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Volumn 389, Issue 2, 2009, Pages 150-156

Development of an isoenzyme-specific colorimetric assay for tissue transglutaminase 2 cross-linking activity

Author keywords

Colorimetric assay; Solid phase assay; Spermine; TG2; TG2 specific assay; Tissue transglutaminase

Indexed keywords

AMINO ACIDS; COLOR; MAMMALS; PROTEINS; TISSUE;

EID: 67349084359     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2009.03.029     Document Type: Article
Times cited : (27)

References (40)
  • 1
    • 0036901574 scopus 로고    scopus 로고
    • Transglutaminases: nature's biological glues
    • Griffin M., Casadio R., and Bergamini C.M. Transglutaminases: nature's biological glues. Biochem. J. 368 (2002) 377-396
    • (2002) Biochem. J. , vol.368 , pp. 377-396
    • Griffin, M.1    Casadio, R.2    Bergamini, C.M.3
  • 2
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: crosslinking enzymes with pleiotropic functions
    • Lorand L., and 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
  • 3
    • 0036804796 scopus 로고    scopus 로고
    • Transglutaminase 2: an enigmatic enzyme with diverse functions
    • Fesus L., and Piacentini M. Transglutaminase 2: an enigmatic enzyme with diverse functions. Trends Biochem. Sci. 27 (2002) 534-539
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 534-539
    • Fesus, L.1    Piacentini, M.2
  • 4
    • 18944366339 scopus 로고    scopus 로고
    • Transglutaminase type II is a key element in the regulation of the anti-inflammatory response elicited by apoptotic cell engulfment
    • Falasca L., Iadevaia V., Ciccosanti F., Melino G., Serafino A., and Piacentini M. Transglutaminase type II is a key element in the regulation of the anti-inflammatory response elicited by apoptotic cell engulfment. J. Immunol. 174 (2005) 7330-7340
    • (2005) J. Immunol. , vol.174 , pp. 7330-7340
    • Falasca, L.1    Iadevaia, V.2    Ciccosanti, F.3    Melino, G.4    Serafino, A.5    Piacentini, M.6
  • 5
    • 33749635159 scopus 로고    scopus 로고
    • ATP-binding cassette transporter 1 and transglutaminase 2 act on the same genetic pathway in the apoptotic cell clearance
    • Iadevaia V., Rinaldi A., Falasca L., Pucillo L.P., Alonzi T., Chimini G., and Piacentini M. ATP-binding cassette transporter 1 and transglutaminase 2 act on the same genetic pathway in the apoptotic cell clearance. Cell Death Differ. 13 (2006) 1998-2001
    • (2006) Cell Death Differ. , vol.13 , pp. 1998-2001
    • Iadevaia, V.1    Rinaldi, A.2    Falasca, L.3    Pucillo, L.P.4    Alonzi, T.5    Chimini, G.6    Piacentini, M.7
  • 7
    • 51349086373 scopus 로고    scopus 로고
    • Tissue transglutaminase contributes to interstitial renal fibrosis by favoring accumulation of fibrillar collagen through TGF-beta activation and cell infiltration
    • Shweke N., Boulos N., Jouanneau C., Vandermeersch S., Melino G., Dussaule J.C., Chatziantoniou C., Ronco P., and Boffa J.J. Tissue transglutaminase contributes to interstitial renal fibrosis by favoring accumulation of fibrillar collagen through TGF-beta activation and cell infiltration. Am. J. Pathol. 173 (2008) 631-642
    • (2008) Am. J. Pathol. , vol.173 , pp. 631-642
    • Shweke, N.1    Boulos, N.2    Jouanneau, C.3    Vandermeersch, S.4    Melino, G.5    Dussaule, J.C.6    Chatziantoniou, C.7    Ronco, P.8    Boffa, J.J.9
  • 8
    • 38749143294 scopus 로고    scopus 로고
    • Transglutaminase and the pathogenesis of coeliac disease
    • Stenberg P., Roth E.B., and Sjoberg K. Transglutaminase and the pathogenesis of coeliac disease. Eur. J. Intern. Med. 19 (2008) 83-91
    • (2008) Eur. J. Intern. Med. , vol.19 , pp. 83-91
    • Stenberg, P.1    Roth, E.B.2    Sjoberg, K.3
  • 9
    • 39749124295 scopus 로고    scopus 로고
    • Type 2 transglutaminase in neurodegenerative diseases: the mitochondrial connection
