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[1]G. E. Gibson, A. Starkov, J. P. Blass, R. R. Ratan and M. F. Beal: Cause and consequence: mitochondrial dysfunction initiates and propagates neuronal dysfunction, neuronal death and behavioral abnormalities in age-associated neurodegenerative diseases. Biochim Biophys Acta, 1802(1), 122-34 (2010)
[2]Y. T. Wu, S. B. Wu and Y. H. Wei: Metabolic reprogramming of human cells in response to oxidative stress: implications in the pathophysiology and therapy of mitochondrial diseases. Curr Pharm Des, 20(35), 5510-26 (2014)
[3]D. G. Nicholls: Mitochondria and calcium signaling. Cell Calcium, 38(3-4), 311-7 (2005)
[4]A. I. Tarasov, E. J. Griffiths and G. A. Rutter: Regulation of ATP production by mitochondrial Ca(2+). Cell Calcium, 52(1), 28-35 (2012)
[5]M. R. Duchen, A. Verkhratsky and S. Muallem: Mitochondria and calcium in health and disease. Cell Calcium, 44(1), 1-5 (2008) 1
[6]C. Giorgi, F. Baldassari, A. Bononi, M. Bonora, E. De Marchi, S. Marchi, S. Missiroli, S. Patergnani, A. Rimessi, J. M. Suski, M. R. Wieckowski and P. Pinton: Mitochondrial Ca(2+) and apoptosis. Cell Calcium, 52(1), 36-43 (2012)
[7]A. F. Schinder, E. C. Olson, N. C. Spitzer and M. Montal: Mitochondrial dysfunction is a primary event in glutamate neurotoxicity. J Neurosci, 16(19), 6125-33 (1996)
[8]N. B. Pivovarova and S. B. Andrews: Calcium-dependent mitochondrial function and dysfunction in neurons. FEBS J, 277(18), 3622-36 (2010)
[9]M. Kubota, T. Kasahara, T. Nakamura, M. Ishiwata, T. Miyauchi and T. Kato: Abnormal Ca2+ dynamics in transgenic mice with neuron-specific mitochondrial DNA defects. J Neurosci, 26(47), 12314-24 (2006)
[10]M. McKenzie and M. R. Duchen: Impaired Cellular Bioenergetics Causes Mitochondrial Calcium Handling Defects in MT-ND5 Mutant Cybrids. PLoS One, 11(4), e0154371 (2016)
[11]M. Brini, P. Pinton, M. P. King, M. Davidson, E. A. Schon and R. Rizzuto: A calcium signaling defect in the pathogenesis of a mitochondrial DNA inherited oxidative phosphorylation deficiency. Nat Med, 5(8), 951-4 (1999)
[12]E. Mbaya, B. Oules, C. Caspersen, R. Tacine, H. Massinet, M. Pennuto, D. Chretien, A. Munnich, A. Rotig, R. Rizzuto, G. A. Rutter, P. Paterlini-Brechot and M. Chami: Calcium signalling-dependent mitochondrial dysfunction and bioenergetics regulation in respiratory chain Complex II deficiency. Cell Death Differ, 17(12), 1855-66 (2010)
[13]A. M. Moudy, S. D. Handran, M. P. Goldberg, N. Ruffin, I. Karl, P. Kranz-Eble, D. C. DeVivo and S. M. Rothman: Abnormal calcium homeostasis and mitochondrial polarization in a human encephalomyopathy. Proc Natl Acad Sci U S A, 92(3), 729-33 (1995)
[14]A. Federico, E. Cardaioli, P. Da Pozzo, P. Formichi, G. N. Gallus and E. Radi: Mitochondria, oxidative stress and neurodegeneration. J Neurol Sci, 322(1-2), 254-62 (2012)
[15]M. Moran, D. Moreno-Lastres, L. Marin-Buera, J. Arenas, M. A. Martin and C. Ugalde: Mitochondrial respiratory chain dysfunction: implications in neurodegeneration. Free Radic Biol Med, 53(3), 595-609 (2012)
[16]T. W. Lai, S. Zhang and Y. T. Wang: Excitotoxicity and stroke: identifying novel targets for neuroprotection. Prog Neurobiol, 115, 157-88 (2014)
[17]L. Lorand and R. M. Graham: Transglutaminases: crosslinking enzymes with pleiotropic functions. Nat Rev Mol Cell Biol, 4(2), 140-56 (2003)
[18]T. S. Lai, C. J. Lin and C. S. Greenberg: Role of tissue transglutaminase-2 (TG2)-mediated aminylation in biological processes. Amino Acids (2016)
[19]C. S. Greenberg, P. J. Birckbichler and R. H. Rice: Transglutaminases: multifunctional cross-linking enzymes that stabilize tissues. Faseb J, 5(15), 3071-7. (1991)
[20]D. Aeschlimann and V. Thomazy: Protein crosslinking in assembly and remodelling of extracellular matrices: the role of transglutaminases. Connect Tissue Res, 41(1), 1-27 (2000)
[21]R. L. Eckert, M. T. Kaartinen, M. Nurminskaya, A. M. Belkin, G. Colak, G. V. Johnson and K. Mehta: Transglutaminase regulation of cell function. Physiol Rev, 94(2), 383-417 (2014)
[22]T. S. Lai, and C. S. Greenberg: TGM2 and implications for human disease: role of alternative splicing Frontiers in Bioscience-Landmark,, 18, 504-519 (2013)
[23]G. Hasegawa, M. Suwa, Y. Ichikawa, T. Ohtsuka, S. Kumagai, M. Kikuchi, Y. Sato and Y. Saito: A novel function of tissue-type transglutaminase: protein disulphide isomerase. Biochem J, 373(Pt 3), 793-803 (2003)
[24]T. S. Lai, T. F. Slaughter, C. M. Koropchak, Z. A. Haroon and C. S. Greenberg: C-terminal deletion of human tissue transglutaminase enhances magnesium-dependent GTP/ATPase activity. J Biol Chem, 271(49), 31191-5 (1996)
[25]T. S. Lai, A. Hausladen, T. F. Slaughter, J. P. Eu, J. S. Stamler and C. S. Greenberg: Calcium regulates S-nitrosylation, denitrosylation, and activity of tissue transglutaminase. Biochemistry, 40(16), 4904-10 (2001)
[26]L. Xu, S. Begum, J. D. Hearn and R. O. Hynes: GPR56, an atypical G protein-coupled receptor, binds tissue transglutaminase, TG2, and inhibits melanoma tumor growth and metastasis. Proc Natl Acad Sci U S A, 103(24), 9023-8 (2006)
[27]H. Nakaoka, D. M. Perez, K. J. Baek, T. Das, A. Husain, K. Misono, M. J. Im and R. M. Graham: Gh: a GTP-binding protein with transglutaminase activity and receptor signaling function. Science, 264(5165), 1593-6 (1994)
[28]S. S. Akimov, D. Krylov, L. F. Fleischman and A. M. Belkin: Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin. J Cell Biol, 148(4), 825-38. (2000)
[29]T. Konno, T. Morii, A. Hirata, S. Sato, S. Oiki and K. Ikura: Covalent blocking of fibril formation and aggregation of intracellular amyloidgenic proteins by transglutaminase-catalyzed intramolecular cross-linking. Biochemistry, 44(6), 2072-9 (2005)
[30]A. J. Cooper, K. R. Sheu, J. R. Burke, O. Onodera, W. J. Strittmatter, A. D. Roses and J. P. Blass: Transglutaminase-catalyzed inactivation of glyceraldehyde 3-phosphate dehydrogenase and alpha-ketoglutarate dehydrogenase complex by polyglutamine domains of pathological length. Proc Natl Acad Sci U S A, 94(23), 12604-9 (1997)
[31]A. J. Cooper, J. Wang, R. Pasternack, H. L. Fuchsbauer, R. K. Sheu and J. P. Blass: Lysine-rich histone (H1) is a lysyl substrate of tissue transglutaminase: possible involvement of transglutaminase in the formation of nuclear aggregates in (CAG)(n)/Q(n) expansion diseases. Dev Neurosci, 22(5-6), 404-17 (2000)
[32]S. Gundemir, G. Colak, J. Tucholski and G. V. Johnson: Transglutaminase 2: a molecular Swiss army knife. Biochim Biophys Acta, 1823(2), 406-19 (2012)
[33]E. Ballestar, C. Abad and L. Franco: Core histones are glutaminyl substrates for tissue transglutaminase. J Biol Chem, 271(31), 18817-24 (1996)
[34]J. Lee, Y. S. Kim, D. H. Choi, M. S. Bang, T. R. Han, T. H. Joh and S. Y. Kim: Transglutaminase 2 induces nuclear factor-kappaB activation via a novel pathway in BV-2 microglia. J Biol Chem, 279(51), 53725-35 (2004)
[35]N. J. Robinson, P. N. Baker, C. J. Jones and J. D. Aplin: A role for tissue transglutaminase in stabilization of membrane-cytoskeletal particles shed from the human placenta. Biol Reprod, 77(4), 648-57 (2007)
[36]A. J. Cooper, T. M. Jeitner, V. Gentile and J. P. Blass: Cross linking of polyglutamine domains catalyzed by tissue transglutaminase is greatly favored with pathological-length repeats: does transglutaminase activity play a role in (CAG)(n)/Q(n)-expansion diseases? Neurochem Int, 40(1), 53-67. (2002)
[37]A. M. Belkin: Extracellular TG2: emerging functions and regulation. FEBS J, 278(24), 4704-16 (2011)
[38]D. J. Walther, J. U. Peter, S. Winter, M. Holtje, N. Paulmann, M. Grohmann, J. Vowinckel, V. Alamo-Bethencourt, C. S. Wilhelm, G. Ahnert-Hilger and M. Bader: Serotonylation of small GTPases is a signal transduction pathway that triggers platelet alpha-granule release. Cell, 115(7), 851-62 (2003)
[39]N. A. Muma and Z. Mi: Serotonylation and Transamidation of Other Monoamines. ACS Chem Neurosci, 6(7), 961-9 (2015)
[40]T. S. Lai and C. S. Greenberg: Histaminylation of fibrinogen by tissue transglutaminase-2 (TGM-2): potential role in modulating inflammation. Amino Acids, 45(4), 857-64 (2013)
[41]J. Vowinckel, S. Stahlberg, N. Paulmann, K. Bluemlein, M. Grohmann, M. Ralser and D. J. Walther: Histaminylation of glutamine residues is a novel posttranslational modification implicated in G-protein signaling. FEBS Lett, 586(21), 3819-24 (2012)
[42]D. J. Walther, S. Stahlberg and J. Vowinckel: Novel roles for biogenic monoamines: from monoamines in transglutaminase-mediated post-translational protein modification to monoaminylation deregulation diseases. FEBS J, 278(24), 4740-55 (2011)
[43]R. Szasz and G. L. Dale: Thrombospondin and fibrinogen bind serotonin-derivatized proteins on COAT-platelets. Blood, 100(8), 2827-31 (2002)
[44]G. L. Dale, P. Friese, P. Batar, S. F. Hamilton, G. L. Reed, K. W. Jackson, K. J. Clemetson and L. Alberio: Stimulated platelets use serotonin to enhance their retention of procoagulant proteins on the cell surface. Nature, 415(6868), 175-9 (2002)
[45]C. I. Prodan, P. M. Joseph, A. S. Vincent and G. L. Dale: Coated-platelet levels are influenced by smoking, aspirin, and selective serotonin reuptake inhibitors. J Thromb Haemost, 5(10), 2149-51 (2007)
[46]J. E. Folk: Mechanism and basis for specificity of transglutaminase-catalyzed epsilon-(gamma-glutamyl) lysine bond formation. Adv Enzymol Relat Areas Mol Biol, 54, 1-56 (1983)
[47]J. E. Folk and S. I. Chung: Transglutaminases. Methods Enzymol, 113, 358-75 (1985)
[48]L. Lorand and S. M. Conrad: Transglutaminases. Mol Cell Biochem, 58(1-2), 9-35 (1984)
[49]L. Lorand, K. N. Parameswaran, P. Stenberg, Y. S. Tong, P. T. Velasco, N. A. Jonsson, L. Mikiver and P. Moses: Specificity of guinea pig liver transglutaminase for amine substrates. Biochemistry, 18(9), 1756-65 (1979)
[50]C. W. Tabor and H. Tabor: Polyamines. Annu Rev Biochem, 53, 749-90 (1984)
[51]T. S. Lai, T. Tucker, J. R. Burke, W. J. Strittmatter and C. S. Greenberg: Effect of tissue transglutaminase on the solubility of proteins containing expanded polyglutamine repeats. J Neurochem, 88(5), 1253-60 (2004)
