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Volumn 25, Issue 3, 2004, Pages 493-503

Validity of mouse models for the study of tissue transglutaminase in neurodegenerative diseases

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; MESSENGER RNA; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE;

EID: 1642336449     PISSN: 10447431     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mcn.2003.11.016     Document Type: Article
Times cited : (27)

References (70)
  • 1
    • 0023644524 scopus 로고
    • Identification of a guanosine triphosphate-binding site on guinea pig liver transglutaminase. Role of GTP and calcium ions in modulating activity
    • Achyuthan K.E., Greenberg C.S. Identification of a guanosine triphosphate-binding site on guinea pig liver transglutaminase. Role of GTP and calcium ions in modulating activity. J. Biol. Chem. 262:1987;1901-1906.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1901-1906
    • Achyuthan, K.E.1    Greenberg, C.S.2
  • 2
    • 0027516486 scopus 로고
    • Expression of tissue transglutaminase in skeletal tissues correlates with events of terminal differentiation of chondrocytes
    • Aeschlimann D., Wetterwald A., Fleisch H., Paulsson M. Expression of tissue transglutaminase in skeletal tissues correlates with events of terminal differentiation of chondrocytes. J. Cell Biol. 120:1993;1461-1470.
    • (1993) J. Cell Biol. , vol.120 , pp. 1461-1470
    • Aeschlimann, D.1    Wetterwald, A.2    Fleisch, H.3    Paulsson, M.4
  • 3
    • 1342304083 scopus 로고    scopus 로고
    • Structural basis for the coordinated regulation of transglutaminase 3 by guanine nucleotides and calcium/magnesium
    • In press
    • Ahvazi B., Boeshans K.M., Idler W., Baxa U., Steinert P.M., Rastinejad F. Structural basis for the coordinated regulation of transglutaminase 3 by guanine nucleotides and calcium/magnesium. J. Biol. Chem. 2004;. In press.
    • (2004) J. Biol. Chem.
    • Ahvazi, B.1    Boeshans, K.M.2    Idler, W.3    Baxa, U.4    Steinert, P.M.5    Rastinejad, F.6
  • 5
    • 0034002644 scopus 로고    scopus 로고
    • Sodium butyrate/retinoic acid costimulation induces apoptosis- independent growth arrest and cell differentiation in normal and ras-transformed seminal vesicle epithelial cells unresponsive to retinoic acid
    • Buommino E., Pasquali D., Sinisi A.A., Bellastella A., Morelli F., Metafora S. Sodium butyrate/retinoic acid costimulation induces apoptosis-independent growth arrest and cell differentiation in normal and ras-transformed seminal vesicle epithelial cells unresponsive to retinoic acid. J. Mol. Endocrinol. 24:2000;83-94.
    • (2000) J. Mol. Endocrinol. , vol.24 , pp. 83-94
    • Buommino, E.1    Pasquali, D.2    Sinisi, A.A.3    Bellastella, A.4    Morelli, F.5    Metafora, S.6
  • 6
    • 0029657914 scopus 로고    scopus 로고
    • Alpha1-adrenergic receptor signaling via Gh is subtype specific and independent of its transglutaminase activity
    • Chen S., Lin F., Iismaa S., Lee K.N., Birckbichler P.J., Graham R.M. Alpha1-adrenergic receptor signaling via Gh is subtype specific and independent of its transglutaminase activity. J. Biol. Chem. 271:1996;32385-32391.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32385-32391
    • Chen, S.1    Lin, F.2    Iismaa, S.3    Lee, K.N.4    Birckbichler, P.J.5    Graham, R.M.6
  • 7
    • 0034990512 scopus 로고    scopus 로고
    • Tissue transglutaminase selectively modifies proteins associated with truncated mutant huntingtin in intact cells
    • Chun W., Lesort M., Tucholski J., Faber P.W., MacDonald M.E., Ross C.A., Johnson G.V. Tissue transglutaminase selectively modifies proteins associated with truncated mutant huntingtin in intact cells. Neurobiol. Dis. 8:2001;391-404.
