655
    • Iismaa, S.E.1    Chung, L.2    Wu, M.J.3    Teller, D.C.4    Yee, V.C.5    Graham, R.M.6
  • 55
    • 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., Wu, M. J., Nanda, N., Church, W. B., and Graham, R. M. (2000) GTP binding and signaling by Gh/transglutaminase II involves distinct residues in a unique GTP-binding pocket, J. Biol. Chem. 275, 18259.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18259
    • Iismaa, S.E.1    Wu, M.J.2    Nanda, N.3    Church, W.B.4    Graham, R.M.5
  • 56
    • 0032718477 scopus 로고    scopus 로고
    • Interactions of G(h)/transglutaminase with phospholipase Cdelta1 and with GTP
    • Murthy, S. N., Lomasney, J. W., Mak, E. C., and Lorand, L. (1999) Interactions of G(h)/transglutaminase with phospholipase Cdelta1 and with GTP, Proc. Natl. Acad. Sci. U.S.A. 96, 11815.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 11815
    • Murthy, S.N.1    Lomasney, J.W.2    Mak, E.C.3    Lorand, L.4
  • 57
    • 0030997651 scopus 로고    scopus 로고
    • Sphingosylphosphocholine reduces the calcium ion requirement for activating tissue transglutaminase
    • Lai, T. S., Bielawska, A., Peoples, K. A., Hannun, Y. A., and Greenberg, C. S. (1997) Sphingosylphosphocholine reduces the calcium ion requirement for activating tissue transglutaminase, J. Biol. Chem. 272, 16295.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16295
    • Lai, T.S.1    Bielawska, A.2    Peoples, K.A.3    Hannun, Y.A.4    Greenberg, C.S.5
  • 58
    • 0035942305 scopus 로고    scopus 로고
    • Calcium regulates S-nitrosylation, denitrosylation, and activity of tissue transglutaminase
    • Lai, T. S., Hausladen, A., Slaughter, T. F., Eu, J. P., Stamler, J. S., and Greenberg, C. S. (2001) Calcium regulates S-nitrosylation, denitrosylation, and activity of tissue transglutaminase, Biochemistry 40, 4904.
    • (2001) Biochemistry , vol.40 , pp. 4904
    • Lai, T.S.1    Hausladen, A.2    Slaughter, T.F.3    Eu, J.P.4    Stamler, J.S.5    Greenberg, C.S.6
  • 59
    • 0035872859 scopus 로고    scopus 로고
    • Role of transglutaminase II in retinoic acid-induced activation of RhoA-associated kinase-2
    • Singh, U. S.,Kunar, M. T.,Kao,Y. L., and Baker,K.M. (2001), Role of transglutaminase II in retinoic acid-induced activation of RhoA-associated kinase-2, Embo. J. 20, 2413.
    • (2001) Embo. J. , vol.20 , pp. 2413
    • Singh, U.S.1    Kunar, M.T.2    Kao, Y.L.3    Baker, K.M.4
  • 60
    • 0037414822 scopus 로고    scopus 로고
    • Tissue transglutaminase mediates activation of RhoA and MAP kinase pathways during retinoic acid-induced neuronal differentiation of SH-SY5Y cells
    • Singh, U. S., Pan, J., Kao, Y. L., Joshi, S., Young, K. L., and Baker, K. M. (2003), Tissue transglutaminase mediates activation of RhoA and MAP kinase pathways during retinoic acid-induced neuronal differentiation of SH-SY5Y cells, J. Biol. Chem. 278, 391.
    • (2003) J. Biol. Chem. , vol.278 , pp. 391
    • Singh, U.S.1    Pan, J.2    Kao, Y.L.3    Joshi, S.4    Young, K.L.5    Baker, K.M.6
  • 61
    • 0040041521 scopus 로고    scopus 로고
    • Crosslinking sites of the human tau protein, probed by reactions with human transglutaminase
    • Murthy, S. N., Wilson, J. H., Lukas, T. J., Kuret, J., and Lorand, L. (1998) Crosslinking sites of the human tau protein, probed by reactions with human transglutaminase, J. Neurochem. 71, 2607.
    • (1998) J. Neurochem. , vol.71 , pp. 2607
    • Murthy, S.N.1    Wilson, J.H.2    Lukas, T.J.3    Kuret, J.4    Lorand, L.5
  • 63
    • 0032988045 scopus 로고    scopus 로고
    • Interaction of tissue transglutaminase with nuclear transport protein importinalpha3
    • Peng, X., Zhang, Y., Zhang, H., Graner, S., Williams, J. F., Levitt, M. L., and Lokshin, A. (1999) Interaction of tissue transglutaminase with nuclear transport protein importinalpha3, FEBS Lett. 446, 35.
    • (1999) FEBS Lett , vol.446 , pp. 35
    • Peng, X.1    Zhang, Y.2    Zhang, H.3    Graner, S.4    Williams, J.F.5    Levitt, M.L.6    Lokshin, A.7
  • 64
    • 0029745606 scopus 로고    scopus 로고
    • Core histones are glutaminyl substrates for tissue transglutaminase
    • Ballestar, E., Abad, C., and Franco, L. (1996) Core histones are glutaminyl substrates for tissue transglutaminase, J. Biol. Chem. 271, 18817.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18817
    • Ballestar, E.1    Abad, C.2    Franco, L.3
  • 65
    • 0035916311 scopus 로고    scopus 로고
    • Conformational changes in the nucleosome followed by the selective accessibility of histone glutamines in the transglutaminase reaction: effects of ionic strength
    • Ballestar, E., Boix-Chornet, M., and Franco, L. (2001) Conformational changes in the nucleosome followed by the selective accessibility of histone glutamines in the transglutaminase reaction: effects of ionic strength, Biochemistry 40, 1922.
    • (2001) Biochemistry , vol.40 , pp. 1922
    • Ballestar, E.1    Boix-Chornet, M.2    Franco, L.3
  • 66
    • 0030863635 scopus 로고    scopus 로고
    • Tissue transglutaminase-dependent posttranslational modification of the retinoblastoma gene product in promonocytic cells undergoing apoptosis
    • Oliverio, S., Amendola, A., Di Sano, F., Farrace, M. G., Fesus, L., Nemes, Z., Piredda, L., Spinedi, A., and Piacentini, M. (1997) Tissue transglutaminase-dependent posttranslational modification of the retinoblastoma gene product in promonocytic cells undergoing apoptosis, Mol. Cell Biol. 17, 6040.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 6040
    • 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
  • 67
    • 0024520475 scopus 로고
    • Apoptotic hepatocytes become insoluble in detergents and chaotropic agents as a result of transglutaminase action
    • Fesus, L., Thomazy, V., Autuori, F., Ceru, M. P., Tarcsa, E., and Piacentini, M. (1989) Apoptotic hepatocytes become insoluble in detergents and chaotropic agents as a result of transglutaminase action, FEBS Lett. 245, 150.
    • (1989) FEBS Lett , vol.245 , pp. 150
    • Fesus, L.1    Thomazy, V.2    Autuori, F.3    Ceru, M.P.4    Tarcsa, E.5    Piacentini, M.6
  • 68
    • 0023159034 scopus 로고
    • Induction and activation of tissue transglutaminase during programmed cell death
    • Fesus, L., Thomazy, V., and Falus, A. (1987) Induction and activation of tissue transglutaminase during programmed cell death, FEBS Lett. 224, 104.
    • (1987) FEBS Lett , vol.224 , pp. 104
    • Fesus, L.1    Thomazy, V.2    Falus, A.3
  • 69
    • 0033607671 scopus 로고    scopus 로고
    • Inhibition of " tissue" transglutaminase increases cell survival by preventing apoptosis
    • Oliverio, S., Amendola, A., Rodolfo,C., Spinedi, A., and Piacentini, M. (1999) Inhibition of " tissue" transglutaminase increases cell survival by preventing apoptosis, J. Biol. Chem. 274, 34123.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34123
    • Oliverio, S.1    Amendola, A.2    Rodolfo, C.3    Spinedi, A.4    Piacentini, M.5
  • 72
    • 0031042223 scopus 로고    scopus 로고
    • Differential expression of tissue transglutaminase during in vivo apoptosis of thymocytes induced via distinct signalling pathways
    • Szondy, Z., Molnar, P., Nemes, Z., Boyiadzis, M., Kedei, N., Toth, R., and Fesus, L. (1997) Differential expression of tissue transglutaminase during in vivo apoptosis of thymocytes induced via distinct signalling pathways, FEBS Lett. 404, 307.
    • (1997) FEBS Lett , vol.404 , pp. 307
    • Szondy, Z.1    Molnar, P.2    Nemes, Z.3    Boyiadzis, M.4    Kedei, N.5    Toth, R.6    Fesus, L.7
  • 73
    • 0030960146 scopus 로고    scopus 로고
    • Induction of apoptosis by retinoids and retinoic acid receptor gamma-selective compounds in mouse thymocytes through a novel apoptosis pathway
    • Szondy, Z., Reichert, U., Bernardon, J. M., Michel, S., Toth, R., Ancian, P., Ajzner, E., and Fesus, L. (1997) Induction of apoptosis by retinoids and retinoic acid receptor gamma-selective compounds in mouse thymocytes through a novel apoptosis pathway, Mol. Pharmacol. 51, 972.
    • (1997) Mol. Pharmacol. , vol.51 , pp. 972
    • Szondy, Z.1    Reichert, U.2    Bernardon, J.M.3    Michel, S.4    Toth, R.5    Ancian, P.6    Ajzner, E.7    Fesus, L.8
  • 74
    • 0031851862 scopus 로고    scopus 로고
    • A transgenic mouse model for the study of apoptosis during limb development
    • Nagy, L., Thomazy, V. A., and Davies, P. J. (1998) A transgenic mouse model for the study of apoptosis during limb development, Cell Death Differ. 5, 126.
    • (1998) Cell Death Differ , vol.5 , pp. 126
    • Nagy, L.1    Thomazy, V.A.2    Davies, P.J.3
  • 75
    • 2542509469 scopus 로고    scopus 로고
    • Expression of tissue transglutaminase in the developing chicken limb is associated bothwith apoptosis and endochondral ossification
    • Thomazy, V. A. and Davies, P. J. (1999) Expression of tissue transglutaminase in the developing chicken limb is associated bothwith apoptosis and endochondral ossification, Cell Death Differ. 6, 146.