[52]Y. Song, L. L. Kirkpatrick, A. B. Schilling, D. L. Helseth, N. Chabot, J. W. Keillor, G. V. Johnson and S. T. Brady: Transglutaminase and polyamination of tubulin: posttranslational modification for stabilizing axonal microtubules. Neuron, 78(1), 109-23 (2013) doi:10.1.016/j.neuron.2013.0.1.0.36
[53]S. W. Qiao, J. Piper, G. Haraldsen, I. Oynebraten, B. Fleckenstein, O. Molberg, C. Khosla and L. M. Sollid: Tissue transglutaminase-mediated formation and cleavage of histamine-gliadin complexes: biological effects and implications for celiac disease. J Immunol, 174(3), 1657-63 (2005)
[54]S. J. McConoughey, M. Basso, Z. V. Niatsetskaya, S. F. Sleiman, N. A. Smirnova, B. C. Langley, L. Mahishi, A. J. Cooper, M. A. Antonyak, R. A. Cerione, B. Li, A. Starkov, R. K. Chaturvedi, M. F. Beal, G. Coppola, D. H. Geschwind, H. Ryu, L. Xia, S. E. Iismaa, J. Pallos, R. Pasternack, M. Hils, J. Fan, L. A. Raymond, J. L. Marsh, L. M. Thompson and R. R. Ratan: Inhibition of transglutaminase 2 mitigates transcriptional dysregulation in models of Huntington disease. EMBO Mol Med, 2(9), 349-70 (2010)
[55]M. T. Lin and M. F. Beal: Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature, 443(7113), 787-95 (2006)
[56]T. M. Jeitner, M. B. Bogdanov, W. R. Matson, Y. Daikhin, M. Yudkoff, J. E. Folk, L. Steinman, S. E. Browne, M. F. Beal, J. P. Blass and A. J. Cooper: N(epsilon)-(gamma-L-glutamyl)-L-lysine (GGEL) is increased in cerebrospinal fluid of patients with Huntington’s disease. J Neurochem, 79(5), 1109-12. (2001)
[57]M. V. Karpuj, H. Garren, H. Slunt, D. L. Price, J. Gusella, M. W. Becher and L. Steinman: 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(13), 7388-93 (1999)
[58]T. M. Jeitner, K. Battaile and A. J. Cooper: gamma-Glutamylamines and neurodegenerative diseases. Amino Acids, 44(1), 129-42 (2013)
[59]T. M. Jeitner, W. R. Matson, J. E. Folk, J. P. Blass and A. J. Cooper: Increased levels of gamma-glutamylamines in Huntington disease CSF. J Neurochem, 106(1), 37-44 (2008)
[60]T. M. Jeitner, N. A. Muma, K. P. Battaile and A. J. Cooper: Transglutaminase activation in neurodegenerative diseases. Future Neurol, 4(4), 449-467 (2009)
[61]T. Lai, Tucker, T., Burke, JR., Strittmatter, WJ., and Greenberg, CS: Effect of Tissue Transglutaminase on the Solubility of Proteins Containing Expanded Polyglutamine Repeats. J. Neurochemistry, 88(5), 1253-1260 (2004)
[62]T. Konno, T. Morii, H. Shimizu, S. Oiki and K. Ikura: Paradoxical inhibition of protein aggregation and precipitation by transglutaminase-catalyzed intermolecular cross-linking. J Biol Chem, 280(17), 17520-5 (2005)
[63]H. T. Orr: Neurodegenerative disease: neuron protection agency. Nature, 431(7010), 747-8 (2004)
[64]M. Arrasate, S. Mitra, E. S. Schweitzer, M. R. Segal and S. Finkbeiner: Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature, 431(7010), 805-10 (2004)
[65]S. Boros, E. Ahrman, L. Wunderink, B. Kamps, W. W. de Jong, W. C. Boelens and C. S. Emanuelsson: Site-specific transamidation and deamidation of the small heat-shock protein Hsp20 by tissue transglutaminase. Proteins, 62(4), 1044-52 (2006)
[66]K. Iwai, Y. Shibukawa, N. Yamazaki and Y. Wada: Transglutaminase 2-dependent deamidation of glyceraldehyde-3-phosphate dehydrogenase promotes trophoblastic cell fusion. J Biol Chem, 289(8), 4989-99 (2014)
[67]K. N. Parameswaran, X. F. Cheng, E. C. Chen, P. T. Velasco, J. H. Wilson and L. Lorand: Hydrolysis of gamma:epsilon isopeptides by cytosolic transglutaminases and by coagulation factor XIIIa. J Biol Chem, 272(15), 10311-7 (1997)
[68]R. Kiraly, K. Thangaraju, Z. Nagy, R. Collighan, Z. Nemes, M. Griffin and L. Fesus: Isopeptidase activity of human transglutaminase 2: disconnection from transamidation and characterization by kinetic parameters. Amino Acids, 48(1), 31-40 (2016)
[69]R. Chandrashekar, N. Tsuji, T. Morales, V. Ozols and K. Mehta: An ERp60-like protein from the filarial parasite Dirofilaria immitis has both transglutaminase and protein disulfide isomerase activity. Proc Natl Acad Sci U S A, 95(2), 531-6 (1998)
[70]B. Blasko, A. Madi and L. Fesus: Thioredoxin motif of Caenorhabditis elegans PDI-3 provides Cys and His catalytic residues for transglutaminase activity. Biochem Biophys Res Commun, 303(4), 1142-7 (2003)
[71]P. G. Mastroberardino, M. G. Farrace, I. Viti, F. Pavone, G. M. Fimia, G. Melino, C. Rodolfo and M. Piacentini: “Tissue” transglutaminase contributes to the formation of disulphide bridges in proteins of mitochondrial respiratory complexes. Biochim Biophys Acta, 1757(9-10), 1357-65 (2006)
[72]W. Malorni, M. G. Farrace, P. Matarrese, A. Tinari, L. Ciarlo, P. Mousavi-Shafaei, M. D’Eletto, G. Di Giacomo, G. Melino, L. Palmieri, C. Rodolfo and M. Piacentini: The adenine nucleotide translocator 1 acts as a type 2 transglutaminase substrate: implications for mitochondrial-dependent apoptosis. Cell Death Differ, 16(11), 1480-92 (2009)
[73]T. S. Lai, T. F. Slaughter, K. A. Peoples, J. M. Hettasch and C. S. Greenberg: Regulation of human tissue transglutaminase function by magnesium- nucleotide complexes. Identification of distinct binding sites for Mg- GTP and Mg-ATP. J Biol Chem, 273(3), 1776-81. (1998)
[74]S. Liu, R. A. Cerione and J. Clardy: Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity. Proc Natl Acad Sci U S A, 99(5), 2743-7 (2002)
[75]D. M. Pinkas, P. Strop, A. T. Brunger and C. Khosla: Transglutaminase 2 undergoes a large conformational change upon activation. PLoS Biol, 5(12), e327 (2007)
[76]J. H. Jeon, C. W. Kim, D. M. Shin, K. Kim, S. Y. Cho, J. C. Kwon, K. H. Choi, H. S. Kang and I. G. Kim: Differential incorporation of biotinylated polyamines by transglutaminase 2. FEBS Lett, 534(1-3), 180-4 (2003)
[77]J. H. Jeon, G. Y. Jang, C. W. Kim, D. M. Shin, S. Y. Cho, J. C. Kwon, H. J. Lee, K. H. Choi and I. G. Kim: Cell-based assay for monitoring transglutaminase activity. Anal Biochem, 333(2), 399-401 (2004)
[78]D. M. Shin, J. H. Jeon, C. W. Kim, S. Y. Cho, J. C. Kwon, H. J. Lee, K. H. Choi, S. C. Park and I. G. Kim: Cell type-specific activation of intracellular transglutaminase 2 by oxidative stress or ultraviolet irradiation: implications of transglutaminase 2 in age-related cataractogenesis. J Biol Chem, 279(15), 15032-9 (2004)
[79]A. V. Panov, C. A. Gutekunst, B. R. Leavitt, M. R. Hayden, J. R. Burke, W. J. Strittmatter and J. T. Greenamyre: Early mitochondrial calcium defects in Huntington’s disease are a direct effect of polyglutamines. Nat Neurosci, 5(8), 731-6 (2002)
[80]J. Stamnaes, D. M. Pinkas, B. Fleckenstein, C. Khosla and L. M. Sollid: Redox regulation of transglutaminase 2 activity. J Biol Chem, 285(33), 25402-9 (2010)
[81]X. Jin, J. Stamnaes, C. Klock, T. R. DiRaimondo, L. M. Sollid and C. Khosla: Activation of extracellular transglutaminase 2 by thioredoxin. J Biol Chem, 286(43), 37866-73 (2011)
[82]B. G. Han, J. W. Cho, Y. D. Cho, K. C. Jeong, S. Y. Kim and B. I. Lee: Crystal structure of human transglutaminase 2 in complex with adenosine triphosphate. Int J Biol Macromol, 47(2), 190-5 (2010)
[83]J. S. Stamler, E. J. Toone, S. A. Lipton and N. J. Sucher: (S)NO signals: translocation, regulation, and a consensus motif. Neuron, 18(5), 691-6 (1997)
[84]L. Santhanam, E. C. Tuday, A. K. Webb, P. Dowzicky, J. H. Kim, Y. J. Oh, G. Sikka, M. Kuo, M. K. Halushka, A. M. Macgregor, J. Dunn, S. Gutbrod, D. Yin, A. Shoukas, D. Nyhan, N. A. Flavahan, A. M. Belkin and D. E. Berkowitz: Decreased S-nitrosylation of tissue transglutaminase contributes to age-related increases in vascular stiffness. Circ Res, 107(1), 117-25 (2010)
[85]A. Mirza, S. L. Liu, E. Frizell, J. Zhu, S. Maddukuri, J. Martinez, P. Davies, R. Schwarting, P. Norton and M. A. Zern: A role for tissue transglutaminase in hepatic injury and fibrogenesis, and its regulation by NF-kappaB. Am J Physiol, 272(2 Pt 1), G281-8 (1997)
[86]P. J. Davies, M. P. Murtaugh, W. T. Moore, Jr., G. S. Johnson and D. Lucas: Retinoic acid-induced expression of tissue transglutaminase in human promyelocytic leukemia (HL-60) cells. J Biol Chem, 260(8), 5166-74 (1985)
[87]U. S. Singh and R. A. Cerione: Biochemical effects of retinoic acid on GTP-binding Protein/Transglutaminases in HeLa cells. Stimulation of GTP-binding and transglutaminase activity, membrane association, and phosphatidylinositol lipid turnover. J Biol Chem, 271(44), 27292-8 (1996)
[88]A. P. Mann, A. Verma, G. Sethi, B. Manavathi, H. Wang, J. Y. Fok, A. B. Kunnumakkara, R. Kumar, B. B. Aggarwal and K. Mehta: Overexpression of Tissue Transglutaminase Leads to Constitutive Activation of Nuclear Factor-{kappa}B in Cancer Cells: Delineation of a Novel Pathway. Cancer Res, 66(17), 8788-95 (2006)
[89]S. Y. Kim: Transglutaminase 2 in inflammation. Front Biosci, 11, 3026-35 (2006)
[90]A. Verma and K. Mehta: Transglutaminase-Mediated Activation of Nuclear Transcription Factor-kappaB in Cancer Cells: A New Therapeutic Opportunity. Curr Cancer Drug Targets, 7(6), 559-65 (2007)
[91]S. Kumar and K. Mehta: Tissue transglutaminase constitutively activates HIF-1alpha promoter and nuclear factor-kappaB via a non-canonical pathway. PLoS One, 7(11), e49321 (2012)
[92]S. J. Ritter and P. J. Davies: Identification of a transforming growth factor-beta1/bone morphogenetic protein 4 (TGF-beta1/BMP4) response element within the mouse tissue transglutaminase gene promoter. J Biol Chem, 273(21), 12798-806 (1998)
[93]A. J. Filiano, C. D. Bailey, J. Tucholski, S. Gundemir and G. V. Johnson: Transglutaminase 2 protects against ischemic insult, interacts with HIF1beta, and attenuates HIF1 signaling. FASEB J, 22(8), 2662-75 (2008)
[94]M. D. George, T. M. Vollberg, E. E. Floyd, J. P. Stein and A. M. Jetten: Regulation of transglutaminase type II by transforming growth factor-beta 1 in normal and transformed human epidermal keratinocytes. J Biol Chem, 265(19), 11098-104 (1990)
[95]M. M. Shull, I. Ormsby, A. B. Kier, S. Pawlowski, R. J. Diebold, M. Yin, R. Allen, C. Sidman, G. Proetzel, D. Calvin and et al.: Targeted disruption of the mouse transforming growth factor-beta 1 gene results in multifocal inflammatory disease. Nature, 359(6397), 693-9 (1992)
