Tissue transglutaminase is a caspase substrate during apoptosis. Cleavage causes loss of transamidating function and is a biochemical marker of caspase 3 activation

Marina Fabbi, Danilo Marimpietri, Stefania Martini, Claudio Brancolini, Angela Amoresano, Andrea Scaloni, Antonio Bargellesi, Elisabetta Cosulich

Research output: Contribution to journalArticle


Tissue transglutaminase (tTG) is a Ca2+-dependent cross-linking enzyme that participates in the apoptotic machinery by irreversibly assembling a protein scaffold that prevents the leakage of intracellular components. In the present study a single-chain antibody fragment (scFv) detecting tTG is described. We demonstrate that TG/F8 scFv, selected from a phase display library of human V-gene segments by binding to guinea-pig liver tTG, can react with human tTG, both in Western blot and in immunohistochemistry. The specific detection of tTG by TG/F8 in human thymocytes is verified by mass spectrometric analysis of the purified protein. Furthermore, we demonstrate that in lymphoid cells tTG is cleaved by caspase 3 during the late phase of apoptotic death, concomitant to DNA fragmentation, cleavage causes loss of cross-linking propose tTG cleavage as a valuable biochemical marker of caspase 3 activation during the late execution phase of apoptosis.

Original languageEnglish
Pages (from-to)992-1001
Number of pages10
JournalCell Death and Differentiation
Issue number10
Publication statusPublished - Oct 1999



  • Apoptosis
  • Caspase 3
  • Single chain antibody fragment
  • Tissue transglutaminase

ASJC Scopus subject areas

  • Cell Biology

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