    • (2001) Neurobiol. Dis. , vol.8 , pp. 391-404
    • Chun, W.1    Lesort, M.2    Tucholski, J.3    Faber, P.W.4    MacDonald, M.E.5    Ross, C.A.6    Johnson, G.V.7
  • 8
    • 0035795406 scopus 로고    scopus 로고
    • Tissue transglutaminase does not contribute to the formation of mutant huntingtin aggregates
    • Chun W., Lesort M., Tucholski J., Ross C.A., Johnson G.V. Tissue transglutaminase does not contribute to the formation of mutant huntingtin aggregates. J. Cell Biol. 153:2001;25-34.
    • (2001) J. Cell Biol. , vol.153 , pp. 25-34
    • Chun, W.1    Lesort, M.2    Tucholski, J.3    Ross, C.A.4    Johnson, G.V.5
  • 9
    • 0035793583 scopus 로고    scopus 로고
    • Intron-exon swapping of transglutaminase mRNA and neuronal Tau aggregation in Alzheimer's disease
    • Citron B.A., SantaCruz K.S., Davies P.J., Festoff B.W. Intron-exon swapping of transglutaminase mRNA and neuronal Tau aggregation in Alzheimer's disease. J. Biol. Chem. 276:2001;3295-3301.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3295-3301
    • Citron, B.A.1    Santacruz, K.S.2    Davies, P.J.3    Festoff, B.W.4
  • 10
    • 0036135523 scopus 로고    scopus 로고
    • Protein crosslinking, tissue transglutaminase, alternative splicing and neurodegeneration
    • Citron B.A., Suo Z., SantaCruz K., Davies P.J., Qin F., Festoff B.W. Protein crosslinking, tissue transglutaminase, alternative splicing and neurodegeneration. Neurochem. Int. 40:2002;69-78.
    • (2002) Neurochem. Int. , vol.40 , pp. 69-78
    • Citron, B.A.1    Suo, Z.2    Santacruz, K.3    Davies, P.J.4    Qin, F.5    Festoff, B.W.6
  • 11
    • 0030906890 scopus 로고    scopus 로고
    • Polyglutamine domains are substrates of tissue transglutaminase: Does transglutaminase play a role in expanded CAG/poly-Q neurodegenerative diseases?
    • Cooper A.J., Sheu K.F., Burke J.R., Onodera O., Strittmatter W.J., Roses A.D., Blass J.P. Polyglutamine domains are substrates of tissue transglutaminase: does transglutaminase play a role in expanded CAG/poly-Q neurodegenerative diseases? J. Neurochem. 69:1997;431-434.
    • (1997) J. Neurochem. , vol.69 , pp. 431-434
    • Cooper, A.J.1    Sheu, K.F.2    Burke, J.R.3    Onodera, O.4    Strittmatter, W.J.5    Roses, A.D.6    Blass, J.P.7
  • 13
    • 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., Aronin N. Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science. 277:1997;1990-1993.
    • (1997) Science , vol.277 , pp. 1990-1993
    • 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
  • 14
    • 0027184294 scopus 로고
    • Transglutaminase catalyzes the formation of sodium dodecyl sulfate-insoluble. Alz-50-reactive polymers of tau
    • Dudek S.M., Johnson G.V. Transglutaminase catalyzes the formation of sodium dodecyl sulfate-insoluble. Alz-50-reactive polymers of tau. J. Neurochem. 61:1993;1159-1162.
    • (1993) J. Neurochem. , vol.61 , pp. 1159-1162
    • Dudek, S.M.1    Johnson, G.V.2
  • 15
    • 0028298620 scopus 로고
    • Transglutaminase facilitates the formation of polymers of the beta-amyloid peptide
    • Dudek S.M., Johnson G.V. Transglutaminase facilitates the formation of polymers of the beta-amyloid peptide. Brain Res. 651:1994;129-133.