[96]Z. Szondy, Z. Sarang, P. Molnar, T. Nemeth, M. Piacentini, P. G. Mastroberardino, L. Falasca, D. Aeschlimann, J. Kovacs, I. Kiss, E. Szegezdi, G. Lakos, E. Rajnavolgyi, P. J. Birckbichler, G. Melino and L. Fesus: Transglutaminase 2-/- mice reveal a phagocytosis-associated crosstalk between macrophages and apoptotic cells. Proc Natl Acad Sci U S A, 100(13), 7812-7 (2003)
[97]Z. A. Haroon, J. M. Hettasch, T. S. Lai, M. W. Dewhirst and C. S. Greenberg: Tissue transglutaminase is expressed, active, and directly involved in rat dermal wound healing and angiogenesis. Faseb J, 13(13), 1787-95 (1999)
[98]Z. A. Haroon, T. S. Lai, J. M. Hettasch, R. A. Lindberg, M. W. Dewhirst and C. S. Greenberg: Tissue transglutaminase is expressed as a host response to tumor invasion and inhibits tumor growth. Lab Invest, 79(12), 1679-86. (1999)
[99]Z. A. Haroon, T. Wannenburg, M. Gupta, C. S. Greenberg, R. Wallin and D. C. Sane: Localization of tissue transglutaminase in human carotid and coronary artery atherosclerosis: implications for plaque stability and progression. Lab Invest, 81(1), 83-93 (2001)
[100]A. Campisi, D. Caccamo, G. Li Volti, M. Curro, G. Parisi, R. Avola, A. Vanella and R. Ientile: Glutamate-evoked redox state alterations are involved in tissue transglutaminase upregulation in primary astrocyte cultures. FEBS Lett, 578(1-2), 80-4 (2004)
[101]C. M. Bergamini, M. Griffin and F. S. Pansini: Transglutaminase and vascular biology: physiopathologic implications and perspectives for therapeutic interventions. Curr Med Chem, 12(20), 2357-72 (2005)
[102]S. Katoh, N. Nakagawa, Y. Yano, K. Satoh, H. Kohno and Y. Ohkubo: Transglutaminase induced by epidermal growth factor negatively regulates the growth signal in primary cultured hepatocytes. Biochem J, 313 ( Pt 1), 305-9 (1996)
[103]R. Ientile, D. Caccamo and M. Griffin: Tissue transglutaminase and the stress response. Amino Acids, 33(2), 385-94 (2007)
[104]V. Thomazy and L. Fesus: Differential expression of tissue transglutaminase in human cells. An immunohistochemical study. Cell Tissue Res, 255(1), 215-24 (1989)
[105]S. Lu and P. J. Davies: Regulation of the expression of the tissue transglutaminase gene by DNA methylation. Proc Natl Acad Sci U S A, 94(9), 4692-7 (1997)
[106]B. Seiving, K. Ohlsson, C. Linder and P. Stenberg: Transglutaminase differentiation during maturation of human blood monocytes to macrophages. Eur J Haematol, 46(5), 263-71 (1991)
[107]M. Lesort, K. Attanavanich, J. Zhang and G. V. Johnson: Distinct nuclear localization and activity of tissue transglutaminase. J Biol Chem, 273(20), 11991-4 (1998)
[108]U. Landmesser, B. Hornig and H. Drexler: Endothelial function: a critical determinant in atherosclerosis? Circulation, 109(21 Suppl 1), II27-33 (2004)
[109]K. Mohan, D. Pinto and T. B. Issekutz: Identification of tissue transglutaminase as a novel molecule involved in human CD8+ T cell transendothelial migration. J Immunol, 171(6), 3179-86 (2003)
[110]S. E. Iismaa, G. E. Begg and R. M. Graham: Cross-linking transglutaminases with G protein-coupled receptor signaling. Sci STKE, 2006(353), pe34 (2006)
[111]S. Mishra and L. J. Murphy: Tissue transglutaminase has intrinsic kinase activity: identification of transglutaminase 2 as an insulin-like growth factor-binding protein-3 kinase. J Biol Chem, 279(23), 23863-8 (2004)
[112]U. S. Singh, J. Pan, Y. L. Kao, S. Joshi, K. L. Young and K. M. Baker: Tissue transglutaminase mediates activation of RhoA and MAP kinase pathways during retinoic acid-induced neuronal differentiation of SH-SY5Y cells. J Biol Chem, 278(1), 391-9 (2003)
[113]S. Mishra, A. Saleh, P. S. Espino, J. R. Davie and L. J. Murphy: Phosphorylation of histones by tissue transglutaminase. J Biol Chem, 281(9), 5532-8 (2006)
[114]M. Piacentini, M. G. Farrace, L. Piredda, P. Matarrese, F. Ciccosanti, L. Falasca, C. Rodolfo, A. M. Giammarioli, E. Verderio, M. Griffin and W. Malorni: Transglutaminase overexpression sensitizes neuronal cell lines to apoptosis by increasing mitochondrial membrane potential and cellular oxidative stress. J Neurochem, 81(5), 1061-72 (2002)
[115]C. Rodolfo, E. Mormone, P. Matarrese, F. Ciccosanti, M. G. Farrace, E. Garofano, L. Piredda, G. M. Fimia, W. Malorni and M. Piacentini: Tissue transglutaminase is a multifunctional BH3-only protein. J Biol Chem, 279(52), 54783-92 (2004)
[116]D. Park, S. S. Choi and K. S. Ha: Transglutaminase 2: a multi-functional protein in multiple subcellular compartments. Amino Acids, 39(3), 619-31 (2010)
[117]Z. Balajthy, K. Csomos, G. Vamosi, A. Szanto, M. Lanotte and L. Fesus: Tissue-transglutaminase contributes to neutrophil granulocyte differentiation and functions. Blood, 108(6), 2045-54 (2006)
[118]Z. Szondy, P. G. Mastroberardino, J. Varadi, M. G. Farrace, N. Nagy, I. Bak, I. Viti, M. R. Wieckowski, G. Melino, R. Rizzuto, A. Tosaki, L. Fesus and M. Piacentini: Tissue transglutaminase (TG2) protects cardiomyocytes against ischemia/reperfusion injury by regulating ATP synthesis. Cell Death Differ, 13(10), 1827-9 (2006)
[119]F. Bernassola, M. Federici, M. Corazzari, A. Terrinoni, M. L. Hribal, V. De Laurenzi, M. Ranalli, O. Massa, G. Sesti, W. H. McLean, G. Citro, F. Barbetti and G. Melino: Role of transglutaminase 2 in glucose tolerance: knockout mice studies and a putative mutation in a MODY patient. FASEB J, 16(11), 1371-8 (2002)
[120]G. Battaglia, M. G. Farrace, P. G. Mastroberardino, I. Viti, G. M. Fimia, J. Van Beeumen, B. Devreese, G. Melino, G. Molinaro, C. L. Busceti, F. Biagioni, F. Nicoletti and M. Piacentini: Transglutaminase 2 ablation leads to defective function of mitochondrial respiratory complex I affecting neuronal vulnerability in experimental models of extrapyramidal disorders. J Neurochem, 100(1), 36-49 (2007)
[121]S. Orru, I. Caputo, A. D’Amato, M. Ruoppolo and C. Esposito: Proteomics identification of acyl-acceptor and acyl-donor substrates for transglutaminase in a human intestinal epithelial cell line. Implications for celiac disease. J Biol Chem, 278(34), 31766-73 (2003)
[122]S. Altuntas, F. Rossin, C. Marsella, M. D’Eletto, L. Diaz-Hidalgo, M. G. Farrace, M. Campanella, M. Antonioli, G. M. Fimia and M. Piacentini: The transglutaminase type 2 and pyruvate kinase isoenzyme M2 interplay in autophagy regulation. Oncotarget, 6(42), 44941-54 (2015)
[123]K. N. Lee, M. D. Maxwell, M. K. Patterson, Jr., P. J. Birckbichler and E. Conway: Identification of transglutaminase substrates in HT29 colon cancer cells: use of 5-(biotinamido)pentylamine as a transglutaminase-specific probe. Biochim Biophys Acta, 1136(1), 12-6 (1992)
[124]B. M. Ku, C. H. Lee, S. H. Lee and S. Y. Kim: Increased expression of transglutaminase 2 drives glycolytic metabolism in renal carcinoma cells. Amino Acids, 46(6), 1527-36 (2014)
[125]R. Rizzuto, P. Pinton, W. Carrington, F. S. Fay, K. E. Fogarty, L. M. Lifshitz, R. A. Tuft and T. Pozzan: Close contacts with the endoplasmic reticulum as determinants of mitochondrial Ca2+ responses. Science, 280(5370), 1763-6 (1998)
[126]K. Hamada, A. Terauchi, K. Nakamura, T. Higo, N. Nukina, N. Matsumoto, C. Hisatsune, T. Nakamura and K. Mikoshiba: Aberrant calcium signaling by transglutaminase-mediated posttranslational modification of inositol 1,4,5-trisphosphate receptors. Proc Natl Acad Sci U S A, 111(38), E3966-75 (2014)
[127]M. J. Berridge, P. Lipp and M. D. Bootman: The versatility and universality of calcium signalling. Nat Rev Mol Cell Biol, 1(1), 11-21 (2000)
[128]J. K. Foskett, C. White, K. H. Cheung and D. O. Mak: Inositol trisphosphate receptor Ca2+ release channels. Physiol Rev, 87(2), 593-658 (2007)
[129]S. Sileno, V. D’Oria, R. Stucchi, M. Alessio, S. Petrini, V. Bonetto, P. Maechler, F. Bertuzzi, V. Grasso, K. Paolella, F. Barbetti and O. Massa: A possible role of transglutaminase 2 in the nucleus of INS-1E and of cells of human pancreatic islets. J Proteomics, 96, 314-27 (2014)
[130]Y. F. Hsieh, G. Y. Liu, Y. J. Lee, J. J. Yang, K. Sandor, Z. Sarang, A. Bononi, P. Pinton, L. Tretter, Z. Szondy and G. J. Tsay: Transglutaminase 2 contributes to apoptosis induction in Jurkat T cells by modulating Ca2+ homeostasis via cross-linking RAP1GDS1. PLoS One, 8(12), e81516 (2013)
[131]J. P. Hutchinson, K. Rittinger and J. F. Eccleston: Purification and characterization of guanine nucleotide dissociation stimulator protein. Methods Enzymol, 325, 71-82 (2000)
[132]P. Kazemi-Esfarjani and A. R. La Spada: Deja vu with a twist: transglutaminases in bioenergetics and transcriptional dysfunction in Huntington’s disease. EMBO Mol Med, 2(9), 335-7 (2010)
[133]A. W. Leung and A. P. Halestrap: Recent progress in elucidating the molecular mechanism of the mitochondrial permeability transition pore. Biochim Biophys Acta, 1777(7-8), 946-52 (2008)
[134]F. Rossin, M. D’Eletto, L. Falasca, S. Sepe, S. Cocco, G. M. Fimia, M. Campanella, P. G. Mastroberardino, M. G. Farrace and M. Piacentini: Transglutaminase 2 ablation leads to mitophagy impairment associated with a metabolic shift towards aerobic glycolysis. Cell Death Differ, 22(3), 408-18 (2015)
[135]H. Lu, G. Li, L. Liu, L. Feng, X. Wang and H. Jin: Regulation and function of mitophagy in development and cancer. Autophagy, 9(11), 1720-36 (2013)
[136]S. Kumar, T. R. Donti, N. Agnihotri and K. Mehta: Transglutaminase 2 reprogramming of glucose metabolism in mammary epithelial cells via activation of inflammatory signaling pathways. Int J Cancer, 134(12), 2798-807 (2014)
[137]O. Warburg: On respiratory impairment in cancer cells. Science, 124(3215), 269-70 (1956)
[138]C. Y. Liu, C. F. Lee, C. H. Hong and Y. H. Wei: Mitochondrial DNA mutation and depletion increase the susceptibility of human cells to apoptosis. Ann N Y Acad Sci, 1011, 133-45 (2004)
[139]J. P. Thiery: Epithelial-mesenchymal transitions in tumour progression. Nat Rev Cancer, 2(6), 442-54 (2002)
[140]I. Nunes, P. E. Gleizes, C. N. Metz and D. B. Rifkin: Latent transforming growth factor-beta binding protein domains involved in activation and transglutaminase-dependent cross-linking of latent transforming growth factor-beta. J Cell Biol, 136(5), 1151-63 (1997)
[141]A. Kumar, J. Xu, S. Brady, H. Gao, D. Yu, J. Reuben and K. Mehta: Tissue transglutaminase promotes drug resistance and invasion by inducing mesenchymal transition in mammary epithelial cells. PLoS One, 5(10), e13390 (2010)
