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   <subfield code="a">10.1007/s00726-007-0517-0</subfield>
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   <subfield code="a">Tissue transglutaminase and the stress response</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[R. Ientile, D. Caccamo, M. Griffin]</subfield>
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   <subfield code="a">Summary.: The expression of the protein crosslinking enzyme tissue transglutaminase (TG2, tTG), the ubiquitous member of transglutaminase family, can be regulated by multiple factors. Although it has been suggested that TG2 can be involved in apoptotic cell death, high levels of enzyme have also been associated with cell survival in response to different stimuli. Furthermore, evidence indicates that increases in TG2 production cause enzyme translocation to cell membrane. Cell stress can also lead to TG2 accumulation on the cell surface and in the extracellular matrix resulting in changes in cell-matrix interactions. Here, we discuss the underlying mechanisms of TG2 up-regulation induced by various stimuli including glutamate exposure, calcium influx, oxidative stress, UV, and inflammatory cytokines. These findings agree with a postulated role for transglutaminases in molecular mechanisms involved in several diseases suggesting that cross-linking reactions could be a relevant part of the biochemical changes observed in pathological conditions.</subfield>
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   <subfield code="a">Springer-Verlag, 2007</subfield>
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  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">Keywords: Transglutaminases - Tissue transglutaminase - Neurodegeneration - Oxidative stress - Inflammation - Extracellular matrix</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">AMPA : α-amino-3-hydroxy-5-methyl-4-isoxazole-propionic acid</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">CD : celiac disease</subfield>
   <subfield code="2">nationallicence</subfield>
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  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">ECM : extracellular matrix</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">FN : fibronectin</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">GYKI 52466 : 1-(4′-aminophenyl)-4-methyl-7,8-methylenedioxy-5H-2,3-benzo-diazepine</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">IFN-γ : interferon-γ</subfield>
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   <subfield code="a">LPA : lysophosphatidic acid</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">TGF-beta : transforming growth factor-beta</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">MK-801 : (+)-5-Methyl-10,11-dihydro-5H-dibenzo [a, d]-cyclohepten-5,10-imine hydrogen maleate</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">NF-κB : nuclear factor-kappa B</subfield>
   <subfield code="2">nationallicence</subfield>
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  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">NMDA : N-methyl-D-aspartic acid</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">3-NP : 3-nitropropionic acid</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">PLA2 : phospholipase A2</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">ROS : reactive oxygen species</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">TG(s) : transglutaminase(s)</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">TG2 : tissue transglutaminase</subfield>
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   <subfield code="a">Ientile</subfield>
   <subfield code="D">R.</subfield>
   <subfield code="u">Department of Biochemical, Physiological and Nutritional Sciences, University of Messina, Messina, Italy</subfield>
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   <subfield code="a">Metadata rights reserved</subfield>
   <subfield code="b">Springer special CC-BY-NC licence</subfield>
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