    • (1994) Brain Res. , vol.651 , pp. 129-133
    • Dudek, S.M.1    Johnson, G.V.2
  • 16
    • 0036312181 scopus 로고    scopus 로고
    • Recent advances in Huntington's disease: Implications for experimental therapeutics
    • Feigin A., Zgaljardic D. Recent advances in Huntington's disease: implications for experimental therapeutics. Curr. Opin. Neurol. 15:2002;483-489.
    • (2002) Curr. Opin. Neurol. , vol.15 , pp. 483-489
    • Feigin, A.1    Zgaljardic, D.2
  • 17
    • 0036312393 scopus 로고    scopus 로고
    • Injury-induced "switch" from GTP-regulated to novel GTP-independent isoform of tissue transglutaminase in the rat spinal cord
    • Festoff B.W., SantaCruz K., Arnold P.M., Sebastian C.T., Davies P.J., Citron B.A. Injury-induced "switch" from GTP-regulated to novel GTP-independent isoform of tissue transglutaminase in the rat spinal cord. J. Neurochem. 81:2002;708-718.
    • (2002) J. Neurochem. , vol.81 , pp. 708-718
    • Festoff, B.W.1    Santacruz, K.2    Arnold, P.M.3    Sebastian, C.T.4    Davies, P.J.5    Citron, B.A.6
  • 18
    • 0023159034 scopus 로고
    • Induction and activation of tissue transglutaminase during programmed cell death
    • Fesus L., Thomazy V., Falus A. Induction and activation of tissue transglutaminase during programmed cell death. FEBS Lett. 224:1987;104-108.
    • (1987) FEBS Lett. , vol.224 , pp. 104-108
    • Fesus, L.1    Thomazy, V.2    Falus, A.3
  • 20
    • 0026338017 scopus 로고
    • Transglutaminases: Multifunctional cross-linking enzymes that stabilize tissues
    • Greenberg C.S., Birckbichler P.J., Rice R.H. Transglutaminases: multifunctional cross-linking enzymes that stabilize tissues. FASEB J. 5:1991;3071-3077.
    • (1991) FASEB J. , vol.5 , pp. 3071-3077
    • Greenberg, C.S.1    Birckbichler, P.J.2    Rice, R.H.3
  • 21
    • 0032824155 scopus 로고    scopus 로고
    • Tissue transglutaminase is expressed, active, and directly involved in rat dermal wound healing and angiogenesis
    • Haroon Z.A., Hettasch J.M., Lai T.S., Dewhirst M.W., Greenberg C.S. Tissue transglutaminase is expressed, active, and directly involved in rat dermal wound healing and angiogenesis. FASEB J. 13:1999;1787-1795.
    • (1999) FASEB J. , vol.13 , pp. 1787-1795
    • Haroon, Z.A.1    Hettasch, J.M.2    Lai, T.S.3    Dewhirst, M.W.4    Greenberg, C.S.5
  • 22
    • 0033607637 scopus 로고    scopus 로고
    • Transglutaminase type 1 and its cross-linking activity are concentrated at adherens junctions in simple epithelial cells
    • Hiiragi T., Sasaki H., Nagafuchi A., Sabe H., Shen S.C., Matsuki M., Yamanishi K., Tsukita S. Transglutaminase type 1 and its cross-linking activity are concentrated at adherens junctions in simple epithelial cells. J. Biol. Chem. 274:1999;34148-34154.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34148-34154
    • Hiiragi, T.1    Sasaki, H.2    Nagafuchi, A.3    Sabe, H.4    Shen, S.C.5    Matsuki, M.6    Yamanishi, K.7    Tsukita, S.8
  • 23
    • 0035013377 scopus 로고    scopus 로고
    • Analysis of epidermal-type transglutaminase (TGase 3) expression in mouse tissues and cell lines
    • Hitomi K., Horio Y., Ikura K., Yamanishi K., Maki M. Analysis of epidermal-type transglutaminase (TGase 3) expression in mouse tissues and cell lines. Int. J. Biochem. Cell Biol. 33:2001;491-498.