[142]M. L. Huynh, V. A. Fadok and P. M. Henson: Phosphatidylserine-dependent ingestion of apoptotic cells promotes TGF-beta1 secretion and the resolution of inflammation. J Clin Invest, 109(1), 41-50 (2002)
[143]L. Falasca, V. Iadevaia, F. Ciccosanti, G. Melino, A. Serafino and M. Piacentini: Transglutaminase type II is a key element in the regulation of the anti-inflammatory response elicited by apoptotic cell engulfment. J Immunol, 174(11), 7330-40 (2005)
[144]P. G. Mastroberardino, C. Iannicola, R. Nardacci, F. Bernassola, V. De Laurenzi, G. Melino, S. Moreno, F. Pavone, S. Oliverio, L. Fesus and M. Piacentini: ‘Tissue’ transglutaminase ablation reduces neuronal death and prolongs survival in a mouse model of Huntington’s disease. Cell Death Differ, 9(9), 873-80. (2002)
[145]C. D. Bailey and G. V. Johnson: Tissue transglutaminase contributes to disease progression in the R6/2 Huntington’s disease mouse model via aggregate-independent mechanisms. J Neurochem, 92(1), 83-92 (2005)
[146]M. V. Karpuj, M. W. Becher, J. E. Springer, D. Chabas, S. Youssef, R. Pedotti, D. Mitchell and L. Steinman: Prolonged survival and decreased abnormal movements in transgenic model of Huntington disease, with administration of the transglutaminase inhibitor cystamine. Nat Med, 8(2), 143-9. (2002)
[147]A. Dedeoglu, J. K. Kubilus, T. M. Jeitner, S. A. Matson, M. Bogdanov, N. W. Kowall, W. R. Matson, A. J. Cooper, R. R. Ratan, M. F. Beal, S. M. Hersch and R. J. Ferrante: Therapeutic effects of cystamine in a murine model of Huntington’s disease. J Neurosci, 22(20), 8942-50. (2002)
[148]E. Junn, R. D. Ronchetti, M. M. Quezado, S. Y. Kim and M. M. Mouradian: 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(4), 2047-52. (2003)
[149]G. Andringa, K. Y. Lam, M. Chegary, X. Wang, T. N. Chase and M. C. Bennett: Tissue transglutaminase catalyzes the formation of alpha-synuclein crosslinks in Parkinson’s disease. FASEB J, 18(7), 932-4 (2004)
[150]P. H. Jensen, E. S. Sorensen, T. E. Petersen, J. Gliemann and L. K. Rasmussen: Residues in the synuclein consensus motif of the alpha-synuclein fragment, NAC, participate in transglutaminase-catalysed cross-linking to Alzheimer-disease amyloid beta A4 peptide. Biochem J, 310 ( Pt 1), 91-4 (1995)
[151]Z. Nemes, B. Devreese, P. M. Steinert, J. Van Beeumen and L. Fesus: Cross-linking of ubiquitin, HSP27, parkin, and alpha-synuclein by gamma-glutamyl-epsilon-lysine bonds in Alzheimer’s neurofibrillary tangles. FASEB J, 18(10), 1135-7 (2004)
[152]M. M. Wilhelmus, A. M. van Dam and B. Drukarch: Tissue transglutaminase: a novel pharmacological target in preventing toxic protein aggregation in neurodegenerative diseases. Eur J Pharmacol, 585(2-3), 464-72 (2008)
[153]S. AbdAlla, H. Lother, A. el Missiry, A. Langer, P. Sergeev, Y. el Faramawy and U. Quitterer: Angiotensin II AT2 receptor oligomers mediate G-protein dysfunction in an animal model of Alzheimer disease. J Biol Chem, 284(10), 6554-65 (2009)
[154]M. Griffin, R. Casadio and C. M. Bergamini: Transglutaminases: nature’s biological glues. Biochem J, 368(Pt 2), 377-96 (2002)
[155]V. Larreta-Garde and H. Berry: Modeling extracellular matrix degradation balance with proteinase/transglutaminase cycle. J Theor Biol, 217(1), 105-24 (2002)
[156]H. Nakane, A. Ishida-Yamamoto, H. Takahashi and H. Iizuka: Elafin, a secretory protein, is cross-linked into the cornified cell envelopes from the inside of psoriatic keratinocytes. J Invest Dermatol, 119(1), 50-5 (2002)
[157]E. A. Verderio, T. Johnson and M. Griffin: Tissue transglutaminase in normal and abnormal wound healing: review article. Amino Acids, 26(4), 387-404 (2004)
[158]H. Ritchie, L. C. Lawrie, M. W. Mosesson and N. A. Booth: Characterization of crosslinking sites in fibrinogen for plasminogen activator inhibitor 2 (PAI-2). Ann N Y Acad Sci, 936, 215-8 (2001)
[159]K. N. Lee, C. S. Lee, W. C. Tae, K. W. Jackson, V. J. Christiansen and P. A. McKee: Cross-linking of wild-type and mutant alpha 2-antiplasmins to fibrin by activated factor XIII and by a tissue transglutaminase. J Biol Chem, 275(48), 37382-9. (2000)
[160]A. Agah, T. R. Kyriakides and P. Bornstein: Proteolysis of cell-surface tissue transglutaminase by matrix metalloproteinase-2 contributes to the adhesive defect and matrix abnormalities in thrombospondin-2-null fibroblasts and mice. Am J Pathol, 167(1), 81-8 (2005)
[161]E. A. Verderio, D. Telci, A. Okoye, G. Melino and M. Griffin: A novel RGD-independent cel adhesion pathway mediated by fibronectin-bound tissue transglutaminase rescues cells from anoikis. J Biol Chem, 278(43), 42604-14 (2003)
[162]S. S. Akimov and A. M. Belkin: Cell surface tissue transglutaminase is involved in adhesion and migration of monocytic cells on fibronectin. Blood, 98(5), 1567-76 (2001)
[163]S. S. Akimov and A. M. Belkin: Cell-surface transglutaminase promotes fibronectin assembly via interaction with the gelatin-binding domain of fibronectin: a role in TGFbeta-dependent matrix deposition. J Cell Sci, 114(Pt 16), 2989-3000 (2001)
[164]C. Nieder, F. B. Zimmermann, M. Adam and M. Molls: The role of pentoxifylline as a modifier of radiation therapy. Cancer Treat Rev (2005)
[165]N. Suto, K. Ikura and R. Sasaki: Expression induced by interleukin-6 of tissue-type transglutaminase in human hepatoblastoma HepG2 cells. J Biol Chem, 268(10), 7469-73 (1993)
[166]T. S. Johnson, A. F. El-Koraie, N. J. Skill, N. M. Baddour, A. M. El Nahas, M. Njloma, A. G. Adam and M. Griffin: Tissue transglutaminase and the progression of human renal scarring. J Am Soc Nephrol, 14(8), 2052-62 (2003)
[167]N. J. Skill, T. S. Johnson, I. G. Coutts, R. E. Saint, M. Fisher, L. Huang, A. M. El Nahas, R. J. Collighan and M. Griffin: Inhibition of transglutaminase activity reduces extracellular matrix accumulation induced by high glucose levels in proximal tubular epithelial cells. J Biol Chem, 279(46), 47754-62 (2004)
[168]M. Le, C. M. Gohr and A. K. Rosenthal: Transglutaminase participates in the incorporation of latent TGFbeta into the extracellular matrix of aging articular chondrocytes. Connect Tissue Res, 42(4), 245-53 (2001)
[169]I. Yu, C. P. Garnham and A. Roll-Mecak: Writing and Reading the Tubulin Code. J Biol Chem, 290(28), 17163-72 (2015)
[170]L. Piredda, M. G. Farrace, M. Lo Bello, W. Malorni, G. Melino, R. Petruzzelli and M. Piacentini: Identification of ‘tissue’ transglutaminase binding proteins in neural cells committed to apoptosis. Faseb J, 13(2), 355-64 (1999)
[171]P. W. Baas: Microtubule stability in the axon: new answers to an old mystery. Neuron, 78(1), 3-5 (2013)
[172]L. Russo, C. Marsella, G. Nardo, T. Massignan, M. Alessio, E. Piermarini, S. La Rosa, G. Finzi, V. Bonetto, F. Bertuzzi, P. Maechler and O. Massa: Transglutaminase 2 transamidation activity during first-phase insulin secretion: natural substrates in INS-1E. Acta Diabetol, 50(1), 61-72 (2013)
[173]S. Del Duca, D. Serafini-Fracassini, P. Bonner, M. Cresti and G. Cai: Effects of post-translational modifications catalysed by pollen transglutaminase on the functional properties of microtubules and actin filaments. Biochem J, 418(3), 651-64 (2009)
[174]Z. Nemes, Jr., R. Adany, M. Balazs, P. Boross and L. Fesus: Identification of cytoplasmic actin as an abundant glutaminyl substrate for tissue transglutaminase in HL-60 and U937 cells undergoing apoptosis. J Biol Chem, 272(33), 20577-83 (1997)
[175]L. Dolge, K. Aufenvenne, H. Traupe and W. Baumgartner: Beta-actin is a target for transglutaminase activity at synaptic endings in chicken telencephalic cell cultures. J Mol Neurosci, 46(2), 410-9 (2012)
[176]C. H. Yu, C. C. Chou, Y. J. Lee, K. H. Khoo and G. D. Chang: Uncovering protein polyamination by the spermine-specific antiserum and mass spectrometric analysis. Amino Acids, 47(3), 469-81 (2015)
[177]U. S. Singh, M. T. Kunar, Y. L. Kao and K. M. Baker: Role of transglutaminase II in retinoic acid-induced activation of RhoA-associated kinase-2. EMBO J, 20(10), 2413-23 (2001)
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Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.
Tissue transglutaminase (TG2) and mitochondrial function and dysfunction
1 Institute of Biomedical Science, Mackay Medical College, New Taipei City, Taiwan, ROC
2 Nephrology/Department of Internal Medicine, Mackay Memorial Hospital, Taipei, Taiwan, ROC
3 Nursing and Management, Mackay Junior College of Medicine, Taipei, Taiwan, ROC
4 Institute of Biochemistry and Molecular Biology, National Yang-Ming University, Taipei, Taiwan
5 Department of Medicine, Mackay Medical College, New Taipei City, Taiwan, ROC
6 Graduate Institute of Medical Science, Taipei Medical University, Taipei, Taiwan, ROC
Abstract
Mitochondria are the cell’s power plant to satisfy the energy demands. However, dysfunctional mitochondria can cause overproduction of reactive oxygen species (ROS), oxidative stress, and alteration of calcium homeostasis, which are the hallmarks of mitochondrial diseases. Under prolong oxidative stress, repeated cytosolic calcium elevations even only transiently, can lead to activation of some enzymes. One calcium-activated enzyme with demonstrated pathophysiological important in mitochondrial disease is tissue transglutaminase (TG2). TG2 is known as a post-translational modification (PTM) enzyme that is induced by oxidative stress. Compared to other types of PTMs, the physiological significance of TG2 mediated PTM is just beginning to be understood. Once activated, TG2 can modulate transcription, inactivate metabolic enzymes, and cause aggregation of critical proteins. Recent data indicate that TG2’s activity not only can modulate the assembly of respiratory chain complexes but can also modulate the transcription of critical genes including PGC-1α and cytochrome C that are important for function and biogenesis of mitochondria. Here, we summarize dysfunctional mitochondria in diseases such as in neurodegenerative disorders can modulate TG2’s activity and function. TG2 is also important for normal function of mitochondria.