    • Malorni W., Farrace M.G., Rodolfo C., and Piacentini M. Type 2 transglutaminase in neurodegenerative diseases: the mitochondrial connection. Curr. Pharm. Des. 14 (2008) 278-288
    • (2008) Curr. Pharm. Des. , vol.14 , pp. 278-288
    • Malorni, W.1    Farrace, M.G.2    Rodolfo, C.3    Piacentini, M.4
  • 11
    • 55249094350 scopus 로고    scopus 로고
    • Quantitative proteomic signature of liver cancer cells: tissue transglutaminase 2 could be a novel protein candidate of human hepatocellular carcinoma
    • Sun Y., Mi W., Cai J., Ying W., Liu F., Lu H., Qiao Y., Jia W., Bi X., Lu N., Liu S., Qian X., and Zhao X. Quantitative proteomic signature of liver cancer cells: tissue transglutaminase 2 could be a novel protein candidate of human hepatocellular carcinoma. J. Proteome Res. 7 (2008) 3847-3859
    • (2008) J. Proteome Res. , vol.7 , pp. 3847-3859
    • Sun, Y.1    Mi, W.2    Cai, J.3    Ying, W.4    Liu, F.5    Lu, H.6    Qiao, Y.7    Jia, W.8    Bi, X.9    Lu, N.10    Liu, S.11    Qian, X.12    Zhao, X.13
  • 13
    • 0026660488 scopus 로고
    • A microtiter plate transglutaminase assay utilizing 5-(biotinamido)pentylamine as substrate
    • Slaughter T.F., Achyuthan K.E., Lai T.S., and Greenberg C.S. A microtiter plate transglutaminase assay utilizing 5-(biotinamido)pentylamine as substrate. Anal. Biochem. 205 (1992) 166-171
    • (1992) Anal. Biochem. , vol.205 , pp. 166-171
    • Slaughter, T.F.1    Achyuthan, K.E.2    Lai, T.S.3    Greenberg, C.S.4
  • 14
    • 0034307358 scopus 로고    scopus 로고
    • A direct continuous spectrophotometric assay for transglutaminase activity
    • de Macedo P., Marrano C., and Keillor J.W. A direct continuous spectrophotometric assay for transglutaminase activity. Anal. Biochem. 285 (2000) 16-20
    • (2000) Anal. Biochem. , vol.285 , pp. 16-20
    • de Macedo, P.1    Marrano, C.2    Keillor, J.W.3
  • 15
    • 2942547867 scopus 로고    scopus 로고
    • An improved colorimetric assay for the measurement of transglutaminase (type II)-(gamma-glutamyl) lysine cross-linking activity
    • Trigwell S.M., Lynch P.T., Griffin M., Hargreaves A.J., and Bonner P.L. An improved colorimetric assay for the measurement of transglutaminase (type II)-(gamma-glutamyl) lysine cross-linking activity. Anal. Biochem. 330 (2004) 164-166
    • (2004) Anal. Biochem. , vol.330 , pp. 164-166
    • Trigwell, S.M.1    Lynch, P.T.2    Griffin, M.3    Hargreaves, A.J.4    Bonner, P.L.5
  • 16
    • 34347212436 scopus 로고    scopus 로고
    • A highly sensitive fluorometric assay for determination of human coagulation factor XIII in plasma
    • Oertel K., Hunfeld A., Specker E., Reiff C., Seitz R., Pasternack R., and Dodt J. A highly sensitive fluorometric assay for determination of human coagulation factor XIII in plasma. Anal. Biochem. 367 (2007) 152-158
    • (2007) Anal. Biochem. , vol.367 , pp. 152-158
    • Oertel, K.1    Hunfeld, A.2    Specker, E.3    Reiff, C.4    Seitz, R.5    Pasternack, R.6    Dodt, J.7
  • 17
    • 23044488791 scopus 로고    scopus 로고
    • High-throughput scintillation proximity assay for transglutaminase activity measurement
    • Madi A., Karpati L., Kovacs A., Muszbek L., and Fesus L. High-throughput scintillation proximity assay for transglutaminase activity measurement. Anal. Biochem. 343 (2005) 256-262
    • (2005) Anal. Biochem. , vol.343 , pp. 256-262
    • Madi, A.1    Karpati, L.2    Kovacs, A.3    Muszbek, L.4    Fesus, L.5
  • 18
    • 33749856395 scopus 로고    scopus 로고
    • A rapid transglutaminase assay for high-throughput screening applications
    • Wu Y.W., and Tsai Y.H. A rapid transglutaminase assay for high-throughput screening applications. J. Biomol. Screen. 11 (2006) 836-843
    • (2006) J. Biomol. Screen. , vol.11 , pp. 836-843
    • Wu, Y.W.1    Tsai, Y.H.2
  • 20
    • 0033636292 scopus 로고    scopus 로고