    • (1999) Cell Death Differ , vol.6 , pp. 146
    • Thomazy, V.A.1    Davies, P.J.2
  • 77
    • 0029884873 scopus 로고    scopus 로고
    • Expression and activation of tissue transglutaminase in apoptotic cells of involuting rodent mammary tissue
    • Nemes, Z., Jr., Friis, R. R., Aeschlimann, D., Saurer, S., Paulsson, M., and Fesus, L. (1996) Expression and activation of tissue transglutaminase in apoptotic cells of involuting rodent mammary tissue, Eur. J. Cell Biol. 70, 125.
    • (1996) Eur. J. Cell Biol. , vol.70 , pp. 125
    • Nemes Jr, Z.1    Friis, R.R.2    Aeschlimann, D.3    Saurer, S.4    Paulsson, M.5    Fesus, L.6
  • 78
    • 34250174215 scopus 로고    scopus 로고
    • Type 2 transglutaminase differentially modulates striatal cell death in the presence of wild type or mutant huntingtin
    • Ruan, Q., Quintanilla, R. A., and Johnson, G. V. (2007) Type 2 transglutaminase differentially modulates striatal cell death in the presence of wild type or mutant huntingtin, J. Neurochem. 102, 25.
    • (2007) J. Neurochem. , vol.102 , pp. 25
    • Ruan, Q.1    Quintanilla, R.A.2    Johnson, G.V.3
  • 81
    • 0030970927 scopus 로고    scopus 로고
    • Troponin T cross-linking in human apoptotic cardiomyocytes
    • Gorza, L., Menabo, R., Di Lisa, F., and Vitadello, M. (1997) Troponin T cross-linking in human apoptotic cardiomyocytes, Am. J. Pathol. 150, 2087.
    • (1997) Am. J. Pathol. , vol.150 , pp. 2087
    • Gorza, L.1    Menabo, R.2    Di Lisa, F.3    Vitadello, M.4
  • 82
    • 0029975234 scopus 로고    scopus 로고
    • Cardiomyocyte troponin T immunoreactivity is modified by cross-linking resulting from intracellular calcium overload
    • Gorza, L., Menabo, R., Vitadello, M., Bergamini, C. M., and Di Lisa, F. (1996) Cardiomyocyte troponin T immunoreactivity is modified by cross-linking resulting from intracellular calcium overload, Circulation 93, 1896.
    • (1996) Circulation , vol.93 , pp. 1896
    • Gorza, L.1    Menabo, R.2    Vitadello, M.3    Bergamini, C.M.4    Di Lisa, F.5
  • 83
    • 0033558825 scopus 로고    scopus 로고
    • Hormonal control of " tissue" transglutaminase induction during programmed cell death in frog liver
    • Assisi, L., Autuori, F., Botte, V., Farrace, M. G., and Piacentini, M. (1999) Hormonal control of " tissue" transglutaminase induction during programmed cell death in frog liver, Exp. Cell Res. 247, 339.
    • (1999) Exp. Cell Res. , vol.247 , pp. 339
    • Assisi, L.1    Autuori, F.2    Botte, V.3    Farrace, M.G.4    Piacentini, M.5
  • 84
    • 0031706064 scopus 로고    scopus 로고
    • Camptothecin induces differentiation, tissue transglutaminase and apoptosis in cultured keratinocytes
    • Lin, X. R., Wilkinson, D. I., and Farber, E. M. (1998) Camptothecin induces differentiation, tissue transglutaminase and apoptosis in cultured keratinocytes, Exp. Dermatol. 7, 179.
    • (1998) Exp. Dermatol. , vol.7 , pp. 179
    • Lin, X.R.1    Wilkinson, D.I.2    Farber, E.M.3
  • 87
    • 0025778292 scopus 로고
    • Degradation of cells dying by apoptosis leads to accumulation of epsilon(gamma-glutamyl)lysine isodipeptide in culture fluid and blood
    • Fesus, L., Tarcsa, E., Kedei, N., Autuori, F., and Piacentini, M. (1991) Degradation of cells dying by apoptosis leads to accumulation of epsilon(gamma-glutamyl)lysine isodipeptide in culture fluid and blood, FEBS Lett. 284, 109.
    • (1991) FEBS Lett , vol.284 , pp. 109
    • Fesus, L.1    Tarcsa, E.2    Kedei, N.3    Autuori, F.4    Piacentini, M.5
  • 88
    • 0029744038 scopus 로고    scopus 로고
    • Induction of " tissue" transglutaminase in HIV pathogenesis: evidence for high rate of apoptosis of CD4+ T lymphocytes and accessory cells in lymphoid tissues
    • Amendola, A., Gougeon, M. L., Poccia, F., Bondurand, A., Fesus, L., and Piacentini, M. (1996) Induction of " tissue" transglutaminase in HIV pathogenesis: evidence for high rate of apoptosis of CD4+ T lymphocytes and accessory cells in lymphoid tissues, Proc. Natl. Acad. Sci. U.S.A. 93, 11057.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 11057
    • Amendola, A.1    Gougeon, M.L.2    Poccia, F.3    Bondurand, A.4    Fesus, L.5    Piacentini, M.6
  • 90
    • 33748152329 scopus 로고    scopus 로고
    • Protective effect against 17beta-estradiol on neuronal apoptosis in hippocampus tissue following transient ischemia/recirculation in mongolian gerbils via down-regulation of tissue transglutaminase activity
    • Fujita, K., Kato, T., Shibayama, K., Imada, H., Yamauchi, M., Yoshimoto, N., Miyachi, E., and Nagata, Y. (2006) Protective effect against 17beta-estradiol on neuronal apoptosis in hippocampus tissue following transient ischemia/recirculation in mongolian gerbils via down-regulation of tissue transglutaminase activity, Neurochem. Res. 31, 1059.
    • (2006) Neurochem. Res. , vol.31 , pp. 1059
    • Fujita, K.1    Kato, T.2    Shibayama, K.3    Imada, H.4    Yamauchi, M.5    Yoshimoto, N.6    Miyachi, E.7    Nagata, Y.8
  • 91
    • 62249162878 scopus 로고    scopus 로고
    • Expression of tissue-type transglutaminase (tTG) and the effect of tTG inhibitor on the hippocampal CA1 region after transient ischemia in gerbils
    • Hwang, I. K., Yoo, K. Y., Yi, S. S., Kim, I. Y., Hwang, H. S., Lee, K. Y., Choi, S. M., Lee, I. S., Yoon, Y. S., Kim, S. Y., Won, M. H., and Seong, J. K. (2009) Expression of tissue-type transglutaminase (tTG) and the effect of tTG inhibitor on the hippocampal CA1 region after transient ischemia in gerbils, Brain Res. 1263, 134.
    • (2009) Brain Res , vol.1263 , pp. 134
    • Hwang, I.K.1    Yoo, K.Y.2    Yi, S.S.3    Kim, I.Y.4    Hwang, H.S.5    Lee, K.Y.6    Choi, S.M.7    Lee, I.S.8    Yoon, Y.S.9    Kim, S.Y.10    Won, M.H.11    Seong, J.K.12
  • 94
    • 70350437632 scopus 로고    scopus 로고
    • Transglutaminase-mediated intramolecular cross-linking of membrane-bound alphasynuclein promotes amyloid formation in Lewy bodies
    • Nemes, Z., Petrovski, G., Aerts, M., Sergeant, K., Devreese, B., and Fesus, L. (2009) Transglutaminase-mediated intramolecular cross-linking of membrane-bound alphasynuclein promotes amyloid formation in Lewy bodies, J. Biol. Chem. 284, 27252.
    • (2009) J. Biol. Chem. , vol.284 , pp. 27252
    • Nemes, Z.1    Petrovski, G.2    Aerts, M.3    Sergeant, K.4    Devreese, B.5    Fesus, L.6
  • 95
    • 13744261331 scopus 로고    scopus 로고
    • Tissue transglutaminase in cell death
    • Griffin, M. and Verderio, E. (2000) Tissue transglutaminase in cell death, Symp. Soc. Exp. Biol. 52, 223.
    • (2000) Symp. Soc. Exp. Biol. , vol.52 , pp. 223
    • Griffin, M.1    Verderio, E.2
  • 97
    • 33748522053 scopus 로고    scopus 로고
    • Clearance of apoptotic and necrotic cells and its immunological consequences
    • Krysko, D. V., D'Herde, K., and Vandenabeele, P. (2006) Clearance of apoptotic and necrotic cells and its immunological consequences, Apoptosis 11, 1709.
    • (2006) Apoptosis , vol.11 , pp. 1709
    • Krysko, D.V.1    D'Herde, K.2    Vandenabeele, P.3
  • 98
    • 0032892638 scopus 로고    scopus 로고
    • Apoptosis and autoimmunity: two sides to the coin
    • Piacentini, M. (1999) Apoptosis and autoimmunity: two sides to the coin, Cell Death Differ. 6, 1.
    • (1999) Cell Death Differ , vol.6 , pp. 1
    • Piacentini, M.1
  • 99
    • 0015383455 scopus 로고
    • Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr, J. F., Wyllie, A. H., and Currie, A. R. (1972) Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics, Br. J. Cancer 26, 239.
    • (1972) Br. J. Cancer , vol.26 , pp. 239
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 100
    • 0034068601 scopus 로고    scopus 로고
    • Mitochondrial control of cell death
    • Kroemer, G. and Reed, J. C. (2000) Mitochondrial control of cell death, Nat. Med. 6, 513.
    • (2000) Nat. Med. , vol.6 , pp. 513
    • Kroemer, G.1    Reed, J.C.2
  • 101
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • Enari, M., Sakahira, H., Yokoyama, H., Okawa, K., Iwamatsu, A., and Nagata, S. (1998) A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD, Nature 391, 43.
    • (1998) Nature , vol.391 , pp. 43
    • Enari, M.1    Sakahira, H.2    Yokoyama, H.3    Okawa, K.4    Iwamatsu, A.5    Nagata, S.6
  • 102
    • 0013934457 scopus 로고
    • The significance of lysosomes in pathology and medicine
    • De Duve, C. (1966) The significance of lysosomes in pathology and medicine, Proc. Inst. Med. Chic. 26, 73.