Keywords
- Tissue transglutaminase
- TG2
- Mitochondria
- Post-Translational Modification
- Calcium Homeostasis
- Reactive Oxygen Species
- Transamidation
- Bioenergetics
- Review
References
- [1] G. E. Gibson, A. Starkov, J. P. Blass, R. R. Ratan and M. F. Beal: Cause and consequence: mitochondrial dysfunction initiates and propagates neuronal dysfunction, neuronal death and behavioral abnormalities in age-associated neurodegenerative diseases. Biochim Biophys Acta, 1802(1), 122-34 (2010)
- [2] Y. T. Wu, S. B. Wu and Y. H. Wei: Metabolic reprogramming of human cells in response to oxidative stress: implications in the pathophysiology and therapy of mitochondrial diseases. Curr Pharm Des, 20(35), 5510-26 (2014)
- [3] D. G. Nicholls: Mitochondria and calcium signaling. Cell Calcium, 38(3-4), 311-7 (2005)
- [4] A. I. Tarasov, E. J. Griffiths and G. A. Rutter: Regulation of ATP production by mitochondrial Ca(2+). Cell Calcium, 52(1), 28-35 (2012)
- [5] M. R. Duchen, A. Verkhratsky and S. Muallem: Mitochondria and calcium in health and disease. Cell Calcium, 44(1), 1-5 (2008) 1
- [6] C. Giorgi, F. Baldassari, A. Bononi, M. Bonora, E. De Marchi, S. Marchi, S. Missiroli, S. Patergnani, A. Rimessi, J. M. Suski, M. R. Wieckowski and P. Pinton: Mitochondrial Ca(2+) and apoptosis. Cell Calcium, 52(1), 36-43 (2012)
- [7] A. F. Schinder, E. C. Olson, N. C. Spitzer and M. Montal: Mitochondrial dysfunction is a primary event in glutamate neurotoxicity. J Neurosci, 16(19), 6125-33 (1996)
- [8] N. B. Pivovarova and S. B. Andrews: Calcium-dependent mitochondrial function and dysfunction in neurons. FEBS J, 277(18), 3622-36 (2010)
- [9] M. Kubota, T. Kasahara, T. Nakamura, M. Ishiwata, T. Miyauchi and T. Kato: Abnormal Ca2+ dynamics in transgenic mice with neuron-specific mitochondrial DNA defects. J Neurosci, 26(47), 12314-24 (2006)
- [10] M. McKenzie and M. R. Duchen: Impaired Cellular Bioenergetics Causes Mitochondrial Calcium Handling Defects in MT-ND5 Mutant Cybrids. PLoS One, 11(4), e0154371 (2016)
- [11] M. Brini, P. Pinton, M. P. King, M. Davidson, E. A. Schon and R. Rizzuto: A calcium signaling defect in the pathogenesis of a mitochondrial DNA inherited oxidative phosphorylation deficiency. Nat Med, 5(8), 951-4 (1999)
- [12] E. Mbaya, B. Oules, C. Caspersen, R. Tacine, H. Massinet, M. Pennuto, D. Chretien, A. Munnich, A. Rotig, R. Rizzuto, G. A. Rutter, P. Paterlini-Brechot and M. Chami: Calcium signalling-dependent mitochondrial dysfunction and bioenergetics regulation in respiratory chain Complex II deficiency. Cell Death Differ, 17(12), 1855-66 (2010)
- [13] A. M. Moudy, S. D. Handran, M. P. Goldberg, N. Ruffin, I. Karl, P. Kranz-Eble, D. C. DeVivo and S. M. Rothman: Abnormal calcium homeostasis and mitochondrial polarization in a human encephalomyopathy. Proc Natl Acad Sci U S A, 92(3), 729-33 (1995)
- [14] A. Federico, E. Cardaioli, P. Da Pozzo, P. Formichi, G. N. Gallus and E. Radi: Mitochondria, oxidative stress and neurodegeneration. J Neurol Sci, 322(1-2), 254-62 (2012)
- [15] M. Moran, D. Moreno-Lastres, L. Marin-Buera, J. Arenas, M. A. Martin and C. Ugalde: Mitochondrial respiratory chain dysfunction: implications in neurodegeneration. Free Radic Biol Med, 53(3), 595-609 (2012)
- [16] T. W. Lai, S. Zhang and Y. T. Wang: Excitotoxicity and stroke: identifying novel targets for neuroprotection. Prog Neurobiol, 115, 157-88 (2014)
- [17] L. Lorand and R. M. Graham: Transglutaminases: crosslinking enzymes with pleiotropic functions. Nat Rev Mol Cell Biol, 4(2), 140-56 (2003)
- [18] T. S. Lai, C. J. Lin and C. S. Greenberg: Role of tissue transglutaminase-2 (TG2)-mediated aminylation in biological processes. Amino Acids (2016)
- [19] C. S. Greenberg, P. J. Birckbichler and R. H. Rice: Transglutaminases: multifunctional cross-linking enzymes that stabilize tissues. Faseb J, 5(15), 3071-7. (1991)
- [20] D. Aeschlimann and V. Thomazy: Protein crosslinking in assembly and remodelling of extracellular matrices: the role of transglutaminases. Connect Tissue Res, 41(1), 1-27 (2000)
- [21] R. L. Eckert, M. T. Kaartinen, M. Nurminskaya, A. M. Belkin, G. Colak, G. V. Johnson and K. Mehta: Transglutaminase regulation of cell function. Physiol Rev, 94(2), 383-417 (2014)
- [22] T. S. Lai, and C. S. Greenberg: TGM2 and implications for human disease: role of alternative splicing Frontiers in Bioscience-Landmark,, 18, 504-519 (2013)
- [23] G. Hasegawa, M. Suwa, Y. Ichikawa, T. Ohtsuka, S. Kumagai, M. Kikuchi, Y. Sato and Y. Saito: A novel function of tissue-type transglutaminase: protein disulphide isomerase. Biochem J, 373(Pt 3), 793-803 (2003)
- [24] T. S. Lai, T. F. Slaughter, C. M. Koropchak, Z. A. Haroon and C. S. Greenberg: C-terminal deletion of human tissue transglutaminase enhances magnesium-dependent GTP/ATPase activity. J Biol Chem, 271(49), 31191-5 (1996)
- [25] T. S. Lai, A. Hausladen, T. F. Slaughter, J. P. Eu, J. S. Stamler and C. S. Greenberg: Calcium regulates S-nitrosylation, denitrosylation, and activity of tissue transglutaminase. Biochemistry, 40(16), 4904-10 (2001)
- [26] L. Xu, S. Begum, J. D. Hearn and R. O. Hynes: GPR56, an atypical G protein-coupled receptor, binds tissue transglutaminase, TG2, and inhibits melanoma tumor growth and metastasis. Proc Natl Acad Sci U S A, 103(24), 9023-8 (2006)
- [27] H. Nakaoka, D. M. Perez, K. J. Baek, T. Das, A. Husain, K. Misono, M. J. Im and R. M. Graham: Gh: a GTP-binding protein with transglutaminase activity and receptor signaling function. Science, 264(5165), 1593-6 (1994)
- [28] S. S. Akimov, D. Krylov, L. F. Fleischman and A. M. Belkin: Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin. J Cell Biol, 148(4), 825-38. (2000)
- [29] T. Konno, T. Morii, A. Hirata, S. Sato, S. Oiki and K. Ikura: Covalent blocking of fibril formation and aggregation of intracellular amyloidgenic proteins by transglutaminase-catalyzed intramolecular cross-linking. Biochemistry, 44(6), 2072-9 (2005)
- [30] A. J. Cooper, K. R. Sheu, J. R. Burke, O. Onodera, W. J. Strittmatter, A. D. Roses and J. P. Blass: Transglutaminase-catalyzed inactivation of glyceraldehyde 3-phosphate dehydrogenase and alpha-ketoglutarate dehydrogenase complex by polyglutamine domains of pathological length. Proc Natl Acad Sci U S A, 94(23), 12604-9 (1997)
- [31] A. J. Cooper, J. Wang, R. Pasternack, H. L. Fuchsbauer, R. K. Sheu and J. P. Blass: Lysine-rich histone (H1) is a lysyl substrate of tissue transglutaminase: possible involvement of transglutaminase in the formation of nuclear aggregates in (CAG)(n)/Q(n) expansion diseases. Dev Neurosci, 22(5-6), 404-17 (2000)
- [32] S. Gundemir, G. Colak, J. Tucholski and G. V. Johnson: Transglutaminase 2: a molecular Swiss army knife. Biochim Biophys Acta, 1823(2), 406-19 (2012)
- [33] E. Ballestar, C. Abad and L. Franco: Core histones are glutaminyl substrates for tissue transglutaminase. J Biol Chem, 271(31), 18817-24 (1996)
- [34] J. Lee, Y. S. Kim, D. H. Choi, M. S. Bang, T. R. Han, T. H. Joh and S. Y. Kim: Transglutaminase 2 induces nuclear factor-kappaB activation via a novel pathway in BV-2 microglia. J Biol Chem, 279(51), 53725-35 (2004)
- [35] N. J. Robinson, P. N. Baker, C. J. Jones and J. D. Aplin: A role for tissue transglutaminase in stabilization of membrane-cytoskeletal particles shed from the human placenta. Biol Reprod, 77(4), 648-57 (2007)
- [36] A. J. Cooper, T. M. Jeitner, V. Gentile and J. P. Blass: Cross linking of polyglutamine domains catalyzed by tissue transglutaminase is greatly favored with pathological-length repeats: does transglutaminase activity play a role in (CAG)(n)/Q(n)-expansion diseases? Neurochem Int, 40(1), 53-67. (2002)
- [37] A. M. Belkin: Extracellular TG2: emerging functions and regulation. FEBS J, 278(24), 4704-16 (2011)
- [38] D. J. Walther, J. U. Peter, S. Winter, M. Holtje, N. Paulmann, M. Grohmann, J. Vowinckel, V. Alamo-Bethencourt, C. S. Wilhelm, G. Ahnert-Hilger and M. Bader: Serotonylation of small GTPases is a signal transduction pathway that triggers platelet alpha-granule release. Cell, 115(7), 851-62 (2003)
- [39] N. A. Muma and Z. Mi: Serotonylation and Transamidation of Other Monoamines. ACS Chem Neurosci, 6(7), 961-9 (2015)
- [40] T. S. Lai and C. S. Greenberg: Histaminylation of fibrinogen by tissue transglutaminase-2 (TGM-2): potential role in modulating inflammation. Amino Acids, 45(4), 857-64 (2013)
- [41] J. Vowinckel, S. Stahlberg, N. Paulmann, K. Bluemlein, M. Grohmann, M. Ralser and D. J. Walther: Histaminylation of glutamine residues is a novel posttranslational modification implicated in G-protein signaling. FEBS Lett, 586(21), 3819-24 (2012)
- [42] D. J. Walther, S. Stahlberg and J. Vowinckel: Novel roles for biogenic monoamines: from monoamines in transglutaminase-mediated post-translational protein modification to monoaminylation deregulation diseases. FEBS J, 278(24), 4740-55 (2011)
- [43] R. Szasz and G. L. Dale: Thrombospondin and fibrinogen bind serotonin-derivatized proteins on COAT-platelets. Blood, 100(8), 2827-31 (2002)
- [44] G. L. Dale, P. Friese, P. Batar, S. F. Hamilton, G. L. Reed, K. W. Jackson, K. J. Clemetson and L. Alberio: Stimulated platelets use serotonin to enhance their retention of procoagulant proteins on the cell surface. Nature, 415(6868), 175-9 (2002)
- [45] C. I. Prodan, P. M. Joseph, A. S. Vincent and G. L. Dale: Coated-platelet levels are influenced by smoking, aspirin, and selective serotonin reuptake inhibitors. J Thromb Haemost, 5(10), 2149-51 (2007)
- [46] J. E. Folk: Mechanism and basis for specificity of transglutaminase-catalyzed epsilon-(gamma-glutamyl) lysine bond formation. Adv Enzymol Relat Areas Mol Biol, 54, 1-56 (1983)
- [47] J. E. Folk and S. I. Chung: Transglutaminases. Methods Enzymol, 113, 358-75 (1985)