    • A modified optimized kinetic photometric assay for the determination of blood coagulation factor XIII activity in plasma
    • Karpati L., Penke B., Katona E., Balogh I., Vamosi G., and Muszbek L. A modified optimized kinetic photometric assay for the determination of blood coagulation factor XIII activity in plasma. Clin. Chem. 46 (2000) 1946-1955
    • (2000) Clin. Chem. , vol.46 , pp. 1946-1955
    • Karpati, L.1    Penke, B.2    Katona, E.3    Balogh, I.4    Vamosi, G.5    Muszbek, L.6
  • 21
    • 33644747243 scopus 로고    scopus 로고
    • Development and evaluation of a modified colorimetric solid-phase microassay for measuring the activity of cellular and plasma (Factor XIII) transglutaminases
    • Thomas V., El Alaoui S., Massignon D., Clement S., Simonet F., and Quash G. Development and evaluation of a modified colorimetric solid-phase microassay for measuring the activity of cellular and plasma (Factor XIII) transglutaminases. Biotechnol. Appl. Biochem. 43 (2006) 171-179
    • (2006) Biotechnol. Appl. Biochem. , vol.43 , pp. 171-179
    • Thomas, V.1    El Alaoui, S.2    Massignon, D.3    Clement, S.4    Simonet, F.5    Quash, G.6
  • 22
    • 33745846379 scopus 로고    scopus 로고
    • Screening for the preferred substrate sequence of transglutaminase using a phage-displayed peptide library: identification of peptide substrates for TGASE 2 and Factor XIIIA
    • Sugimura Y., Hosono M., Wada F., Yoshimura T., Maki M., and Hitomi K. Screening for the preferred substrate sequence of transglutaminase using a phage-displayed peptide library: identification of peptide substrates for TGASE 2 and Factor XIIIA. J. Biol. Chem. 281 (2006) 17699-17706
    • (2006) J. Biol. Chem. , vol.281 , pp. 17699-17706
    • Sugimura, Y.1    Hosono, M.2    Wada, F.3    Yoshimura, T.4    Maki, M.5    Hitomi, K.6
  • 24
    • 76549212824 scopus 로고
    • The enzymatic formation of hydroxamic acids from glutamine and asparagine
    • Grossowicz N., Wainfan E., Borek E., and Waelsch H. The enzymatic formation of hydroxamic acids from glutamine and asparagine. J. Biol. Chem. 187 (1950) 111-125
    • (1950) J. Biol. Chem. , vol.187 , pp. 111-125
    • Grossowicz, N.1    Wainfan, E.2    Borek, E.3    Waelsch, H.4
  • 25
    • 0034297268 scopus 로고    scopus 로고
    • Characterization of human recombinant transglutaminase 1 purified from baculovirus-infected insect cells
    • Hitomi K., Yamagiwa Y., Ikura K., Yamanishi K., and Maki M. Characterization of human recombinant transglutaminase 1 purified from baculovirus-infected insect cells. Biosci. Biotechnol. Biochem. 64 (2000) 2128-2137
    • (2000) Biosci. Biotechnol. Biochem. , vol.64 , pp. 2128-2137
    • Hitomi, K.1    Yamagiwa, Y.2    Ikura, K.3    Yamanishi, K.4    Maki, M.5
  • 26
    • 0032801976 scopus 로고    scopus 로고
    • Characterization of recombinant mouse epidermal-type transglutaminase (TGase 3): regulation of its activity by proteolysis and guanine nucleotides
    • Hitomi K., Kanehiro S., Ikura K., and Maki M. Characterization of recombinant mouse epidermal-type transglutaminase (TGase 3): regulation of its activity by proteolysis and guanine nucleotides. J. Biochem. 125 (1999) 1048-1054
    • (1999) J. Biochem. , vol.125 , pp. 1048-1054
    • Hitomi, K.1    Kanehiro, S.2    Ikura, K.3    Maki, M.4
  • 27
    • 33750893192 scopus 로고    scopus 로고
    • A role for tissue transglutaminase in alpha-gliadin peptide cytotoxicity
    • Sakly W., Thomas V., Quash G., and El Alaoui S. A role for tissue transglutaminase in alpha-gliadin peptide cytotoxicity. Clin. Exp. Immunol. 146 (2006) 550-558
    • (2006) Clin. Exp. Immunol. , vol.146 , pp. 550-558
    • Sakly, W.1    Thomas, V.2    Quash, G.3    El Alaoui, S.4
  • 28
    • 0022552371 scopus 로고
    • Transglutaminase activity and putrescine-binding capacity in cloned cell lines with different metastatic potential