    • (1966) Proc. Inst. Med. Chic. , vol.26 , pp. 73
    • De Duve, C.1
  • 104
  • 105
    • 34548265278 scopus 로고    scopus 로고
    • Autophagy and human disease
    • Huang, J. and Klionsky, D. J. (2007) Autophagy and human disease, Cell Cycle 6, 1837.
    • (2007) Cell Cycle , vol.6 , pp. 1837
    • Huang, J.1    Klionsky, D.J.2
  • 108
    • 29944438881 scopus 로고    scopus 로고
    • Necrotic death as a cell fate
    • Zong,W. X. and Thompson, C. B. (2006) Necrotic death as a cell fate, Genes Dev. 20, 1.
    • (2006) Genes Dev , vol.20 , pp. 1
    • Zong, W.X.1    Thompson, C.B.2
  • 112
    • 33947714475 scopus 로고    scopus 로고
    • Caspase inhibitors promote alternative cell death pathways
    • Vandenabeele, P.,Vanden Berghe, T., and Festjens, N. (2006) Caspase inhibitors promote alternative cell death pathways, Sci. STKE 2006, pe44.
    • (2006) Sci. STKE , vol.2006
    • Vandenabeele, P.1    Vanden Berghe, T.2    Festjens, N.3
  • 113
    • 0036783252 scopus 로고    scopus 로고
    • Detection of in situ activation of transglutaminase during apoptosis: correlation with the cell cycle phase by multiparameter flow and laser scanning cytometry
    • Grabarek, J., Ardelt, B., Kunicki, J., and Darzynkiewicz, Z. (2002) Detection of in situ activation of transglutaminase during apoptosis: correlation with the cell cycle phase by multiparameter flow and laser scanning cytometry, Cytometry 49, 83.
    • (2002) Cytometry , vol.49 , pp. 83
    • Grabarek, J.1    Ardelt, B.2    Kunicki, J.3    Darzynkiewicz, Z.4
  • 114
    • 2442676613 scopus 로고    scopus 로고
    • Tissue transglutaminase triggers oligomerization and activation of dual leucine zipper-bearing kinase in calphostin C-treated cells to facilitate apoptosis
    • Robitaille, K., Daviau, A., Tucholski, J., Johnson, G. V., Rancourt, C., and Blouin, R. (2004) Tissue transglutaminase triggers oligomerization and activation of dual leucine zipper-bearing kinase in calphostin C-treated cells to facilitate apoptosis, Cell Death Differ. 11, 542.
    • (2004) Cell Death Differ , vol.11 , pp. 542
    • Robitaille, K.1    Daviau, A.2    Tucholski, J.3    Johnson, G.V.4    Rancourt, C.5    Blouin, R.6
  • 116
    • 73649115337 scopus 로고    scopus 로고
    • Epithelial-to-mesenchymal transition and ovarian tumor progression induced by tissue transglutaminase
    • Shao, M., Cao, L., Shen, C., Satpathy, M., Chelladurai, B., Bigsby, R. M., Nakshatri, H., and Matei, D. (2009) Epithelial-to-mesenchymal transition and ovarian tumor progression induced by tissue transglutaminase, Cancer Res. 69, 9192.
    • (2009) Cancer Res , vol.69 , pp. 9192
    • Shao, M.1    Cao, L.2    Shen, C.3    Satpathy, M.4    Chelladurai, B.5    Bigsby, R.M.6    Nakshatri, H.7    Matei, D.8
  • 118
    • 72949098051 scopus 로고    scopus 로고
    • Transglutaminase 2 expression levels regulate sensitivity to cystamine plus TRAIL-mediated apoptosis
    • Jang, J. H., Park, J. S., Lee, T. J., and Kwon, T. K. (2009) Transglutaminase 2 expression levels regulate sensitivity to cystamine plus TRAIL-mediated apoptosis, Cancer Lett. 287, 224.
    • (2009) Cancer Lett , vol.287 , pp. 224
    • Jang, J.H.1    Park, J.S.2    Lee, T.J.3    Kwon, T.K.4
  • 119
    • 34250827844 scopus 로고    scopus 로고
    • Tissue transglutaminase induces the release of apoptosis inducing factor and results in apoptotic death of pancreatic cancer cells
    • Fok, J. Y. andMehta, K. (2007) Tissue transglutaminase induces the release of apoptosis inducing factor and results in apoptotic death of pancreatic cancer cells, Apoptosis 12, 1455.
    • (2007) Apoptosis , vol.12 , pp. 1455
    • Fok, J.Y.1    Mehta, K.2
  • 120
    • 53349143213 scopus 로고    scopus 로고
    • Tissue transglutaminase protects epithelial ovarian cancer cells from cisplatin-induced apoptosis by promoting cell survival signaling
    • Cao, L., Petrusca, D. N., Satpathy, M., Nakshatri, H., Petrache, I., and Matei, D. (2008) Tissue transglutaminase protects epithelial ovarian cancer cells from cisplatin-induced apoptosis by promoting cell survival signaling, Carcinogenesis 29, 1893.
    • (2008) Carcinogenesis , vol.29 , pp. 1893
    • Cao, L.1    Petrusca, D.N.2    Satpathy, M.3    Nakshatri, H.4    Petrache, I.5    Matei, D.6
  • 121
    • 0032055173 scopus 로고    scopus 로고
    • Evidence for the involvement of both retinoic acid receptor-and retinoic X receptor-dependent signaling pathways in the induction of tissue transglutaminase and apoptosis in the human myeloma cell line RPMI 8226
    • Joseph, B., Lefebvre, O., Mereau-Richard, C., Danze, P. M., Belin-Plancot, M. T., and Formstecher, P. (1998) Evidence for the involvement of both retinoic acid receptor-and retinoic X receptor-dependent signaling pathways in the induction of tissue transglutaminase and apoptosis in the human myeloma cell line RPMI 8226, Blood 91, 2423.
    • (1998) Blood , vol.91 , pp. 2423
    • Joseph, B.1    Lefebvre, O.2    Mereau-Richard, C.3    Danze, P.M.4    Belin-Plancot, M.T.5    Formstecher, P.6
  • 122
    • 0032991862 scopus 로고    scopus 로고
    • Induction of apoptosis by all-trans retinoic acid in the human myeloma cell line RPMI 8226 and negative regulation of some of its typical morphological features by dexamethasone
    • Lefebvre, O., Wouters, D., Mereau-Richard, C., Facon, T., Zandecki, M., Formstecher, P., and Belin, M. T. (1999) Induction of apoptosis by all-trans retinoic acid in the human myeloma cell line RPMI 8226 and negative regulation of some of its typical morphological features by dexamethasone, Cell Death Differ. 6, 433.
    • (1999) Cell Death Differ , vol.6 , pp. 433
    • Lefebvre, O.1    Wouters, D.2    Mereau-Richard, C.3    Facon, T.4    Zandecki, M.5    Formstecher, P.6    Belin, M.T.7
  • 124
  • 127
    • 42249085070 scopus 로고    scopus 로고
    • Tissue transglutaminase regulates focal adhesion kinase/AKT activation by modulating PTEN expression in pancreatic cancer cells
    • Verma, A., Guha, S.,Wang, H., Fok, J.Y.,Koul, D., Abbruzzese, J., and Mehta, K. (2008) Tissue transglutaminase regulates focal adhesion kinase/AKT activation by modulating PTEN expression in pancreatic cancer cells, Clin. Cancer Res. 14, 1997.
    • (2008) Clin. Cancer Res. , vol.14 , pp. 1997
    • Verma, A.1    Guha, S.2    Wang, H.3    Fok, J.Y.4    Koul, D.5    Abbruzzese, J.6    Mehta, K.7
  • 129
    • 0025728132 scopus 로고
    • The expression of " tissue" transglutaminase in two human cancer cell lines is related with the programmed cell death (apoptosis)
    • Piacentini, M., Fesus, L., Farrace, M. G., Ghibelli, L., Piredda, L., andMelino, G. (1991) The expression of " tissue" transglutaminase in two human cancer cell lines is related with the programmed cell death (apoptosis), Eur. J. Cell Biol. 54, 246.
    • (1991) Eur. J. Cell Biol. , vol.54 , pp. 246
    • Piacentini, M.1    Fesus, L.2    Farrace, M.G.3    Ghibelli, L.4    Piredda, L.5    Melino, G.6
  • 130
    • 4744351463 scopus 로고    scopus 로고
    • Augmentation of tissue transglutaminase expression and activation by epidermal growth factor inhibit doxorubicin-induced apoptosis in human breast cancer cells
    • Antonyak,M. A., Miller, A.M., Jansen, J.M., Boehm, J. E., Balkman, C. E.,Wakshlag, J. J., Page, R. L., and Cerione, R. A. (2004) Augmentation of tissue transglutaminase expression and activation by epidermal growth factor inhibit doxorubicin-induced apoptosis in human breast cancer cells, J. Biol. Chem. 279, 41461.
    • (2004) J. Biol. Chem. , vol.279 , pp. 41461
    • Antonyak, M.A.1    Miller, A.M.2    Jansen, J.M.3    Boehm, J.E.4    Balkman, C.E.5    Wakshlag, J.J.6    Page, R.L.7    Cerione, R.A.8
  • 131
    • 33750735045 scopus 로고    scopus 로고
    • Importance of Ca(2+)-dependent transamidation activity in the protection afforded by tissue transglutaminase against doxorubicin-induced apoptosis
    • Datta, S., Antonyak,M. A., and Cerione, R. A. (2006) Importance of Ca(2+)-dependent transamidation activity in the protection afforded by tissue transglutaminase against doxorubicin-induced apoptosis, Biochemistry 45, 13163.
    • (2006) Biochemistry , vol.45 , pp. 13163
    • Datta, S.1    Antonyak, M.A.2    Cerione, R.A.3
  • 132
    • 63849213920 scopus 로고    scopus 로고
    • Silencing of TGase 2 sensitizes breast cancer cells to apoptosis by regulation of survival factors
    • Kim, D. S., Park, K. S., and Kim, S. Y. (2009) Silencing of TGase 2 sensitizes breast cancer cells to apoptosis by regulation of survival factors, Front. Biosci. 14, 2514.