- [48] L. Lorand and S. M. Conrad: Transglutaminases. Mol Cell Biochem, 58(1-2), 9-35 (1984)
- [49] L. Lorand, K. N. Parameswaran, P. Stenberg, Y. S. Tong, P. T. Velasco, N. A. Jonsson, L. Mikiver and P. Moses: Specificity of guinea pig liver transglutaminase for amine substrates. Biochemistry, 18(9), 1756-65 (1979)
- [50] C. W. Tabor and H. Tabor: Polyamines. Annu Rev Biochem, 53, 749-90 (1984)
- [51] T. S. Lai, T. Tucker, J. R. Burke, W. J. Strittmatter and C. S. Greenberg: Effect of tissue transglutaminase on the solubility of proteins containing expanded polyglutamine repeats. J Neurochem, 88(5), 1253-60 (2004)
- [52] Y. Song, L. L. Kirkpatrick, A. B. Schilling, D. L. Helseth, N. Chabot, J. W. Keillor, G. V. Johnson and S. T. Brady: Transglutaminase and polyamination of tubulin: posttranslational modification for stabilizing axonal microtubules. Neuron, 78(1), 109-23 (2013) doi:10.1.016/j.neuron.2013.0.1.0.36
- [53] S. W. Qiao, J. Piper, G. Haraldsen, I. Oynebraten, B. Fleckenstein, O. Molberg, C. Khosla and L. M. Sollid: Tissue transglutaminase-mediated formation and cleavage of histamine-gliadin complexes: biological effects and implications for celiac disease. J Immunol, 174(3), 1657-63 (2005)
- [54] S. J. McConoughey, M. Basso, Z. V. Niatsetskaya, S. F. Sleiman, N. A. Smirnova, B. C. Langley, L. Mahishi, A. J. Cooper, M. A. Antonyak, R. A. Cerione, B. Li, A. Starkov, R. K. Chaturvedi, M. F. Beal, G. Coppola, D. H. Geschwind, H. Ryu, L. Xia, S. E. Iismaa, J. Pallos, R. Pasternack, M. Hils, J. Fan, L. A. Raymond, J. L. Marsh, L. M. Thompson and R. R. Ratan: Inhibition of transglutaminase 2 mitigates transcriptional dysregulation in models of Huntington disease. EMBO Mol Med, 2(9), 349-70 (2010)
- [55] M. T. Lin and M. F. Beal: Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature, 443(7113), 787-95 (2006)
- [56] T. M. Jeitner, M. B. Bogdanov, W. R. Matson, Y. Daikhin, M. Yudkoff, J. E. Folk, L. Steinman, S. E. Browne, M. F. Beal, J. P. Blass and A. J. Cooper: N(epsilon)-(gamma-L-glutamyl)-L-lysine (GGEL) is increased in cerebrospinal fluid of patients with Huntington’s disease. J Neurochem, 79(5), 1109-12. (2001)
- [57] M. V. Karpuj, H. Garren, H. Slunt, D. L. Price, J. Gusella, M. W. Becher and L. Steinman: 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(13), 7388-93 (1999)
- [58] T. M. Jeitner, K. Battaile and A. J. Cooper: gamma-Glutamylamines and neurodegenerative diseases. Amino Acids, 44(1), 129-42 (2013)
- [59] T. M. Jeitner, W. R. Matson, J. E. Folk, J. P. Blass and A. J. Cooper: Increased levels of gamma-glutamylamines in Huntington disease CSF. J Neurochem, 106(1), 37-44 (2008)
- [60] T. M. Jeitner, N. A. Muma, K. P. Battaile and A. J. Cooper: Transglutaminase activation in neurodegenerative diseases. Future Neurol, 4(4), 449-467 (2009)
- [61] T. Lai, Tucker, T., Burke, JR., Strittmatter, WJ., and Greenberg, CS: Effect of Tissue Transglutaminase on the Solubility of Proteins Containing Expanded Polyglutamine Repeats. J. Neurochemistry, 88(5), 1253-1260 (2004)
- [62] T. Konno, T. Morii, H. Shimizu, S. Oiki and K. Ikura: Paradoxical inhibition of protein aggregation and precipitation by transglutaminase-catalyzed intermolecular cross-linking. J Biol Chem, 280(17), 17520-5 (2005)
- [63] H. T. Orr: Neurodegenerative disease: neuron protection agency. Nature, 431(7010), 747-8 (2004)
- [64] M. Arrasate, S. Mitra, E. S. Schweitzer, M. R. Segal and S. Finkbeiner: Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature, 431(7010), 805-10 (2004)
- [65] S. Boros, E. Ahrman, L. Wunderink, B. Kamps, W. W. de Jong, W. C. Boelens and C. S. Emanuelsson: Site-specific transamidation and deamidation of the small heat-shock protein Hsp20 by tissue transglutaminase. Proteins, 62(4), 1044-52 (2006)
- [66] K. Iwai, Y. Shibukawa, N. Yamazaki and Y. Wada: Transglutaminase 2-dependent deamidation of glyceraldehyde-3-phosphate dehydrogenase promotes trophoblastic cell fusion. J Biol Chem, 289(8), 4989-99 (2014)
- [67] K. N. Parameswaran, X. F. Cheng, E. C. Chen, P. T. Velasco, J. H. Wilson and L. Lorand: Hydrolysis of gamma:epsilon isopeptides by cytosolic transglutaminases and by coagulation factor XIIIa. J Biol Chem, 272(15), 10311-7 (1997)
- [68] R. Kiraly, K. Thangaraju, Z. Nagy, R. Collighan, Z. Nemes, M. Griffin and L. Fesus: Isopeptidase activity of human transglutaminase 2: disconnection from transamidation and characterization by kinetic parameters. Amino Acids, 48(1), 31-40 (2016)
- [69] R. Chandrashekar, N. Tsuji, T. Morales, V. Ozols and K. Mehta: An ERp60-like protein from the filarial parasite Dirofilaria immitis has both transglutaminase and protein disulfide isomerase activity. Proc Natl Acad Sci U S A, 95(2), 531-6 (1998)
- [70] B. Blasko, A. Madi and L. Fesus: Thioredoxin motif of Caenorhabditis elegans PDI-3 provides Cys and His catalytic residues for transglutaminase activity. Biochem Biophys Res Commun, 303(4), 1142-7 (2003)
- [71] P. G. Mastroberardino, M. G. Farrace, I. Viti, F. Pavone, G. M. Fimia, G. Melino, C. Rodolfo and M. Piacentini: “Tissue” transglutaminase contributes to the formation of disulphide bridges in proteins of mitochondrial respiratory complexes. Biochim Biophys Acta, 1757(9-10), 1357-65 (2006)
- [72] W. Malorni, M. G. Farrace, P. Matarrese, A. Tinari, L. Ciarlo, P. Mousavi-Shafaei, M. D’Eletto, G. Di Giacomo, G. Melino, L. Palmieri, C. Rodolfo and M. Piacentini: The adenine nucleotide translocator 1 acts as a type 2 transglutaminase substrate: implications for mitochondrial-dependent apoptosis. Cell Death Differ, 16(11), 1480-92 (2009)
- [73] T. S. Lai, T. F. Slaughter, K. A. Peoples, J. M. Hettasch and C. S. Greenberg: Regulation of human tissue transglutaminase function by magnesium- nucleotide complexes. Identification of distinct binding sites for Mg- GTP and Mg-ATP. J Biol Chem, 273(3), 1776-81. (1998)
- [74] S. Liu, R. A. Cerione and J. Clardy: Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity. Proc Natl Acad Sci U S A, 99(5), 2743-7 (2002)
- [75] D. M. Pinkas, P. Strop, A. T. Brunger and C. Khosla: Transglutaminase 2 undergoes a large conformational change upon activation. PLoS Biol, 5(12), e327 (2007)
- [76] J. H. Jeon, C. W. Kim, D. M. Shin, K. Kim, S. Y. Cho, J. C. Kwon, K. H. Choi, H. S. Kang and I. G. Kim: Differential incorporation of biotinylated polyamines by transglutaminase 2. FEBS Lett, 534(1-3), 180-4 (2003)
- [77] J. H. Jeon, G. Y. Jang, C. W. Kim, D. M. Shin, S. Y. Cho, J. C. Kwon, H. J. Lee, K. H. Choi and I. G. Kim: Cell-based assay for monitoring transglutaminase activity. Anal Biochem, 333(2), 399-401 (2004)
- [78] D. M. Shin, J. H. Jeon, C. W. Kim, S. Y. Cho, J. C. Kwon, H. J. Lee, K. H. Choi, S. C. Park and I. G. Kim: Cell type-specific activation of intracellular transglutaminase 2 by oxidative stress or ultraviolet irradiation: implications of transglutaminase 2 in age-related cataractogenesis. J Biol Chem, 279(15), 15032-9 (2004)
- [79] A. V. Panov, C. A. Gutekunst, B. R. Leavitt, M. R. Hayden, J. R. Burke, W. J. Strittmatter and J. T. Greenamyre: Early mitochondrial calcium defects in Huntington’s disease are a direct effect of polyglutamines. Nat Neurosci, 5(8), 731-6 (2002)
- [80] J. Stamnaes, D. M. Pinkas, B. Fleckenstein, C. Khosla and L. M. Sollid: Redox regulation of transglutaminase 2 activity. J Biol Chem, 285(33), 25402-9 (2010)
- [81] X. Jin, J. Stamnaes, C. Klock, T. R. DiRaimondo, L. M. Sollid and C. Khosla: Activation of extracellular transglutaminase 2 by thioredoxin. J Biol Chem, 286(43), 37866-73 (2011)
- [82] B. G. Han, J. W. Cho, Y. D. Cho, K. C. Jeong, S. Y. Kim and B. I. Lee: Crystal structure of human transglutaminase 2 in complex with adenosine triphosphate. Int J Biol Macromol, 47(2), 190-5 (2010)
- [83] J. S. Stamler, E. J. Toone, S. A. Lipton and N. J. Sucher: (S)NO signals: translocation, regulation, and a consensus motif. Neuron, 18(5), 691-6 (1997)
- [84] L. Santhanam, E. C. Tuday, A. K. Webb, P. Dowzicky, J. H. Kim, Y. J. Oh, G. Sikka, M. Kuo, M. K. Halushka, A. M. Macgregor, J. Dunn, S. Gutbrod, D. Yin, A. Shoukas, D. Nyhan, N. A. Flavahan, A. M. Belkin and D. E. Berkowitz: Decreased S-nitrosylation of tissue transglutaminase contributes to age-related increases in vascular stiffness. Circ Res, 107(1), 117-25 (2010)
- [85] A. Mirza, S. L. Liu, E. Frizell, J. Zhu, S. Maddukuri, J. Martinez, P. Davies, R. Schwarting, P. Norton and M. A. Zern: A role for tissue transglutaminase in hepatic injury and fibrogenesis, and its regulation by NF-kappaB. Am J Physiol, 272(2 Pt 1), G281-8 (1997)
- [86] P. J. Davies, M. P. Murtaugh, W. T. Moore, Jr., G. S. Johnson and D. Lucas: Retinoic acid-induced expression of tissue transglutaminase in human promyelocytic leukemia (HL-60) cells. J Biol Chem, 260(8), 5166-74 (1985)
- [87] U. S. Singh and R. A. Cerione: Biochemical effects of retinoic acid on GTP-binding Protein/Transglutaminases in HeLa cells. Stimulation of GTP-binding and transglutaminase activity, membrane association, and phosphatidylinositol lipid turnover. J Biol Chem, 271(44), 27292-8 (1996)
- [88] A. P. Mann, A. Verma, G. Sethi, B. Manavathi, H. Wang, J. Y. Fok, A. B. Kunnumakkara, R. Kumar, B. B. Aggarwal and K. Mehta: Overexpression of Tissue Transglutaminase Leads to Constitutive Activation of Nuclear Factor-{kappa}B in Cancer Cells: Delineation of a Novel Pathway. Cancer Res, 66(17), 8788-95 (2006)Cited within: 0Google Scholar
- [89] S. Y. Kim: Transglutaminase 2 in inflammation. Front Biosci, 11, 3026-35 (2006)
- [90] A. Verma and K. Mehta: Transglutaminase-Mediated Activation of Nuclear Transcription Factor-kappaB in Cancer Cells: A New Therapeutic Opportunity. Curr Cancer Drug Targets, 7(6), 559-65 (2007)
- [91] S. Kumar and K. Mehta: Tissue transglutaminase constitutively activates HIF-1alpha promoter and nuclear factor-kappaB via a non-canonical pathway. PLoS One, 7(11), e49321 (2012)