    • Delcros J.G., Bard S., Roch A.M., Quash G., Poupon M.F., and Korach S. Transglutaminase activity and putrescine-binding capacity in cloned cell lines with different metastatic potential. FEBS Lett. 196 (1986) 325-330
    • (1986) FEBS Lett. , vol.196 , pp. 325-330
    • Delcros, J.G.1    Bard, S.2    Roch, A.M.3    Quash, G.4    Poupon, M.F.5    Korach, S.6
  • 29
    • 0017243178 scopus 로고
    • Fibrin-stabilizing factor (factor XIII)
    • Curtis C.G., and Lorand L. Fibrin-stabilizing factor (factor XIII). Methods Enzymol. 45 (1976) 177-191
    • (1976) Methods Enzymol. , vol.45 , pp. 177-191
    • Curtis, C.G.1    Lorand, L.2
  • 33
    • 0033003760 scopus 로고    scopus 로고
    • A simple statistical parameter for use in evaluation and validation of high throughput screening assays
    • Zhang J.H., Chung T.D., and Oldenburg K.R. A simple statistical parameter for use in evaluation and validation of high throughput screening assays. J. Biomol. Screen. 4 (1999) 67-73
    • (1999) J. Biomol. Screen. , vol.4 , pp. 67-73
    • Zhang, J.H.1    Chung, T.D.2    Oldenburg, K.R.3
  • 34
    • 0031055110 scopus 로고    scopus 로고
    • Assays for the measurement of tissue transglutaminase (type II) mediated protein crosslinking via epsilon-(gamma-glutamyl) lysine and N′,N′-bis (gamma-glutamyl) polyamine linkages using biotin labelled casein
    • Lilley G.R., Griffin M., and Bonner P.L. Assays for the measurement of tissue transglutaminase (type II) mediated protein crosslinking via epsilon-(gamma-glutamyl) lysine and N′,N′-bis (gamma-glutamyl) polyamine linkages using biotin labelled casein. J. Biochem. Biophys. Methods 34 (1997) 31-43
    • (1997) J. Biochem. Biophys. Methods , vol.34 , pp. 31-43
    • Lilley, G.R.1    Griffin, M.2    Bonner, P.L.3
  • 35
    • 38549156658 scopus 로고    scopus 로고
    • Transglutaminase 2 undergoes a large conformational change upon activation
    • Pinkas D.M., Strop P., Brunger A.T., and Khosla C. Transglutaminase 2 undergoes a large conformational change upon activation. PLoS Biol. 5 (2007) e327
    • (2007) PLoS Biol. , vol.5
    • Pinkas, D.M.1    Strop, P.2    Brunger, A.T.3    Khosla, C.4
  • 36
    • 0028319789 scopus 로고
    • Diamine oxidase: an overview of historical, biochemical and functional aspects
    • Wolvekamp M.C., and de Bruin R.W. Diamine oxidase: an overview of historical, biochemical and functional aspects. Dig. Dis. 12 (1994) 2-14
    • (1994) Dig. Dis. , vol.12 , pp. 2-14
    • Wolvekamp, M.C.1    de Bruin, R.W.2
  • 37
    • 0010612589 scopus 로고
    • Diamine oxidase and transglutaminase activities in white lupine seedlings with respect to crosslinking of proteins
    • Muriel J.-C.F.M., and Siepaio P. Diamine oxidase and transglutaminase activities in white lupine seedlings with respect to crosslinking of proteins. J. Agric. Food Chem. 43 (1995) 1151-1156
    • (1995) J. Agric. Food Chem. , vol.43 , pp. 1151-1156
    • Muriel, J.-C.F.M.1    Siepaio, P.2
  • 38
    • 12344314006 scopus 로고    scopus 로고
    • Different inhibition characteristics of intracellular transglutaminase activity by cystamine and cysteamine
    • Jeon J.H., Lee H.J., Jang G.Y., Kim C.W., Shim D.M., Cho S.Y., Yeo E.J., Park S.C., and Kim I.G. Different inhibition characteristics of intracellular transglutaminase activity by cystamine and cysteamine. Exp. Mol. Med. 36 (2004) 576-581
    • (2004) Exp. Mol. Med. , vol.36 , pp. 576-581
    • Jeon, J.H.1    Lee, H.J.2    Jang, G.Y.3    Kim, C.W.4    Shim, D.M.5    Cho, S.Y.6    Yeo, E.J.7    Park, S.C.8    Kim, I.G.9
  • 39
    • 0034747685 scopus 로고    scopus 로고
    • Gene disruption of tissue transglutaminase
    • De Laurenzi V., and Melino G. Gene disruption of tissue transglutaminase. Mol. Cell Biol. 21 (2001) 148-155
    • (2001) Mol. Cell Biol. , vol.21 , pp. 148-155
    • De Laurenzi, V.1    Melino, G.2


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