    • (2009) Front. Biosci. , vol.14 , pp. 2514
    • Kim, D.S.1    Park, K.S.2    Kim, S.Y.3
  • 134
    • 25144449101 scopus 로고    scopus 로고
    • Natural retinoids inhibit proliferation and induce apoptosis in pancreatic cancer cells previously reported to be retinoid resistant
    • El-Metwally, T. H., Hussein, M. R., Pour, P. M., Kuszynski, C. A., and Adrian, T. E. (2005) Natural retinoids inhibit proliferation and induce apoptosis in pancreatic cancer cells previously reported to be retinoid resistant, Cancer Biol. Ther. 4, 474.
    • (2005) Cancer Biol. Ther. , vol.4 , pp. 474
    • El-Metwally, T.H.1    Hussein, M.R.2    Pour, P.M.3    Kuszynski, C.A.4    Adrian, T.E.5
  • 135
    • 2342644667 scopus 로고    scopus 로고
    • Protective role of tissue transglutaminase in the cell death induced by TNF-alpha in SH-SY5Y neuroblastoma cells
    • Kweon, S. M., Lee, Z. W., Yi, S. J., Kim, Y. M., Han, J. A., Paik, S. G., and Ha, S. S. (2004) Protective role of tissue transglutaminase in the cell death induced by TNF-alpha in SH-SY5Y neuroblastoma cells, J. Biochem. Mol. Biol. 37, 185.
    • (2004) J. Biochem. Mol. Biol. , vol.37 , pp. 185
    • Kweon, S.M.1    Lee, Z.W.2    Yi, S.J.3    Kim, Y.M.4    Han, J.A.5    Paik, S.G.6    Ha, S.S.7
  • 136
    • 54249133441 scopus 로고    scopus 로고
    • FLIP and the death effector domain family
    • Yu, J. W. and Shi, Y. (2008) FLIP and the death effector domain family, Oncogene 27, 6216.
    • (2008) Oncogene , vol.27 , pp. 6216
    • Yu, J.W.1    Shi, Y.2
  • 137
    • 20444430478 scopus 로고    scopus 로고
    • Apoptotic pathways: ten minutes to dead
    • Green, D. R. (2005) Apoptotic pathways: ten minutes to dead, Cell 121, 671.
    • (2005) Cell , vol.121 , pp. 671
    • Green, D.R.1
  • 138
    • 58149177449 scopus 로고    scopus 로고
    • Caspase-8 goes cardiolipin: a new platform to provide mitochondria with microdomains of apoptotic signals?
    • Scorrano, L. (2008) Caspase-8 goes cardiolipin: a new platform to provide mitochondria with microdomains of apoptotic signals? J. Cell Biol. 183, 579.
    • (2008) J. Cell Biol , vol.183 , pp. 579
    • Scorrano, L.1
  • 139
    • 41149152733 scopus 로고    scopus 로고
    • How do BCL-2 proteins induce mitochondrial outer membrane permeabilization?
    • Chipuk, J. E. and Green, D. R. (2008) How do BCL-2 proteins induce mitochondrial outer membrane permeabilization?, Trends Cell Biol. 18, 157.
    • (2008) Trends Cell Biol , vol.18 , pp. 157
    • Chipuk, J.E.1    Green, D.R.2
  • 140
    • 0037427412 scopus 로고    scopus 로고
    • Mechanisms of cytochrome c release by proapoptotic BCL-2 family members
    • Scorrano, L. and Korsmeyer, S. J. (2003) Mechanisms of cytochrome c release by proapoptotic BCL-2 family members, Biochem. Biophys. Res. Commun. 304, 437.
    • (2003) Biochem. Biophys. Res. Commun. , vol.304 , pp. 437
    • Scorrano, L.1    Korsmeyer, S.J.2
  • 143
    • 37549069901 scopus 로고    scopus 로고
    • BCL-2 family proteins: critical checkpoints of apoptotic cell death
    • Danial, N. N. (2007) BCL-2 family proteins: critical checkpoints of apoptotic cell death, Clin Cancer Res 13, 7254.
    • (2007) Clin Cancer Res , vol.13 , pp. 7254
    • Danial, N.N.1
  • 144
    • 68249106060 scopus 로고    scopus 로고
    • BH3-only proteins in apoptosis and beyond: an overview
    • Lomonosova, E. andChinnadurai, G. (2008) BH3-only proteins in apoptosis and beyond: an overview, Oncogene 27(Suppl 1), S2.
    • (2008) Oncogene , vol.27 , Issue.SUPPL 1
    • Lomonosova, E.1    Chinnadurai, G.2
  • 146
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: opposing activities that mediate cell death
    • Youle, R. J. and Strasser, A. (2008) The BCL-2 protein family: opposing activities that mediate cell death, Nat. Rev. Mol. Cell Biol. 9, 47.
    • (2008) Nat. Rev. Mol. Cell Biol , vol.9 , pp. 47
    • Youle, R.J.1    Strasser, A.2
  • 148
    • 0026018673 scopus 로고
    • " Tissue" transglutaminase is specifically expressed in neonatal rat liver cells undergoing apoptosis upon epidermal growth factor-stimulation
    • Piacentini, M., Autuori, F., Dini, L., Farrace, M. G., Ghibelli, L., Piredda, L., and Fesus, L. (1991) " Tissue" transglutaminase is specifically expressed in neonatal rat liver cells undergoing apoptosis upon epidermal growth factor-stimulation, Cell Tissue Res. 263, 227.
    • (1991) Cell Tissue Res , vol.263 , pp. 227
    • Piacentini, M.1    Autuori, F.2    Dini, L.3    Farrace, M.G.4    Ghibelli, L.5    Piredda, L.6    Fesus, L.7
  • 150
    • 67650239851 scopus 로고    scopus 로고
    • Nucleophosmin blocks mitochondrial localization of p53 and apoptosis
    • Dhar, S. K. and St Clair, D. K. (2009) Nucleophosmin blocks mitochondrial localization of p53 and apoptosis, J. Biol. Chem. 284, 16409.
    • (2009) J. Biol. Chem. , vol.284 , pp. 16409
    • Dhar, S.K.1    St Clair, D.K.2
  • 153
    • 39749124295 scopus 로고    scopus 로고
    • Type 2 transglutaminase in neurodegenerative diseases: the mitochondrial connection
    • Malorni,W., Farrace, M. G., Rodolfo, C., and Piacentini, M. (2008) Type 2 transglutaminase in neurodegenerative diseases: the mitochondrial connection, Curr. Pharm. Des. 14, 278.
    • (2008) Curr. Pharm. Des. , vol.14 , pp. 278
    • Malorni, W.1    Farrace, M.G.2    Rodolfo, C.3    Piacentini, M.4
  • 154
    • 0032524312 scopus 로고    scopus 로고
    • Distinct nuclear localization and activity of tissue transglutaminase
    • Lesort, M., Attanavanich, K., Zhang, J., and Johnson, G. V. (1998) Distinct nuclear localization and activity of tissue transglutaminase, J. Biol. Chem. 273, 11991.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11991
    • Lesort, M.1    Attanavanich, K.2    Zhang, J.3    Johnson, G.V.4
  • 155
    • 16844384185 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase kinase kinase dual leucine zipper-bearing kinase (DLK) acts as a key regulator of keratinocyte terminal differentiation
    • Robitaille, H., Proulx, R., Robitaille, K., Blouin, R., and Germain, L. (2005) The mitogen-activated protein kinase kinase kinase dual leucine zipper-bearing kinase (DLK) acts as a key regulator of keratinocyte terminal differentiation, J. Biol. Chem. 280, 12732.
    • (2005) J. Biol. Chem. , vol.280 , pp. 12732
    • Robitaille, H.1    Proulx, R.2    Robitaille, K.3    Blouin, R.4    Germain, L.5
  • 156
    • 49949098410 scopus 로고    scopus 로고
    • Calphostin C-induced apoptosis is mediated by a tissue transglutaminase-dependent mechanism involving the DLK/JNK signaling pathway
    • Robitaille, K., Daviau, A., Lachance, G., Couture, J. P., and Blouin, R. (2008) Calphostin C-induced apoptosis is mediated by a tissue transglutaminase-dependent mechanism involving the DLK/JNK signaling pathway, Cell Death Differ. 15, 1522.
    • (2008) Cell Death Differ , vol.15 , pp. 1522
    • Robitaille, K.1    Daviau, A.2    Lachance, G.3    Couture, J.P.4    Blouin, R.5
  • 157
  • 158
    • 0035976314 scopus 로고    scopus 로고
    • Dlk/ZIP kinase-induced apoptosis in human medulloblastoma cells: requirement of the mitochondrial apoptosis pathway
    • Kogel, D., Reimertz, C., Mech, P., Poppe, M., Fruhwald, M. C., Engemann, H., Scheidtmann, K. H., and Prehn, J. H. (2001), Dlk/ZIP kinase-induced apoptosis in human medulloblastoma cells: requirement of the mitochondrial apoptosis pathway, Br. J. Cancer 85, 1801.
    • (2001) Br. J. Cancer , vol.85 , pp. 1801
    • Kogel, D.1    Reimertz, C.2    Mech, P.3    Poppe, M.4    Fruhwald, M.C.5    Engemann, H.6    Scheidtmann, K.H.7    Prehn, J.H.8
  • 159
    • 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., Telci, D., Okoye, A., Melino, G., and Griffin, M. (2003) A novel RGD-independent cell adhesion pathway mediated by fibronectin-bound tissue transglutaminase rescues cells from anoikis, J. Biol. Chem. 278, 42604.
    • (2003) J. Biol. Chem. , vol.278 , pp. 42604
    • Verderio, E.A.1    Telci, D.2    Okoye, A.3    Melino, G.4    Griffin, M.5
  • 160
    • 62949217561 scopus 로고    scopus 로고
    • Transglutaminase 2 cross-linking of matrix proteins: biological significance and medical applications
    • Collighan, R. J. and Griffin, M. (2009) Transglutaminase 2 cross-linking of matrix proteins: biological significance and medical applications, Amino Acids 36, 659.
    • (2009) Amino Acids , vol.36 , pp. 659
    • Collighan, R.J.1    Griffin, M.2
  • 161
    • 67651246845 scopus 로고    scopus 로고
    • Intracellular localization and conformational state of transglutaminase 2 implications for cell death
    • Gundemir, S. and Johnson, G. V. (2009) Intracellular localization and conformational state of transglutaminase 2: implications for cell death, PLoS One 4, e6123.