- [92] S. J. Ritter and P. J. Davies: Identification of a transforming growth factor-beta1/bone morphogenetic protein 4 (TGF-beta1/BMP4) response element within the mouse tissue transglutaminase gene promoter. J Biol Chem, 273(21), 12798-806 (1998)
- [93] A. J. Filiano, C. D. Bailey, J. Tucholski, S. Gundemir and G. V. Johnson: Transglutaminase 2 protects against ischemic insult, interacts with HIF1beta, and attenuates HIF1 signaling. FASEB J, 22(8), 2662-75 (2008)
- [94] M. D. George, T. M. Vollberg, E. E. Floyd, J. P. Stein and A. M. Jetten: Regulation of transglutaminase type II by transforming growth factor-beta 1 in normal and transformed human epidermal keratinocytes. J Biol Chem, 265(19), 11098-104 (1990)
- [95] M. M. Shull, I. Ormsby, A. B. Kier, S. Pawlowski, R. J. Diebold, M. Yin, R. Allen, C. Sidman, G. Proetzel, D. Calvin and et al.: Targeted disruption of the mouse transforming growth factor-beta 1 gene results in multifocal inflammatory disease. Nature, 359(6397), 693-9 (1992)
- [96] Z. Szondy, Z. Sarang, P. Molnar, T. Nemeth, M. Piacentini, P. G. Mastroberardino, L. Falasca, D. Aeschlimann, J. Kovacs, I. Kiss, E. Szegezdi, G. Lakos, E. Rajnavolgyi, P. J. Birckbichler, G. Melino and L. Fesus: Transglutaminase 2-/- mice reveal a phagocytosis-associated crosstalk between macrophages and apoptotic cells. Proc Natl Acad Sci U S A, 100(13), 7812-7 (2003)
- [97] Z. A. Haroon, J. M. Hettasch, T. S. Lai, M. W. Dewhirst and C. S. Greenberg: Tissue transglutaminase is expressed, active, and directly involved in rat dermal wound healing and angiogenesis. Faseb J, 13(13), 1787-95 (1999)
- [98] Z. A. Haroon, T. S. Lai, J. M. Hettasch, R. A. Lindberg, M. W. Dewhirst and C. S. Greenberg: Tissue transglutaminase is expressed as a host response to tumor invasion and inhibits tumor growth. Lab Invest, 79(12), 1679-86. (1999)
- [99] Z. A. Haroon, T. Wannenburg, M. Gupta, C. S. Greenberg, R. Wallin and D. C. Sane: Localization of tissue transglutaminase in human carotid and coronary artery atherosclerosis: implications for plaque stability and progression. Lab Invest, 81(1), 83-93 (2001)
- [100] A. Campisi, D. Caccamo, G. Li Volti, M. Curro, G. Parisi, R. Avola, A. Vanella and R. Ientile: Glutamate-evoked redox state alterations are involved in tissue transglutaminase upregulation in primary astrocyte cultures. FEBS Lett, 578(1-2), 80-4 (2004)
- [101] C. M. Bergamini, M. Griffin and F. S. Pansini: Transglutaminase and vascular biology: physiopathologic implications and perspectives for therapeutic interventions. Curr Med Chem, 12(20), 2357-72 (2005)
- [102] S. Katoh, N. Nakagawa, Y. Yano, K. Satoh, H. Kohno and Y. Ohkubo: Transglutaminase induced by epidermal growth factor negatively regulates the growth signal in primary cultured hepatocytes. Biochem J, 313 ( Pt 1), 305-9 (1996)
- [103] R. Ientile, D. Caccamo and M. Griffin: Tissue transglutaminase and the stress response. Amino Acids, 33(2), 385-94 (2007)
- [104] V. Thomazy and L. Fesus: Differential expression of tissue transglutaminase in human cells. An immunohistochemical study. Cell Tissue Res, 255(1), 215-24 (1989)
- [105] S. Lu and P. J. Davies: Regulation of the expression of the tissue transglutaminase gene by DNA methylation. Proc Natl Acad Sci U S A, 94(9), 4692-7 (1997)
- [106] B. Seiving, K. Ohlsson, C. Linder and P. Stenberg: Transglutaminase differentiation during maturation of human blood monocytes to macrophages. Eur J Haematol, 46(5), 263-71 (1991)
- [107] M. Lesort, K. Attanavanich, J. Zhang and G. V. Johnson: Distinct nuclear localization and activity of tissue transglutaminase. J Biol Chem, 273(20), 11991-4 (1998)
- [108] U. Landmesser, B. Hornig and H. Drexler: Endothelial function: a critical determinant in atherosclerosis? Circulation, 109(21 Suppl 1), II27-33 (2004)
- [109] K. Mohan, D. Pinto and T. B. Issekutz: Identification of tissue transglutaminase as a novel molecule involved in human CD8+ T cell transendothelial migration. J Immunol, 171(6), 3179-86 (2003)
- [110] S. E. Iismaa, G. E. Begg and R. M. Graham: Cross-linking transglutaminases with G protein-coupled receptor signaling. Sci STKE, 2006(353), pe34 (2006)
- [111] S. Mishra and L. J. Murphy: Tissue transglutaminase has intrinsic kinase activity: identification of transglutaminase 2 as an insulin-like growth factor-binding protein-3 kinase. J Biol Chem, 279(23), 23863-8 (2004)
- [112] U. S. Singh, J. Pan, Y. L. Kao, S. Joshi, K. L. Young and K. M. Baker: Tissue transglutaminase mediates activation of RhoA and MAP kinase pathways during retinoic acid-induced neuronal differentiation of SH-SY5Y cells. J Biol Chem, 278(1), 391-9 (2003)
- [113] S. Mishra, A. Saleh, P. S. Espino, J. R. Davie and L. J. Murphy: Phosphorylation of histones by tissue transglutaminase. J Biol Chem, 281(9), 5532-8 (2006)
- [114] M. Piacentini, M. G. Farrace, L. Piredda, P. Matarrese, F. Ciccosanti, L. Falasca, C. Rodolfo, A. M. Giammarioli, E. Verderio, M. Griffin and W. Malorni: Transglutaminase overexpression sensitizes neuronal cell lines to apoptosis by increasing mitochondrial membrane potential and cellular oxidative stress. J Neurochem, 81(5), 1061-72 (2002)
- [115] C. Rodolfo, E. Mormone, P. Matarrese, F. Ciccosanti, M. G. Farrace, E. Garofano, L. Piredda, G. M. Fimia, W. Malorni and M. Piacentini: Tissue transglutaminase is a multifunctional BH3-only protein. J Biol Chem, 279(52), 54783-92 (2004)
- [116] D. Park, S. S. Choi and K. S. Ha: Transglutaminase 2: a multi-functional protein in multiple subcellular compartments. Amino Acids, 39(3), 619-31 (2010)
- [117] Z. Balajthy, K. Csomos, G. Vamosi, A. Szanto, M. Lanotte and L. Fesus: Tissue-transglutaminase contributes to neutrophil granulocyte differentiation and functions. Blood, 108(6), 2045-54 (2006)
- [118] Z. Szondy, P. G. Mastroberardino, J. Varadi, M. G. Farrace, N. Nagy, I. Bak, I. Viti, M. R. Wieckowski, G. Melino, R. Rizzuto, A. Tosaki, L. Fesus and M. Piacentini: Tissue transglutaminase (TG2) protects cardiomyocytes against ischemia/reperfusion injury by regulating ATP synthesis. Cell Death Differ, 13(10), 1827-9 (2006)
- [119] F. Bernassola, M. Federici, M. Corazzari, A. Terrinoni, M. L. Hribal, V. De Laurenzi, M. Ranalli, O. Massa, G. Sesti, W. H. McLean, G. Citro, F. Barbetti and G. Melino: Role of transglutaminase 2 in glucose tolerance: knockout mice studies and a putative mutation in a MODY patient. FASEB J, 16(11), 1371-8 (2002)
- [120] G. Battaglia, M. G. Farrace, P. G. Mastroberardino, I. Viti, G. M. Fimia, J. Van Beeumen, B. Devreese, G. Melino, G. Molinaro, C. L. Busceti, F. Biagioni, F. Nicoletti and M. Piacentini: Transglutaminase 2 ablation leads to defective function of mitochondrial respiratory complex I affecting neuronal vulnerability in experimental models of extrapyramidal disorders. J Neurochem, 100(1), 36-49 (2007)
- [121] S. Orru, I. Caputo, A. D’Amato, M. Ruoppolo and C. Esposito: Proteomics identification of acyl-acceptor and acyl-donor substrates for transglutaminase in a human intestinal epithelial cell line. Implications for celiac disease. J Biol Chem, 278(34), 31766-73 (2003)
- [122] S. Altuntas, F. Rossin, C. Marsella, M. D’Eletto, L. Diaz-Hidalgo, M. G. Farrace, M. Campanella, M. Antonioli, G. M. Fimia and M. Piacentini: The transglutaminase type 2 and pyruvate kinase isoenzyme M2 interplay in autophagy regulation. Oncotarget, 6(42), 44941-54 (2015)
- [123] K. N. Lee, M. D. Maxwell, M. K. Patterson, Jr., P. J. Birckbichler and E. Conway: Identification of transglutaminase substrates in HT29 colon cancer cells: use of 5-(biotinamido)pentylamine as a transglutaminase-specific probe. Biochim Biophys Acta, 1136(1), 12-6 (1992)
- [124] B. M. Ku, C. H. Lee, S. H. Lee and S. Y. Kim: Increased expression of transglutaminase 2 drives glycolytic metabolism in renal carcinoma cells. Amino Acids, 46(6), 1527-36 (2014)
- [125] R. Rizzuto, P. Pinton, W. Carrington, F. S. Fay, K. E. Fogarty, L. M. Lifshitz, R. A. Tuft and T. Pozzan: Close contacts with the endoplasmic reticulum as determinants of mitochondrial Ca2+ responses. Science, 280(5370), 1763-6 (1998)
- [126] K. Hamada, A. Terauchi, K. Nakamura, T. Higo, N. Nukina, N. Matsumoto, C. Hisatsune, T. Nakamura and K. Mikoshiba: Aberrant calcium signaling by transglutaminase-mediated posttranslational modification of inositol 1,4,5-trisphosphate receptors. Proc Natl Acad Sci U S A, 111(38), E3966-75 (2014)
- [127] M. J. Berridge, P. Lipp and M. D. Bootman: The versatility and universality of calcium signalling. Nat Rev Mol Cell Biol, 1(1), 11-21 (2000)
- [128] J. K. Foskett, C. White, K. H. Cheung and D. O. Mak: Inositol trisphosphate receptor Ca2+ release channels. Physiol Rev, 87(2), 593-658 (2007)
- [129] S. Sileno, V. D’Oria, R. Stucchi, M. Alessio, S. Petrini, V. Bonetto, P. Maechler, F. Bertuzzi, V. Grasso, K. Paolella, F. Barbetti and O. Massa: A possible role of transglutaminase 2 in the nucleus of INS-1E and of cells of human pancreatic islets. J Proteomics, 96, 314-27 (2014)
- [130] Y. F. Hsieh, G. Y. Liu, Y. J. Lee, J. J. Yang, K. Sandor, Z. Sarang, A. Bononi, P. Pinton, L. Tretter, Z. Szondy and G. J. Tsay: Transglutaminase 2 contributes to apoptosis induction in Jurkat T cells by modulating Ca2+ homeostasis via cross-linking RAP1GDS1. PLoS One, 8(12), e81516 (2013)
- [131] J. P. Hutchinson, K. Rittinger and J. F. Eccleston: Purification and characterization of guanine nucleotide dissociation stimulator protein. Methods Enzymol, 325, 71-82 (2000)
- [132] P. Kazemi-Esfarjani and A. R. La Spada: Deja vu with a twist: transglutaminases in bioenergetics and transcriptional dysfunction in Huntington’s disease. EMBO Mol Med, 2(9), 335-7 (2010)