    • (2001) Int. J. Biochem. Cell Biol. , vol.33 , pp. 491-498
    • Hitomi, K.1    Horio, Y.2    Ikura, K.3    Yamanishi, K.4    Maki, M.5
  • 24
    • 0028177277 scopus 로고
    • Cross-linking of beta-amyloid protein precursor catalyzed by tissue transglutaminase
    • Ho G.J., Gregory E.J., Smirnova I.V., Zoubine M.N., Festoff B.W. Cross-linking of beta-amyloid protein precursor catalyzed by tissue transglutaminase. FEBS Lett. 349:1994;151-154.
    • (1994) FEBS Lett. , vol.349 , pp. 151-154
    • Ho, G.J.1    Gregory, E.J.2    Smirnova, I.V.3    Zoubine, M.N.4    Festoff, B.W.5
  • 25
    • 0037049234 scopus 로고    scopus 로고
    • NMDA-evoked excitotoxicity increases tissue transglutaminase in cerebellar granule cells
    • Ientile R., Caccamo D., Macaione V., Torre V., Macaione S. NMDA-evoked excitotoxicity increases tissue transglutaminase in cerebellar granule cells. Neuroscience. 115:2002;723-729.
    • (2002) Neuroscience , vol.115 , pp. 723-729
    • Ientile, R.1    Caccamo, D.2    MacAione, V.3    Torre, V.4    MacAione, S.5
  • 26
    • 0027289153 scopus 로고
    • Cross-linking of a synthetic partial-length (1-28) peptide of the Alzheimer beta/A4 amyloid protein by transglutaminase
    • Ikura K., Takahata K., Sasaki R. Cross-linking of a synthetic partial-length (1-28) peptide of the Alzheimer beta/A4 amyloid protein by transglutaminase. FEBS Lett. 326:1993;109-111.
    • (1993) FEBS Lett. , vol.326 , pp. 109-111
    • Ikura, K.1    Takahata, K.2    Sasaki, R.3
  • 29
    • 0037452813 scopus 로고    scopus 로고
    • Tissue transglutaminase-induced aggregation of alpha-synuclein: Implications for Lewy body formation in Parkinson's disease and dementia with Lewy bodies
    • Junn E., Ronchetti R.D., Quezado M.M., Kim S.Y., Mouradian M.M. Tissue transglutaminase-induced aggregation of alpha-synuclein: implications for Lewy body formation in Parkinson's disease and dementia with Lewy bodies. Proc. Natl. Acad. Sci. U. S. A. 100:2003;2047-2052.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 2047-2052
    • Junn, E.1    Ronchetti, R.D.2    Quezado, M.M.3    Kim, S.Y.4    Mouradian, M.M.5
  • 30
    • 0032014092 scopus 로고    scopus 로고
    • Transglutaminase action imitates Huntington's disease: Selective polymerization of Huntingtin containing expanded polyglutamine
    • Kahlem P., Green H., Djian P. Transglutaminase action imitates Huntington's disease: selective polymerization of Huntingtin containing expanded polyglutamine. Mol. Cell. 1:1998;595-601.