    • (2009) PLoS One , vol.4
    • Gundemir, S.1    Johnson, G.V.2
  • 162
    • 0035823548 scopus 로고    scopus 로고
    • Effects of tissue transglutaminase on retinoic acid-induced cellular differentiation and protection against apoptosis
    • Antonyak, M. A., Singh, U. S., Lee, D. A., Boehm, J. E., Combs, C., Zgola, M. M., Page, R. L., and Cerione, R. A. (2001) Effects of tissue transglutaminase on retinoic acid-induced cellular differentiation and protection against apoptosis, J. Biol. Chem. 276, 33582.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33582
    • Antonyak, M.A.1    Singh, U.S.2    Lee, D.A.3    Boehm, J.E.4    Combs, C.5    Zgola, M.M.6    Page, R.L.7    Cerione, R.A.8
  • 163
    • 33746472503 scopus 로고    scopus 로고
    • The role of tissue transglutaminase in 1-methyl-4-phenylpyridinium (MPP+)-induced toxicity in differentiated human SH-SY5Y neuroblastoma cells
    • Beck, K. E., De Girolamo, L. A., Griffin, M., and Billett, E. E. (2006) The role of tissue transglutaminase in 1-methyl-4-phenylpyridinium (MPP+)-induced toxicity in differentiated human SH-SY5Y neuroblastoma cells, Neurosci. Lett. 405, 46.
    • (2006) Neurosci. Lett. , vol.405 , pp. 46
    • Beck, K.E.1    De Girolamo, L.A.2    Griffin, M.3    Billett, E.E.4
  • 164
    • 34548399498 scopus 로고    scopus 로고
    • Transglutaminase-mediated activation of nuclear transcription factor-kappaB in cancer cells: a new therapeutic opportunity
    • Verma, A. and Mehta, K. (2007) Transglutaminase-mediated activation of nuclear transcription factor-kappaB in cancer cells: a new therapeutic opportunity, Curr. Cancer Drug Targets 7, 559.
    • (2007) Curr. Cancer Drug Targets , vol.7 , pp. 559
    • Verma, A.1    Mehta, K.2
  • 165
    • 34548848815 scopus 로고    scopus 로고
    • Tissue transglutaminase-mediated chemoresistance in cancer cells
    • Verma, A. and Mehta, K. (2007) Tissue transglutaminase-mediated chemoresistance in cancer cells, Drug Resist. Update 10, 144.
    • (2007) Drug Resist. Update , vol.10 , pp. 144
    • Verma, A.1    Mehta, K.2
  • 166
    • 0037036409 scopus 로고    scopus 로고
    • Tissue transglutaminase protects against apoptosis by modifying the tumor suppressor protein p110 Rb
    • Boehm, J. E., Singh, U., Combs, C., Antonyak, M. A., and Cerione, R. A. (2002) Tissue transglutaminase protects against apoptosis by modifying the tumor suppressor protein p110 Rb, J. Biol. Chem. 277, 20127.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20127
    • Boehm, J.E.1    Singh, U.2    Combs, C.3    Antonyak, M.A.4    Cerione, R.A.5
  • 167
    • 0037177889 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase activity is required for retinoic acid-induced expression and activation of the tissue transglutaminase
    • Antonyak, M. A., Boehm, J. E., and Cerione, R. A. (2002) Phosphoinositide 3-kinase activity is required for retinoic acid-induced expression and activation of the tissue transglutaminase, J. Biol. Chem. 277, 14712.
    • (2002) J. Biol. Chem. , vol.277 , pp. 14712
    • Antonyak, M.A.1    Boehm, J.E.2    Cerione, R.A.3
  • 168
    • 0038521257 scopus 로고    scopus 로고
    • Activation of the Ras-ERK pathway inhibits retinoic acid-induced stimulation of tissue transglutaminase expression in NIH3T3 cells
    • Antonyak, M. A., McNeill, C. J., Wakshlag, J. J., Boehm, J. E., and Cerione, R. A. (2003) Activation of the Ras-ERK pathway inhibits retinoic acid-induced stimulation of tissue transglutaminase expression in NIH3T3 cells, J. Biol. Chem. 278, 15859.
    • (2003) J. Biol. Chem. , vol.278 , pp. 15859
    • Antonyak, M.A.1    McNeill, C.J.2    Wakshlag, J.J.3    Boehm, J.E.4    Cerione, R.A.5
  • 170
    • 34250864795 scopus 로고    scopus 로고
    • Protein turnover via autophagy: implications for metabolism
    • Mizushima, N. and Klionsky, D. J. (2007) Protein turnover via autophagy: implications for metabolism, Annu. Rev. Nutr. 27, 19.
    • (2007) Annu. Rev. Nutr. , vol.27 , pp. 19
    • Mizushima, N.1    Klionsky, D.J.2
  • 171
    • 36249025723 scopus 로고    scopus 로고
    • Autophagy: process and function
    • Mizushima, N. (2007) Autophagy: process and function, Genes Dev. 21, 2861.
    • (2007) Genes Dev , vol.21 , pp. 2861
    • Mizushima, N.1
  • 172
    • 41749114288 scopus 로고    scopus 로고
    • Autophagy: basic principles and relevance to disease
    • Kundu, M. and Thompson, C. B. (2008) Autophagy: basic principles and relevance to disease, Annu. Rev. Pathol. 3, 427.
    • (2008) Annu. Rev. Pathol. , vol.3 , pp. 427
    • Kundu, M.1    Thompson, C.B.2
  • 173
    • 1842583789 scopus 로고    scopus 로고
    • Development by self-digestion: molecular mechanisms and biological functions of autophagy
    • Levine, B. and Klionsky, D. J. (2004) Development by self-digestion: molecular mechanisms and biological functions of autophagy, Dev. Cell 6, 463.
    • (2004) Dev. Cell , vol.6 , pp. 463
    • Levine, B.1    Klionsky, D.J.2
  • 174
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • Levine, B. and Kroemer, G. (2008) Autophagy in the pathogenesis of disease, Cell 132, 27.
    • (2008) Cell , vol.132 , pp. 27
    • Levine, B.1    Kroemer, G.2
  • 175
    • 33750322790 scopus 로고    scopus 로고
    • Autophagy in innate immunity against intracellular bacteria
    • Amano, A., Nakagawa, I., and Yoshimori, T. (2006) Autophagy in innate immunity against intracellular bacteria, J. Biochem. 140, 161.
    • (2006) J. Biochem. , vol.140 , pp. 161
    • Amano, A.1    Nakagawa, I.2    Yoshimori, T.3
  • 176
    • 34548700796 scopus 로고    scopus 로고
    • Unveiling the roles of autophagy in innate and adaptive immunity
    • Levine, B. and Deretic, V. (2007) Unveiling the roles of autophagy in innate and adaptive immunity, Nat. Rev. Immunol. 7, 767.
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 767
    • Levine, B.1    Deretic, V.2
  • 178
    • 66349135139 scopus 로고    scopus 로고
    • An executioner caspase regulates autophagy
    • Hou, Y. C., Hannigan, A. M., and Gorski, S.M. (2009) An executioner caspase regulates autophagy, Autophagy 5, 530.
    • (2009) Autophagy , vol.5 , pp. 530
    • Hou, Y.C.1    Hannigan, A.M.2    Gorski, S.M.3
  • 179
    • 35448981935 scopus 로고    scopus 로고
    • Autophagy: from phenomenology to molecular understanding in less than a decade
    • Klionsky, D. J. (2007) Autophagy: from phenomenology to molecular understanding in less than a decade, Nat. Rev. Mol. Cell Biol. 8, 931.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 931
    • Klionsky, D.J.1
  • 180
    • 3142677196 scopus 로고    scopus 로고
    • Cargo proteins facilitate the formation of transport vesicles in the cytoplasm to vacuole targeting pathway
    • Shintani, T. and Klionsky,D. J. (2004) Cargo proteins facilitate the formation of transport vesicles in the cytoplasm to vacuole targeting pathway, J. Biol. Chem. 279, 29889.
    • (2004) J. Biol. Chem. , vol.279 , pp. 29889
    • Shintani, T.1    Klionsky, D.J.2
  • 181
    • 20344387475 scopus 로고    scopus 로고
    • Autophagy: dual roles in life and death?
    • Baehrecke, E. H. (2005) Autophagy: dual roles in life and death? Nat. Rev. Mol. Cell Biol. 6, 505.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 505
    • Baehrecke, E.H.1
  • 183
    • 12944303650 scopus 로고    scopus 로고
    • Growth factor regulation of autophagy and cell survival in the absence of apoptosis
    • Lum, J. J., Bauer, D. E., Kong, M., Harris, M. H., Li, C., Lindsten, T., and Thompson, C. B. (2005) Growth factor regulation of autophagy and cell survival in the absence of apoptosis, Cell 120, 237.
    • (2005) Cell , vol.120 , pp. 237
    • Lum, J.J.1    Bauer, D.E.2    Kong, M.3    Harris, M.H.4    Li, C.5    Lindsten, T.6    Thompson, C.B.7
  • 184
    • 44649101436 scopus 로고    scopus 로고
    • p53: The Janus of autophagy?
    • Levine, B. and Abrams, J. (2008) p53: The Janus of autophagy? Nat. Cell Biol. 10, 637.
    • (2008) Nat. Cell Biol , vol.10 , pp. 637
    • Levine, B.1    Abrams, J.2
  • 185
    • 33749052075 scopus 로고    scopus 로고
    • Signalling and autophagy regulation in health, aging and disease
    • Meijer, A. J. and Codogno, P. (2006) Signalling and autophagy regulation in health, aging and disease, Mol. Aspects Med. 27, 411.
    • (2006) Mol. Aspects Med. , vol.27 , pp. 411
    • Meijer, A.J.1    Codogno, P.2
  • 188
    • 35848967804 scopus 로고    scopus 로고
    • How to interpret LC3 immunoblotting
    • Mizushima, N. and Yoshimori, T. (2007) How to interpret LC3 immunoblotting, Autophagy 3, 542.
    • (2007) Autophagy , vol.3 , pp. 542
    • Mizushima, N.1    Yoshimori, T.2
  • 189
    • 64749103447 scopus 로고    scopus 로고
    • Inhibition of lysosomal functions reduces proteasomal activity
    • Qiao, L. and Zhang, J. (2009) Inhibition of lysosomal functions reduces proteasomal activity, Neurosci. Lett. 456, 15.