- [133] A. W. Leung and A. P. Halestrap: Recent progress in elucidating the molecular mechanism of the mitochondrial permeability transition pore. Biochim Biophys Acta, 1777(7-8), 946-52 (2008)
- [134] F. Rossin, M. D’Eletto, L. Falasca, S. Sepe, S. Cocco, G. M. Fimia, M. Campanella, P. G. Mastroberardino, M. G. Farrace and M. Piacentini: Transglutaminase 2 ablation leads to mitophagy impairment associated with a metabolic shift towards aerobic glycolysis. Cell Death Differ, 22(3), 408-18 (2015)
- [135] H. Lu, G. Li, L. Liu, L. Feng, X. Wang and H. Jin: Regulation and function of mitophagy in development and cancer. Autophagy, 9(11), 1720-36 (2013)
- [136] S. Kumar, T. R. Donti, N. Agnihotri and K. Mehta: Transglutaminase 2 reprogramming of glucose metabolism in mammary epithelial cells via activation of inflammatory signaling pathways. Int J Cancer, 134(12), 2798-807 (2014)
- [137] O. Warburg: On respiratory impairment in cancer cells. Science, 124(3215), 269-70 (1956)
- [138] C. Y. Liu, C. F. Lee, C. H. Hong and Y. H. Wei: Mitochondrial DNA mutation and depletion increase the susceptibility of human cells to apoptosis. Ann N Y Acad Sci, 1011, 133-45 (2004)
- [139] J. P. Thiery: Epithelial-mesenchymal transitions in tumour progression. Nat Rev Cancer, 2(6), 442-54 (2002)
- [140] I. Nunes, P. E. Gleizes, C. N. Metz and D. B. Rifkin: Latent transforming growth factor-beta binding protein domains involved in activation and transglutaminase-dependent cross-linking of latent transforming growth factor-beta. J Cell Biol, 136(5), 1151-63 (1997)
- [141] A. Kumar, J. Xu, S. Brady, H. Gao, D. Yu, J. Reuben and K. Mehta: Tissue transglutaminase promotes drug resistance and invasion by inducing mesenchymal transition in mammary epithelial cells. PLoS One, 5(10), e13390 (2010)
- [142] M. L. Huynh, V. A. Fadok and P. M. Henson: Phosphatidylserine-dependent ingestion of apoptotic cells promotes TGF-beta1 secretion and the resolution of inflammation. J Clin Invest, 109(1), 41-50 (2002)
- [143] L. Falasca, V. Iadevaia, F. Ciccosanti, G. Melino, A. Serafino and M. Piacentini: Transglutaminase type II is a key element in the regulation of the anti-inflammatory response elicited by apoptotic cell engulfment. J Immunol, 174(11), 7330-40 (2005)
- [144] P. G. Mastroberardino, C. Iannicola, R. Nardacci, F. Bernassola, V. De Laurenzi, G. Melino, S. Moreno, F. Pavone, S. Oliverio, L. Fesus and M. Piacentini: ‘Tissue’ transglutaminase ablation reduces neuronal death and prolongs survival in a mouse model of Huntington’s disease. Cell Death Differ, 9(9), 873-80. (2002)
- [145] C. D. Bailey and G. V. Johnson: Tissue transglutaminase contributes to disease progression in the R6/2 Huntington’s disease mouse model via aggregate-independent mechanisms. J Neurochem, 92(1), 83-92 (2005)
- [146] M. V. Karpuj, M. W. Becher, J. E. Springer, D. Chabas, S. Youssef, R. Pedotti, D. Mitchell and L. Steinman: Prolonged survival and decreased abnormal movements in transgenic model of Huntington disease, with administration of the transglutaminase inhibitor cystamine. Nat Med, 8(2), 143-9. (2002)
- [147] A. Dedeoglu, J. K. Kubilus, T. M. Jeitner, S. A. Matson, M. Bogdanov, N. W. Kowall, W. R. Matson, A. J. Cooper, R. R. Ratan, M. F. Beal, S. M. Hersch and R. J. Ferrante: Therapeutic effects of cystamine in a murine model of Huntington’s disease. J Neurosci, 22(20), 8942-50. (2002)
- [148] E. Junn, R. D. Ronchetti, M. M. Quezado, S. Y. Kim and M. M. Mouradian: 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(4), 2047-52. (2003)
- [149] G. Andringa, K. Y. Lam, M. Chegary, X. Wang, T. N. Chase and M. C. Bennett: Tissue transglutaminase catalyzes the formation of alpha-synuclein crosslinks in Parkinson’s disease. FASEB J, 18(7), 932-4 (2004)
- [150] P. H. Jensen, E. S. Sorensen, T. E. Petersen, J. Gliemann and L. K. Rasmussen: Residues in the synuclein consensus motif of the alpha-synuclein fragment, NAC, participate in transglutaminase-catalysed cross-linking to Alzheimer-disease amyloid beta A4 peptide. Biochem J, 310 ( Pt 1), 91-4 (1995)
- [151] Z. Nemes, B. Devreese, P. M. Steinert, J. Van Beeumen and L. Fesus: Cross-linking of ubiquitin, HSP27, parkin, and alpha-synuclein by gamma-glutamyl-epsilon-lysine bonds in Alzheimer’s neurofibrillary tangles. FASEB J, 18(10), 1135-7 (2004)
- [152] M. M. Wilhelmus, A. M. van Dam and B. Drukarch: Tissue transglutaminase: a novel pharmacological target in preventing toxic protein aggregation in neurodegenerative diseases. Eur J Pharmacol, 585(2-3), 464-72 (2008)
- [153] S. AbdAlla, H. Lother, A. el Missiry, A. Langer, P. Sergeev, Y. el Faramawy and U. Quitterer: Angiotensin II AT2 receptor oligomers mediate G-protein dysfunction in an animal model of Alzheimer disease. J Biol Chem, 284(10), 6554-65 (2009)
- [154] M. Griffin, R. Casadio and C. M. Bergamini: Transglutaminases: nature’s biological glues. Biochem J, 368(Pt 2), 377-96 (2002)
- [155] V. Larreta-Garde and H. Berry: Modeling extracellular matrix degradation balance with proteinase/transglutaminase cycle. J Theor Biol, 217(1), 105-24 (2002)
- [156] H. Nakane, A. Ishida-Yamamoto, H. Takahashi and H. Iizuka: Elafin, a secretory protein, is cross-linked into the cornified cell envelopes from the inside of psoriatic keratinocytes. J Invest Dermatol, 119(1), 50-5 (2002)
- [157] E. A. Verderio, T. Johnson and M. Griffin: Tissue transglutaminase in normal and abnormal wound healing: review article. Amino Acids, 26(4), 387-404 (2004)
- [158] H. Ritchie, L. C. Lawrie, M. W. Mosesson and N. A. Booth: Characterization of crosslinking sites in fibrinogen for plasminogen activator inhibitor 2 (PAI-2). Ann N Y Acad Sci, 936, 215-8 (2001)
- [159] K. N. Lee, C. S. Lee, W. C. Tae, K. W. Jackson, V. J. Christiansen and P. A. McKee: Cross-linking of wild-type and mutant alpha 2-antiplasmins to fibrin by activated factor XIII and by a tissue transglutaminase. J Biol Chem, 275(48), 37382-9. (2000)
- [160] A. Agah, T. R. Kyriakides and P. Bornstein: Proteolysis of cell-surface tissue transglutaminase by matrix metalloproteinase-2 contributes to the adhesive defect and matrix abnormalities in thrombospondin-2-null fibroblasts and mice. Am J Pathol, 167(1), 81-8 (2005)
- [161] E. A. Verderio, D. Telci, A. Okoye, G. Melino and M. Griffin: A novel RGD-independent cel adhesion pathway mediated by fibronectin-bound tissue transglutaminase rescues cells from anoikis. J Biol Chem, 278(43), 42604-14 (2003)
- [162] S. S. Akimov and A. M. Belkin: Cell surface tissue transglutaminase is involved in adhesion and migration of monocytic cells on fibronectin. Blood, 98(5), 1567-76 (2001)
- [163] S. S. Akimov and A. M. Belkin: Cell-surface transglutaminase promotes fibronectin assembly via interaction with the gelatin-binding domain of fibronectin: a role in TGFbeta-dependent matrix deposition. J Cell Sci, 114(Pt 16), 2989-3000 (2001)
- [164] C. Nieder, F. B. Zimmermann, M. Adam and M. Molls: The role of pentoxifylline as a modifier of radiation therapy. Cancer Treat Rev (2005)
- [165] N. Suto, K. Ikura and R. Sasaki: Expression induced by interleukin-6 of tissue-type transglutaminase in human hepatoblastoma HepG2 cells. J Biol Chem, 268(10), 7469-73 (1993)
- [166] T. S. Johnson, A. F. El-Koraie, N. J. Skill, N. M. Baddour, A. M. El Nahas, M. Njloma, A. G. Adam and M. Griffin: Tissue transglutaminase and the progression of human renal scarring. J Am Soc Nephrol, 14(8), 2052-62 (2003)
- [167] N. J. Skill, T. S. Johnson, I. G. Coutts, R. E. Saint, M. Fisher, L. Huang, A. M. El Nahas, R. J. Collighan and M. Griffin: Inhibition of transglutaminase activity reduces extracellular matrix accumulation induced by high glucose levels in proximal tubular epithelial cells. J Biol Chem, 279(46), 47754-62 (2004)
- [168] M. Le, C. M. Gohr and A. K. Rosenthal: Transglutaminase participates in the incorporation of latent TGFbeta into the extracellular matrix of aging articular chondrocytes. Connect Tissue Res, 42(4), 245-53 (2001)
- [169] I. Yu, C. P. Garnham and A. Roll-Mecak: Writing and Reading the Tubulin Code. J Biol Chem, 290(28), 17163-72 (2015)
- [170] L. Piredda, M. G. Farrace, M. Lo Bello, W. Malorni, G. Melino, R. Petruzzelli and M. Piacentini: Identification of ‘tissue’ transglutaminase binding proteins in neural cells committed to apoptosis. Faseb J, 13(2), 355-64 (1999)
- [171] P. W. Baas: Microtubule stability in the axon: new answers to an old mystery. Neuron, 78(1), 3-5 (2013)
- [172] L. Russo, C. Marsella, G. Nardo, T. Massignan, M. Alessio, E. Piermarini, S. La Rosa, G. Finzi, V. Bonetto, F. Bertuzzi, P. Maechler and O. Massa: Transglutaminase 2 transamidation activity during first-phase insulin secretion: natural substrates in INS-1E. Acta Diabetol, 50(1), 61-72 (2013)
- [173] S. Del Duca, D. Serafini-Fracassini, P. Bonner, M. Cresti and G. Cai: Effects of post-translational modifications catalysed by pollen transglutaminase on the functional properties of microtubules and actin filaments. Biochem J, 418(3), 651-64 (2009)
- [174] Z. Nemes, Jr., R. Adany, M. Balazs, P. Boross and L. Fesus: Identification of cytoplasmic actin as an abundant glutaminyl substrate for tissue transglutaminase in HL-60 and U937 cells undergoing apoptosis. J Biol Chem, 272(33), 20577-83 (1997)
- [175] L. Dolge, K. Aufenvenne, H. Traupe and W. Baumgartner: Beta-actin is a target for transglutaminase activity at synaptic endings in chicken telencephalic cell cultures. J Mol Neurosci, 46(2), 410-9 (2012)
- [176] C. H. Yu, C. C. Chou, Y. J. Lee, K. H. Khoo and G. D. Chang: Uncovering protein polyamination by the spermine-specific antiserum and mass spectrometric analysis. Amino Acids, 47(3), 469-81 (2015)
- [177] U. S. Singh, M. T. Kunar, Y. L. Kao and K. M. Baker: Role of transglutaminase II in retinoic acid-induced activation of RhoA-associated kinase-2. EMBO J, 20(10), 2413-23 (2001)