    • (1998) Mol. Cell , vol.1 , pp. 595-601
    • Kahlem, P.1    Green, H.2    Djian, P.3
  • 31
    • 0033594894 scopus 로고    scopus 로고
    • Transglutaminase aggregates huntingtin into nonamyloidogenic polymers, and its enzymatic activity increases in Huntington's disease brain nuclei
    • Karpuj M.V., Garren H., Slunt H., Price D.L., Gusella J., Becher M.W., Steinman L. Transglutaminase aggregates huntingtin into nonamyloidogenic polymers, and its enzymatic activity increases in Huntington's disease brain nuclei. Proc. Natl. Acad. Sci. U. S. A. 96:1999;7388-7393.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 7388-7393
    • Karpuj, M.V.1    Garren, H.2    Slunt, H.3    Price, D.L.4    Gusella, J.5    Becher, M.W.6    Steinman, L.7
  • 32
    • 0036172346 scopus 로고    scopus 로고
    • Prolonged survival and decreased abnormal movements in transgenic model of Huntington disease, with administration of the transglutaminase inhibitor cystamine
    • Karpuj M.V., Becher M.W., Springer J.E., Chabas D., Youssef S., Pedotti R., Mitchell D., Steinman L. Prolonged survival and decreased abnormal movements in transgenic model of Huntington disease, with administration of the transglutaminase inhibitor cystamine. Nat. Med. 8:2002;143-149.
    • (2002) Nat. Med. , vol.8 , pp. 143-149
    • Karpuj, M.V.1    Becher, M.W.2    Springer, J.E.3    Chabas, D.4    Youssef, S.5    Pedotti, R.6    Mitchell, D.7    Steinman, L.8
  • 33
    • 0030059636 scopus 로고    scopus 로고
    • Hepatocyte growth factor induces transglutaminase activity that negatively regulates the growth signal in primary cultured hepatocytes
    • Katoh S., Nakagawa N., Yano Y., Satoh K., Kohno H., Ohkubo Y., Suzuki T., Kitani K. Hepatocyte growth factor induces transglutaminase activity that negatively regulates the growth signal in primary cultured hepatocytes. Exp. Cell Res. 222:1996;255-261.
    • (1996) Exp. Cell Res. , vol.222 , pp. 255-261
    • Katoh, S.1    Nakagawa, N.2    Yano, Y.3    Satoh, K.4    Kohno, H.5    Ohkubo, Y.6    Suzuki, T.7    Kitani, K.8
  • 34
    • 0032749566 scopus 로고    scopus 로고
    • Differential expression of multiple transglutaminases in human brain. Increased expression and cross-linking by transglutaminases 1 and 2 in Alzheimer's disease
    • Kim S.Y., Grant P., Lee J.H., Pant H.C., Steinert P.M. Differential expression of multiple transglutaminases in human brain. Increased expression and cross-linking by transglutaminases 1 and 2 in Alzheimer's disease. J. Biol. Chem. 274:1999;30715-30721.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30715-30721
    • Kim, S.Y.1    Grant, P.2    Lee, J.H.3    Pant, H.C.4    Steinert, P.M.5
  • 35
    • 0032742674 scopus 로고    scopus 로고
    • Tissue transglutaminase is increased in Huntington's disease brain
    • Lesort M., Chun W., Johnson G.V., Ferrante R.J. Tissue transglutaminase is increased in Huntington's disease brain. J. Neurochem. 73:1999;2018-2027.
    • (1999) J. Neurochem. , vol.73 , pp. 2018-2027
    • Lesort, M.1    Chun, W.2    Johnson, G.V.3    Ferrante, R.J.4
  • 36
    • 0037423204 scopus 로고    scopus 로고
    • Cystamine inhibits caspase activity. Implications for the treatment of polyglutamine disorders
    • Lesort M., Lee M., Tucholski J., Johnson G.V. Cystamine inhibits caspase activity. Implications for the treatment of polyglutamine disorders. J. Biol. Chem. 278:2003;3825-3830.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3825-3830
    • Lesort, M.1    Lee, M.2    Tucholski, J.3    Johnson, G.V.4
  • 38
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: Crosslinking enzymes with pleiotropic functions
    • Lorand L., Graham R.M. Transglutaminases: crosslinking enzymes with pleiotropic functions. Nat. Rev., Mol. Cell Biol. 4:2003;140-156.