    • (2009) Neurosci. Lett. , vol.456 , pp. 15
    • Qiao, L.1    Zhang, J.2
  • 194
    • 9144241175 scopus 로고    scopus 로고
    • Inhibition of transglutaminase activity reduces extracellular matrix accumulation induced by high glucose levels in proximal tubular epithelial cells
    • Skill, N. J., Johnson, T. S., Coutts, I. G., Saint, R. E., Fisher, M., Huang, L., El Nahas, A. M., Collighan, R. J., and Griffin, M. (2004) Inhibition of transglutaminase activity reduces extracellular matrix accumulation induced by high glucose levels in proximal tubular epithelial cells, J. Biol. Chem. 279, 47754.
    • (2004) J. Biol. Chem. , vol.279 , pp. 47754
    • Skill, N.J.1    Johnson, T.S.2    Coutts, I.G.3    Saint, R.E.4    Fisher, M.5    Huang, L.6    El Nahas, A.M.7    Collighan, R.J.8    Griffin, M.9
  • 198
    • 62949109449 scopus 로고    scopus 로고
    • Transdab wiki: the interactive transglutaminase substrate database on web 2.0 surface
    • Csosz, E., Mesko, B., and Fesus, L. (2009) Transdab wiki: the interactive transglutaminase substrate database on web 2.0 surface, Amino Acids 36, 615.
    • (2009) Amino Acids , vol.36 , pp. 615
    • Csosz, E.1    Mesko, B.2    Fesus, L.3
  • 199
    • 0034747685 scopus 로고    scopus 로고
    • Gene disruption of tissue transglutaminase
    • De Laurenzi, V. and Melino, G. (2001) Gene disruption of tissue transglutaminase, Mol. Cell Biol. 21, 148.
    • (2001) Mol. Cell Biol. , vol.21 , pp. 148
    • De Laurenzi, V.1    Melino, G.2
  • 204
    • 21344434592 scopus 로고    scopus 로고
    • Transglutaminase and diseases of the central nervous system
    • Hoffner, G. and Djian, P. (2005) Transglutaminase and diseases of the central nervous system, Front. Biosci. 10, 3078.
    • (2005) Front. Biosci. , vol.10 , pp. 3078
    • Hoffner, G.1    Djian, P.2
  • 208
    • 34247153086 scopus 로고    scopus 로고
    • Tissue transglutaminase expression promotes cell attachment, invasion and survival in breast cancer cells
    • Mangala, L. S., Fok, J. Y., Zorrilla-Calancha, I. R., Verma, A., and Mehta, K. (2007) Tissue transglutaminase expression promotes cell attachment, invasion and survival in breast cancer cells, Oncogene 26, 2459.
    • (2007) Oncogene , vol.26 , pp. 2459
    • Mangala, L.S.1    Fok, J.Y.2    Zorrilla-Calancha, I.R.3    Verma, A.4    Mehta, K.5
  • 209
    • 32844474694 scopus 로고    scopus 로고
    • The role of transglutaminase-2 and its substrates in human diseases
    • Facchiano, F., Facchiano, A., and Facchiano, A. M. (2006) The role of transglutaminase-2 and its substrates in human diseases, Front. Biosci. 11, 1758.
    • (2006) Front. Biosci. , vol.11 , pp. 1758
    • Facchiano, F.1    Facchiano, A.2    Facchiano, A.M.3
  • 210
    • 0035318470 scopus 로고    scopus 로고
    • Apoptosis in autoimmune diseases
    • Eguchi, K. (2001) Apoptosis in autoimmune diseases, Intern. Med. 40, 275.
    • (2001) Intern. Med. , vol.40 , pp. 275
    • Eguchi, K.1
  • 212
    • 0036884424 scopus 로고    scopus 로고
    • A blast from the past: clearance of apoptotic cells regulates immune responses
    • Savill, J., Dransfield, I., Gregory, C., and Haslett, C. (2002) A blast from the past: clearance of apoptotic cells regulates immune responses, Nat. Rev. Immunol. 2, 965.
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 965
    • Savill, J.1    Dransfield, I.2    Gregory, C.3    Haslett, C.4
  • 213
    • 18944366339 scopus 로고    scopus 로고
    • Transglutaminase type II is a key element in the regulation of the antiinflammatory response elicited by apoptotic cell engulfment
    • Falasca, L., Iadevaia, V., Ciccosanti, F., Melino, G., Serafino, A., and Piacentini, M. (2005) Transglutaminase type II is a key element in the regulation of the antiinflammatory response elicited by apoptotic cell engulfment, J. Immunol. 174, 7330.
    • (2005) J. Immunol. , vol.174 , pp. 7330
    • Falasca, L.1    Iadevaia, V.2    Ciccosanti, F.3    Melino, G.4    Serafino, A.5    Piacentini, M.6
  • 214
    • 0036479125 scopus 로고    scopus 로고
    • MK2 targets AU-rich elements and regulates biosynthesis of tumor necrosis factor and interleukin-6 independently at different post-transcriptional levels
    • Neininger, A., Kontoyiannis, D., Kotlyarov, A., Winzen, R., Eckert, R., Volk, H. D., Holtmann, H., Kollias, G., and Gaestel, M. (2002) MK2 targets AU-rich elements and regulates biosynthesis of tumor necrosis factor and interleukin-6 independently at different post-transcriptional levels, J. Biol. Chem. 277, 3065.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3065
    • Neininger, A.1    Kontoyiannis, D.2    Kotlyarov, A.3    Winzen, R.4    Eckert, R.5    Volk, H.D.6    Holtmann, H.7    Kollias, G.8    Gaestel, M.9
  • 215
    • 0035889959 scopus 로고    scopus 로고
    • Selective activation of p38 mitogen-activated protein kinase cascade in human neutrophils stimulated by IL-1beta
    • Suzuki, K., Hino, M., Kutsuna, H., Hato, F., Sakamoto, C., Takahashi, T., Tatsumi, N., and Kitagawa, S. (2001) Selective activation of p38 mitogen-activated protein kinase cascade in human neutrophils stimulated by IL-1beta, J. Immunol. 167, 5940.
    • (2001) J. Immunol. , vol.167 , pp. 5940
    • Suzuki, K.1    Hino, M.2    Kutsuna, H.3    Hato, F.4    Sakamoto, C.5    Takahashi, T.6    Tatsumi, N.7    Kitagawa, S.8
  • 216
    • 0029664650 scopus 로고    scopus 로고
    • Role of CSB/p38/RK stress response kinase in LPS and cytokine signaling mechanisms
    • Lee, J. C. and Young, P. R. (1996) Role of CSB/p38/RK stress response kinase in LPS and cytokine signaling mechanisms, J. Leukoc. Biol. 59, 152.
    • (1996) J. Leukoc. Biol. , vol.59 , pp. 152
    • Lee, J.C.1    Young, P.R.2
  • 217
    • 0035106949 scopus 로고    scopus 로고
    • SJL and NOD macrophages are uniquely characterized by genetically programmed, elevated expression of the IL-12(p40) gene, suggesting a conserved pathway for the induction of organ-specific autoimmunity
    • Alleva, D. G., Johnson, E. B., Wilson, J., Beller, D. I., and Conlon, P. J. (2001) SJL and NOD macrophages are uniquely characterized by genetically programmed, elevated expression of the IL-12(p40) gene, suggesting a conserved pathway for the induction of organ-specific autoimmunity, J. Leukoc. Biol. 69, 440.
    • (2001) J. Leukoc. Biol. , vol.69 , pp. 440
    • Alleva, D.G.1    Johnson, E.B.2    Wilson, J.3    Beller, D.I.4    Conlon, P.J.5
  • 218
    • 0033939014 scopus 로고    scopus 로고
    • Aberrant macrophage cytokine production is a conserved feature among autoimmune-prone mouse strains: elevated interleukin (IL)-12 and an imbalance in tumor necrosis factoralpha and IL-10 define a unique cytokine profile in macrophages from young nonobese diabetic mice
    • Alleva, D. G., Pavlovich, R. P., Grant, C., Kaser, S. B., and Beller, D. I. (2000) Aberrant macrophage cytokine production is a conserved feature among autoimmune-prone mouse strains: elevated interleukin (IL)-12 and an imbalance in tumor necrosis factoralpha and IL-10 define a unique cytokine profile in macrophages from young nonobese diabetic mice, Diabetes 49, 1106.
    • (2000) Diabetes , vol.49 , pp. 1106
    • Alleva, D.G.1    Pavlovich, R.P.2    Grant, C.3    Kaser, S.B.4    Beller, D.I.5
  • 219
    • 0036644326 scopus 로고    scopus 로고
    • Aberrant production of IL-12 by macrophages from several autoimmune-prone mouse strains is characterized by intrinsic and unique patterns of NF-kappa B expression and binding to the IL-12 p40 promoter
    • Liu, J. and Beller, D. (2002) Aberrant production of IL-12 by macrophages from several autoimmune-prone mouse strains is characterized by intrinsic and unique patterns of NF-kappa B expression and binding to the IL-12 p40 promoter, J. Immunol. 169, 581.
    • (2002) J. Immunol. , vol.169 , pp. 581
    • Liu, J.1    Beller, D.2
  • 220
    • 33847404337 scopus 로고    scopus 로고
    • Autophagy gene-dependent clearance of apoptotic cells during embryonic development
    • Qu, X., Zou, Z., Sun, Q., Luby-Phelps, K., Cheng, P., Hogan, R. N., Gilpin, C., and Levine, B. (2007) Autophagy gene-dependent clearance of apoptotic cells during embryonic development, Cell 128, 931.
    • (2007) Cell , vol.128 , pp. 931
    • Qu, X.1    Zou, Z.2    Sun, Q.3    Luby-Phelps, K.4    Cheng, P.5    Hogan, R.N.6    Gilpin, C.7    Levine, B.8
  • 221
    • 0043069548 scopus 로고    scopus 로고
    • Therapeutic approaches to innate immunity: severe sepsis and septic shock
    • Lolis, E. and Bucala, R. (2003) Therapeutic approaches to innate immunity: severe sepsis and septic shock, Nat. Rev. Drug Discov. 2, 635.