    • (2003) Nat. Rev., Mol. Cell Biol. , vol.4 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 39
    • 0028907482 scopus 로고
    • Isolation and characterization of the human tissue transglutaminase gene promoter
    • Lu S., Saydak M., Gentile V., Stein J.P., Davies P.J. Isolation and characterization of the human tissue transglutaminase gene promoter. J. Biol. Chem. 270:1995;9748-9756.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9748-9756
    • Lu, S.1    Saydak, M.2    Gentile, V.3    Stein, J.P.4    Davies, P.J.5
  • 40
    • 0022575415 scopus 로고
    • Transglutaminase and neuronal differentiation
    • Maccioni R.B., Seeds N.W. Transglutaminase and neuronal differentiation. Mol. Cell. Biochem. 69:1986;161-168.
    • (1986) Mol. Cell. Biochem. , vol.69 , pp. 161-168
    • MacCioni, R.B.1    Seeds, N.W.2
  • 41
    • 0035503897 scopus 로고    scopus 로고
    • Tissue-transglutaminase in rat and human brain: Light and electron immunocytochemical analysis and in situ hybridization study
    • Maggio N., Sellitti S., Capano C.P., Papa M. Tissue-transglutaminase in rat and human brain: light and electron immunocytochemical analysis and in situ hybridization study. Brain Res. Bull. 56:2001;173-182.
    • (2001) Brain Res. Bull. , vol.56 , pp. 173-182
    • Maggio, N.1    Sellitti, S.2    Capano, C.P.3    Papa, M.4
  • 44
    • 0038478782 scopus 로고    scopus 로고
    • Huntington's disease: New hope for therapeutics
    • McMurray C.T. Huntington's disease: new hope for therapeutics. Trends Neurosci. 24:2001;S32-S38.
    • (2001) Trends Neurosci. , vol.24 , pp. 32-S38
    • McMurray, C.T.1
  • 46
    • 0037107191 scopus 로고    scopus 로고
    • Early motor dysfunction and striosomal distribution of huntingtin microaggregates in Huntington's disease knock-in mice
    • Menalled L.B., Sison J.D., Wu Y., Olivieri M., Li X.J., Li H., Zeitlin S., Chesselet M.F. Early motor dysfunction and striosomal distribution of huntingtin microaggregates in Huntington's disease knock-in mice. J. Neurosci. 22:2002;8266-8276.
    • (2002) J. Neurosci. , vol.22 , pp. 8266-8276
    • Menalled, L.B.1    Sison, J.D.2    Wu, Y.3    Olivieri, M.4    Li, X.J.5    Li, H.6    Zeitlin, S.7    Chesselet, M.F.8
  • 47
    • 0029096258 scopus 로고
    • Transglutaminase cross-linking of the tau protein
    • Miller M.L., Johnson G.V. Transglutaminase cross-linking of the tau protein. J. Neurochem. 65:1995;1760-1770.
    • (1995) J. Neurochem. , vol.65 , pp. 1760-1770
    • Miller, M.L.1    Johnson, G.V.2
  • 48
    • 0040041521 scopus 로고    scopus 로고
    • Cross-linking sites of the human tau protein, probed by reactions with human transglutaminase
    • Murthy S.N., Wilson J.H., Lukas T.J., Kuret J., Lorand L. Cross-linking sites of the human tau protein, probed by reactions with human transglutaminase. J. Neurochem. 71:1998;2607-2614.