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 635
    • Lolis, E.1    Bucala, R.2
  • 222
    • 28944436170 scopus 로고    scopus 로고
    • Contribution of antiinflammatory/ immune suppressive processes to the pathology of sepsis
    • Perl,M., Chung, C. S., Garber,M., Huang, X., and Ayala, A. (2006) Contribution of antiinflammatory/ immune suppressive processes to the pathology of sepsis, Front. Biosci. 11, 272.
    • (2006) Front. Biosci. , vol.11 , pp. 272
    • Perl, M.1    Chung, C.S.2    Garber, M.3    Huang, X.4    Ayala, A.5
  • 223
    • 75549084325 scopus 로고    scopus 로고
    • Cell death in sepsis: a matter of how, when, and where
    • Bantel, H. and Schulze-Osthoff, K. (2009) Cell death in sepsis: a matter of how, when, and where, Crit. Care 13, 173.
    • (2009) Crit. Care , vol.13 , pp. 173
    • Bantel, H.1    Schulze-Osthoff, K.2
  • 224
    • 47249103385 scopus 로고    scopus 로고
    • Role of Programmed Cell Death in the Immunopathogenesis of Sepsis
    • Perl,M., Chung, C. S., Swan, R., and Ayala, A. (2007) Role of Programmed Cell Death in the Immunopathogenesis of Sepsis, Drug Discov. Today Dis. Mech. 4, 223.
    • (2007) Drug Discov. Today Dis. Mech. , vol.4 , pp. 223
    • Perl, M.1    Chung, C.S.2    Swan, R.3    Ayala, A.4
  • 225
    • 0031057128 scopus 로고    scopus 로고
    • Increase in transglutaminase and its extracellular products in response to an inflammatory stimulus by lipopolysaccharide
    • Bowness, J. M. and Tarr, A. H. (1997) Increase in transglutaminase and its extracellular products in response to an inflammatory stimulus by lipopolysaccharide, Mol. Cell Biochem. 169, 157.
    • (1997) Mol. Cell Biochem. , vol.169 , pp. 157
    • Bowness, J.M.1    Tarr, A.H.2
  • 226
    • 0020411865 scopus 로고
    • Enhanced transglutaminase activity associated with macrophage activation. Possible role in Fc-mediated phagocytosis
    • Leu, R. W., Herriott, M. J., Moore, P. E., Orr, G. R., and Birckbichler, P. J. (1982) Enhanced transglutaminase activity associated with macrophage activation. Possible role in Fc-mediated phagocytosis, Exp. Cell Res. 141, 191.
    • (1982) Exp. Cell Res. , vol.141 , pp. 191
    • Leu, R.W.1    Herriott, M.J.2    Moore, P.E.3    Orr, G.R.4    Birckbichler, P.J.5
  • 229
    • 33645116785 scopus 로고    scopus 로고
    • NF-kappa B activation as a pathological mechanism of septic shock and inflammation
    • Liu, S. F. and Malik, A. B. (2006) NF-kappa B activation as a pathological mechanism of septic shock and inflammation, Am. J. Physiol. Lung Cell Mol. Physiol. 290, L622.
    • (2006) Am. J. Physiol. Lung Cell Mol. Physiol , vol.290
    • Liu, S.F.1    Malik, A.B.2
  • 230
    • 0023724778 scopus 로고
    • I kappa B: a specific inhibitor of the NF-kappa B transcription factor
    • Baeuerle, P. A. and Baltimore, D. (1988) I kappa B: a specific inhibitor of the NF-kappa B transcription factor, Science 242, 540.
    • (1988) Science , vol.242 , pp. 540
    • Baeuerle, P.A.1    Baltimore, D.2
  • 231
    • 11144233953 scopus 로고    scopus 로고
    • Transglutaminase 2 induces nuclear factor-kappaB activation via a novel pathway in BV-2 microglia
    • Lee, J., Kim, Y. S., Choi, D. H., Bang, M. S., Han, T. R., Joh, T. H., and Kim, S. Y. (2004) Transglutaminase 2 induces nuclear factor-kappaB activation via a novel pathway in BV-2 microglia, J. Biol. Chem. 279, 53725.
    • (2004) J. Biol. Chem. , vol.279 , pp. 53725
    • Lee, J.1    Kim, Y.S.2    Choi, D.H.3    Bang, M.S.4    Han, T.R.5    Joh, T.H.6    Kim, S.Y.7
  • 232
    • 65349106651 scopus 로고    scopus 로고
    • Persistent elevated tissuetransglutaminase in cystic fibrosis
    • Hasosah, M., Davidson, G., and Jacobson, K. (2009) Persistent elevated tissuetransglutaminase in cystic fibrosis, J. Paediatr. Child Health 45, 172.
    • (2009) J. Paediatr. Child Health , vol.45 , pp. 172
    • Hasosah, M.1    Davidson, G.2    Jacobson, K.3
  • 235
    • 0033940437 scopus 로고    scopus 로고
    • Late-onset neurodegenerative diseases-the role of protein insolubility
    • Johnson, W. G. (2000) Late-onset neurodegenerative diseases-the role of protein insolubility, J. Anat. 196(Pt 4), 609.
    • (2000) J. Anat. , vol.196 , Issue.PT 4 , pp. 609
    • Johnson, W.G.1
  • 237
    • 0022156464 scopus 로고
    • Neuronal origin of a cerebral amyloid: neurofibrillary tangles of Alzheimer's disease contain the same protein as the amyloid of plaque cores and blood vessels
    • Masters, C. L.,Multhaup, G., Simms, G., Pottgiesser, J.,Martins, R. N., and Beyreuther, K. (1985) Neuronal origin of a cerebral amyloid: neurofibrillary tangles of Alzheimer's disease contain the same protein as the amyloid of plaque cores and blood vessels, Embo J. 4, 2757.
    • (1985) Embo J , vol.4 , pp. 2757
    • Masters, C.L.1    Multhaup, G.2    Simms, G.3    Pottgiesser, J.4    Martins, R.N.5    Beyreuther, K.6
  • 239
    • 0022980104 scopus 로고
    • Alzheimer's disease: Tau proteins, the promoting factors of microtubule assembly, are major components of paired helical filaments
    • Delacourte, A. andDefossez, A. (1986) Alzheimer's disease: Tau proteins, the promoting factors of microtubule assembly, are major components of paired helical filaments, J. Neurol. Sci. 76, 173.
    • (1986) J. Neurol. Sci. , vol.76 , pp. 173
    • Delacourte, A.1    Defossez, A.2
  • 240
    • 0009364134 scopus 로고
    • Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease
    • Kosik, K. S., Joachim, C. L., and Selkoe, D. J. (1986) Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease, Proc. Natl. Acad. Sci. U.S.A. 83, 4044.
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 4044
    • Kosik, K.S.1    Joachim, C.L.2    Selkoe, D.J.3
  • 241
    • 0026551711 scopus 로고
    • The switch of tau protein to an Alzheimer-like state includes the phosphorylation of two serine-proline motifs upstream of the microtubule binding region
    • Biernat, J., et al. (1992) The switch of tau protein to an Alzheimer-like state includes the phosphorylation of two serine-proline motifs upstream of the microtubule binding region, Embo J. 11, 1593.
    • (1992) Embo J , vol.11 , pp. 1593
    • Biernat, J.1
  • 242
    • 0026799198 scopus 로고
    • The microtubule binding repeats of tau protein assemble into filaments like those found in Alzheimer's disease
    • Crowther, R. A., Olesen, O. F., Jakes, R., and Goedert, M. (1992) The microtubule binding repeats of tau protein assemble into filaments like those found in Alzheimer's disease, FEBS Lett. 309, 199.
    • (1992) FEBS Lett , vol.309 , pp. 199
    • Crowther, R.A.1    Olesen, O.F.2    Jakes, R.3    Goedert, M.4
  • 243
    • 0026595846 scopus 로고
    • Tau proteins of Alzheimer paired helical filaments: abnormal phosphorylation of all six brain isoforms
    • Goedert, M., Spillantini, M. G., Cairns, N. J., and Crowther, R. A. (1992) Tau proteins of Alzheimer paired helical filaments: abnormal phosphorylation of all six brain isoforms, Neuron 8, 159.
    • (1992) Neuron , vol.8 , pp. 159
    • Goedert, M.1    Spillantini, M.G.2    Cairns, N.J.3    Crowther, R.A.4
  • 244
    • 3242861077 scopus 로고    scopus 로고
    • Localization of transglutaminase in hippocampal neurons: implications for Alzheimer's disease
    • Appelt, D. M., Kopen, G. C., Boyne, L. J., and Balin, B. J. (1996) Localization of transglutaminase in hippocampal neurons: implications for Alzheimer's disease, J. Histochem. Cytochem. 44, 1421.
    • (1996) J. Histochem. Cytochem. , vol.44 , pp. 1421
    • Appelt, D.M.1    Kopen, G.C.2    Boyne, L.J.3    Balin, B.J.4
  • 245
    • 0022627398 scopus 로고
    • Transglutaminase and the neuronal cytoskeleton in Alzheimer's disease
    • Miller,C.C. and Anderton, B. H. (1986) Transglutaminase and the neuronal cytoskeleton in Alzheimer's disease, J. Neurochem. 46, 1912.
    • (1986) J. Neurochem. , vol.46 , pp. 1912
    • Miller, C.C.1    Anderton, B.H.2
  • 246
    • 0031015814 scopus 로고    scopus 로고
    • The association of tissue transglutaminase with human recombinant tau results in the formation of insoluble filamentous structures
    • Appelt, D. M. and Balin, B. J. (1997) The association of tissue transglutaminase with human recombinant tau results in the formation of insoluble filamentous structures, Brain Res. 745, 21.
    • (1997) Brain Res , vol.745 , pp. 21
    • Appelt, D.M.1    Balin, B.J.2
  • 247
    • 0029096258 scopus 로고
    • Transglutaminase cross-linking of the tau protein
    • Miller, M. L. and Johnson, G. V. (1995) Transglutaminase cross-linking of the tau protein, J. Neurochem. 65, 1760.
    • (1995) J. Neurochem. , vol.65 , pp. 1760
    • Miller, M.L.1    Johnson, G.V.2
  • 249
    • 0027176364 scopus 로고
    • The relationship between trinucleotide (CAG) repeat length and clinical features of Huntington's disease
    • Andrew, S. E., et al. (1993) The relationship between trinucleotide (CAG) repeat length and clinical features of Huntington's disease, Nat. Genet. 4, 398.