    • (1998) J. Neurochem. , vol.71 , pp. 2607-2614
    • Murthy, S.N.1    Wilson, J.H.2    Lukas, T.J.3    Kuret, J.4    Lorand, L.5
  • 49
    • 0030051022 scopus 로고    scopus 로고
    • Identification and characterization of a versatile retinoid response element (retinoic acid receptor response element-retinoid X receptor response element) in the mouse tissue transglutaminase gene promoter
    • Nagy L., Saydak M., Shipley N., Lu S., Basilion J.P., Yan Z.H., Syka P., Chandraratna R.A., Stein J.P., Heyman R.A., Davies P.J. Identification and characterization of a versatile retinoid response element (retinoic acid receptor response element-retinoid X receptor response element) in the mouse tissue transglutaminase gene promoter. J. Biol. Chem. 271:1996;4355-4365.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4355-4365
    • Nagy, L.1    Saydak, M.2    Shipley, N.3    Lu, S.4    Basilion, J.P.5    Yan, Z.H.6    Syka, P.7    Chandraratna, R.A.8    Stein, J.P.9    Heyman, R.A.10    Davies, P.J.11
  • 50
    • 0001298461 scopus 로고    scopus 로고
    • The promoter of the mouse tissue transglutaminase gene directs tissue-specific, retinoid-regulated and apoptosis-linked expression
    • Nagy L., Thomazy V.A., Saydak M.M., Stein J.P., Davies P.J. The promoter of the mouse tissue transglutaminase gene directs tissue-specific, retinoid-regulated and apoptosis-linked expression. Cell Death Differ. 4:1997;534-547.
    • (1997) Cell Death Differ. , vol.4 , pp. 534-547
    • Nagy, L.1    Thomazy, V.A.2    Saydak, M.M.3    Stein, J.P.4    Davies, P.J.5
  • 51
    • 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., Graham R.M. Gh: a GTP-binding protein with transglutaminase activity and receptor signaling function. Science. 264:1994;1593-1596.
    • (1994) Science , vol.264 , pp. 1593-1596
    • Nakaoka, H.1    Perez, D.M.2    Baek, K.J.3    Das, T.4    Husain, A.5    Misono, K.6    Im, M.J.7    Graham, R.M.8
  • 53
  • 54
    • 0033607671 scopus 로고    scopus 로고
    • Inhibition of "tissue" transglutaminase increases cell survival by preventing apoptosis
    • Oliverio S., Amendola A., Rodolfo C., Spinedi A., Piacentini M. Inhibition of "tissue" transglutaminase increases cell survival by preventing apoptosis. J. Biol. Chem. 274:1999;34123-34128.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34123-34128
    • Oliverio, S.1    Amendola, A.2    Rodolfo, C.3    Spinedi, A.4    Piacentini, M.5
  • 55
    • 0022586820 scopus 로고
    • A role for transglutaminase in neurotransmitter release by rat brain synaptosomes
    • Pastuszko A., Wilson D.F., Erecinska M. A role for transglutaminase in neurotransmitter release by rat brain synaptosomes. J. Neurochem. 46:1986;499-508.
    • (1986) J. Neurochem. , vol.46 , pp. 499-508
    • Pastuszko, A.1    Wilson, D.F.2    Erecinska, M.3
  • 56
    • 0027243955 scopus 로고
    • Localization and activity of transglutaminase, a retinoid-inducible protein, in developing rat spinal cord
    • Perry M.J., Haynes L.W. Localization and activity of transglutaminase, a retinoid-inducible protein, in developing rat spinal cord. Int. J. Dev. Neurosci. 11:1993;325-337.
    • (1993) Int. J. Dev. Neurosci. , vol.11 , pp. 325-337
    • Perry, M.J.1    Haynes, L.W.2
  • 57
    • 0028927182 scopus 로고
    • Transglutaminase C in cerebellar granule neurons: Regulation and localization of substrate cross-linking
    • Perry M.J., Mahoney S.A., Haynes L.W. Transglutaminase C in cerebellar granule neurons: regulation and localization of substrate cross-linking. Neuroscience. 65:1995;1063-1076.
    • (1995) Neuroscience , vol.65 , pp. 1063-1076
    • Perry, M.J.1    Mahoney, S.A.2    Haynes, L.W.3
  • 58
    • 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., Melino G. The expression of "tissue" transglutaminase in two human cancer cell lines is related with the programmed cell death (apoptosis). Eur. J. Cell Biol. 54:1991;246-254.