    • (1993) Nat. Genet. , vol.4 , pp. 398
    • Andrew, S.E.1
  • 251
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia, M., Sapp, E., Chase, K. O., Davies, S. W., Bates, G. P., Vonsattel, J. P., and Aronin, N. (1997) Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain, Science 277, 1990.
    • (1997) Science , vol.277 , pp. 1990
    • DiFiglia, M.1    Sapp, E.2    Chase, K.O.3    Davies, S.W.4    Bates, G.P.5    Vonsattel, J.P.6    Aronin, N.7
  • 252
    • 0032475931 scopus 로고    scopus 로고
    • Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
    • Saudou, F., Finkbeiner, S., Devys, D., and Greenberg, M. E. (1998) Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions, Cell 95, 55.
    • (1998) Cell , vol.95 , pp. 55
    • Saudou, F.1    Finkbeiner, S.2    Devys, D.3    Greenberg, M.E.4
  • 253
    • 0032522165 scopus 로고    scopus 로고
    • Tissue transglutaminase-catalyzed formation of high-molecularweight aggregates in vitro is favored with long polyglutamine domains: a possible mechanism contributing to CAG-triplet diseases
    • Gentile, V., Sepe, C., Calvani, M.,Melone,M. A., Cotrufo, R., Cooper, A. J., Blass, J. P., and Peluso, G. (1998) Tissue transglutaminase-catalyzed formation of high-molecularweight aggregates in vitro is favored with long polyglutamine domains: a possible mechanism contributing to CAG-triplet diseases, Arch. Biochem. Biophys. 352, 314.
    • (1998) Arch. Biochem. Biophys. , vol.352 , pp. 314
    • Gentile, V.1    Sepe, C.2    Calvani, M.3    Melone, M.A.4    Cotrufo, R.5    Cooper, A.J.6    Blass, J.P.7    Peluso, G.8
  • 254
    • 0034257067 scopus 로고    scopus 로고
    • Tissue transglutaminase: a possible role in neurodegenerative diseases
    • Lesort, M., Tucholski, J., Miller, M. L., and Johnson, G. V. (2000) Tissue transglutaminase: a possible role in neurodegenerative diseases, Prog. Neurobiol. 61, 439.
    • (2000) Prog. Neurobiol. , vol.61 , pp. 439
    • Lesort, M.1    Tucholski, J.2    Miller, M.L.3    Johnson, G.V.4
  • 255
    • 0033794508 scopus 로고    scopus 로고
    • Impaired mitochondrial function results in increased tissue transglutaminase activity in situ
    • Lesort, M., Tucholski, J., Zhang, J., and Johnson, G. V. (2000) Impaired mitochondrial function results in increased tissue transglutaminase activity in situ, J. Neurochem. 75, 1951.
    • (2000) J. Neurochem. , vol.75 , pp. 1951
    • Lesort, M.1    Tucholski, J.2    Zhang, J.3    Johnson, G.V.4
  • 256
    • 56449083411 scopus 로고    scopus 로고
    • Autophagy in neurodegeneration and development
    • Winslow, A. R. and Rubinsztein, D. C. (2008) Autophagy in neurodegeneration and development, Biochim. Biophys. Acta 1782, 723.
    • (2008) Biochim. Biophys. Acta , vol.1782 , pp. 723
    • Winslow, A.R.1    Rubinsztein, D.C.2
  • 258
    • 0037194894 scopus 로고    scopus 로고
    • A novel protein complex linking the delta 2 glutamate receptor and autophagy: implications for neurodegeneration in lurcher mice
    • Yue, Z., Horton, A., Bravin,M., DeJager, P. L., Selimi, F., and Heintz, N. (2002) A novel protein complex linking the delta 2 glutamate receptor and autophagy: implications for neurodegeneration in lurcher mice, Neuron 35, 921.
    • (2002) Neuron , vol.35 , pp. 921
    • Yue, Z.1    Horton, A.2    Bravin, M.3    DeJager, P.L.4    Selimi, F.5    Heintz, N.6
  • 259
    • 33847652900 scopus 로고    scopus 로고
    • Autophagy and neurodegeneration: when the cleaning crew goes on strike
    • Martinez-Vicente, M. and Cuervo, A. M. (2007) Autophagy and neurodegeneration: when the cleaning crew goes on strike, Lancet Neurol 6, 352.
    • (2007) Lancet Neurol , vol.6 , pp. 352
    • Martinez-Vicente, M.1    Cuervo, A.M.2
  • 260
    • 34247210109 scopus 로고    scopus 로고
    • Transglutaminase 2 regulates mallory body inclusion formation and injury-associated liver enlargement
    • Strnad, P., Harada, M., Siegel, M., Terkeltaub, R. A., Graham, R. M., Khosla, C., and Omary, M. B. (2007) Transglutaminase 2 regulates mallory body inclusion formation and injury-associated liver enlargement, Gastroenterology 132, 1515.
    • (2007) Gastroenterology , vol.132 , pp. 1515
    • Strnad, P.1    Harada, M.2    Siegel, M.3    Terkeltaub, R.A.4    Graham, R.M.5    Khosla, C.6    Omary, M.B.7
  • 261
    • 61649124031 scopus 로고    scopus 로고
    • The role of autophagy in pancreatic beta-cell and diabetes
    • Fujitani, Y., Kawamori, R., and Watada, H. (2009) The role of autophagy in pancreatic beta-cell and diabetes, Autophagy 5, 280.
    • (2009) Autophagy , vol.5 , pp. 280
    • Fujitani, Y.1    Kawamori, R.2    Watada, H.3
  • 263
    • 77951915586 scopus 로고    scopus 로고
    • Autophagy during cardiac stress: joys and frustrations of autophagy
    • Gottlieb, R. A. and Mentzer, R. M. (2010) Autophagy during cardiac stress: joys and frustrations of autophagy, Annu. Rev. Physiol. 72, 45.
    • (2010) Annu. Rev. Physiol. , vol.72 , pp. 45
    • Gottlieb, R.A.1    Mentzer, R.M.2
  • 264
    • 59849110194 scopus 로고    scopus 로고
    • Autophagy in ischemic heart disease
    • Gustafsson, A. B. and Gottlieb, R. A. (2009) Autophagy in ischemic heart disease, Circ. Res. 104, 150.
    • (2009) Circ. Res. , vol.104 , pp. 150
    • Gustafsson, A.B.1    Gottlieb, R.A.2
  • 265
    • 58149396003 scopus 로고    scopus 로고
    • Autophagy in load-induced heart disease
    • Rothermel, B. A. and Hill, J. A. (2008) Autophagy in load-induced heart disease, Circ. Res. 103, 1363.
    • (2008) Circ. Res. , vol.103 , pp. 1363
    • Rothermel, B.A.1    Hill, J.A.2
  • 266
    • 77950576949 scopus 로고    scopus 로고
    • Autophagy in hypertensive heart disease
    • Wang, Z. V., Rothermel, B. A., and Hill, J. A. (2010), Autophagy in hypertensive heart disease, J. Biol. Chem. 285, 8509.
    • (2010) J. Biol. Chem. , vol.285 , pp. 8509
    • Wang, Z.V.1    Rothermel, B.A.2    Hill, J.A.3
  • 267
    • 21244476364 scopus 로고    scopus 로고
    • The aging myocardium: roles of mitochondrial damage and lysosomal degradation
    • Terman, A. and Brunk, U. T. (2005) The aging myocardium: roles of mitochondrial damage and lysosomal degradation, Heart Lung Circ. 14, 107.
    • (2005) Heart Lung Circ , vol.14 , pp. 107
    • Terman, A.1    Brunk, U.T.2
  • 268
    • 27644467802 scopus 로고    scopus 로고
    • Autophagy in cardiac myocyte homeostasis, aging, and pathology
    • Terman, A. and Brunk, U. T. (2005) Autophagy in cardiac myocyte homeostasis, aging, and pathology, Cardiovasc. Res. 68, 355.
    • (2005) Cardiovasc. Res. , vol.68 , pp. 355
    • Terman, A.1    Brunk, U.T.2
  • 271
    • 67049115754 scopus 로고    scopus 로고
    • Angiotensin II type 2 receptor antagonizes angiotensin II type 1 receptor-mediated cardiomyocyte autophagy
    • Porrello, E. R., D'Amore, A., Curl, C. L., Allen, A. M., Harrap, S. B., Thomas, W. G., and Delbridge, L. M. (2009) Angiotensin II type 2 receptor antagonizes angiotensin II type 1 receptor-mediated cardiomyocyte autophagy, Hypertension 53, 1032.
    • (2009) Hypertension , vol.53 , pp. 1032
    • Porrello, E.R.1    D'Amore, A.2    Curl, C.L.3    Allen, A.M.4    Harrap, S.B.5    Thomas, W.G.6    Delbridge, L.M.7
  • 272
    • 73449127222 scopus 로고    scopus 로고
    • Cardiomyocyte autophagy is regulated by angiotensin II type 1 and type 2 receptors
    • Porrello, E. R. and Delbridge, L. M. (2009) Cardiomyocyte autophagy is regulated by angiotensin II type 1 and type 2 receptors, Autophagy 5, 1215.
    • (2009) Autophagy , vol.5 , pp. 1215
    • Porrello, E.R.1    Delbridge, L.M.2
  • 273
    • 7044274535 scopus 로고    scopus 로고
    • Factor XIIIA transglutaminase crosslinks AT1 receptor dimers of monocytes at the onset of atherosclerosis
    • AbdAlla, S., Lother, H., Langer, A., El Faramawy, Y., and Quitterer, U. (2004) Factor XIIIA transglutaminase crosslinks AT1 receptor dimers of monocytes at the onset of atherosclerosis, Cell 119, 343.
    • (2004) Cell , vol.119 , pp. 343
    • AbdAlla, S.1    Lother, H.2    Langer, A.3    El Faramawy, Y.4    Quitterer, U.5
  • 274
    • 34548157657 scopus 로고    scopus 로고
    • Roles of transglutaminases in cardiac and vascular diseases
    • Sane, D. C., Kontos, J. L., and Greenberg, C. S. (2007) Roles of transglutaminases in cardiac and vascular diseases, Front. Biosci. 12, 2530.
    • (2007) Front. Biosci. , vol.12 , pp. 2530
    • Sane, D.C.1    Kontos, J.L.2    Greenberg, C.S.3


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