    • (1991) Eur. J. Cell Biol. , vol.54 , pp. 246-254
    • Piacentini, M.1    Fesus, L.2    Farrace, M.G.3    Ghibelli, L.4    Piredda, L.5    Melino, G.6
  • 59
    • 0026786093 scopus 로고
    • Phenotype-specific "tissue" transglutaminase regulation in human neuroblastoma cells in response to retinoic acid: Correlation with cell death by apoptosis
    • Piacentini M., Annicchiarico-Petruzzelli M., Oliverio S., Piredda L., Biedler J.L., Melino E. Phenotype-specific "tissue" transglutaminase regulation in human neuroblastoma cells in response to retinoic acid: correlation with cell death by apoptosis. Int. J. Cancer. 52:1992;271-278.
    • (1992) Int. J. Cancer , vol.52 , pp. 271-278
    • Piacentini, M.1    Annicchiarico-Petruzzelli, M.2    Oliverio, S.3    Piredda, L.4    Biedler, J.L.5    Melino, E.6
  • 61
    • 0037128650 scopus 로고    scopus 로고
    • Epidermal transglutaminase (TGase 3) is the autoantigen of dermatitis herpetiformis
    • Sardy M., Karpati S., Merkl B., Paulsson M., Smyth N. Epidermal transglutaminase (TGase 3) is the autoantigen of dermatitis herpetiformis. J. Exp. Med. 195:2002;747-757.
    • (2002) J. Exp. Med. , vol.195 , pp. 747-757
    • Sardy, M.1    Karpati, S.2    Merkl, B.3    Paulsson, M.4    Smyth, N.5
  • 64
    • 0026754093 scopus 로고
    • Putative nucleotide binding sites of guinea pig liver transglutaminase
    • Takeuchi Y., Birckbichler P.J., Patterson M.K. Jr., Lee K.N. Putative nucleotide binding sites of guinea pig liver transglutaminase. FEBS Lett. 307:1992;177-180.
    • (1992) FEBS Lett. , vol.307 , pp. 177-180
    • Takeuchi, Y.1    Birckbichler, P.J.2    Patterson, M.K.Jr.3    Lee, K.N.4
  • 65
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • The Huntington's Disease Collaborative Research Group A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell. 72:1993;971-983.
    • (1993) Cell , vol.72 , pp. 971-983
  • 67
    • 0036319364 scopus 로고    scopus 로고
    • Tissue transglutaminase differentially modulates apoptosis in a stimuli-dependent manner
    • Tucholski J., Johnson G.V. Tissue transglutaminase differentially modulates apoptosis in a stimuli-dependent manner. J. Neurochem. 81:2002;780-791.
    • (2002) J. Neurochem. , vol.81 , pp. 780-791
    • Tucholski, J.1    Johnson, G.V.2
  • 68
    • 0035863525 scopus 로고    scopus 로고
    • Tissue transglutaminase is essential for neurite outgrowth in human neuroblastoma SH-SY5Y cells
    • Tucholski J., Lesort M., Johnson G.V. Tissue transglutaminase is essential for neurite outgrowth in human neuroblastoma SH-SY5Y cells. Neuroscience. 102:2001;481-491.
    • (2001) Neuroscience , vol.102 , pp. 481-491
    • Tucholski, J.1    Lesort, M.2    Johnson, G.V.3
  • 69
    • 0032972409 scopus 로고    scopus 로고
    • Distribution and activity of transglutaminase in rat brain carcinogenesis and in gliomas
    • Tunici P., Sessa A., Rabellotti E., Calloni A., Perin A. Distribution and activity of transglutaminase in rat brain carcinogenesis and in gliomas. Cancer Lett. 140:1999;47-51.
    • (1999) Cancer Lett. , vol.140 , pp. 47-51
    • Tunici, P.1    Sessa, A.2    Rabellotti, E.3    Calloni, A.4    Perin, A.5


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