Identification of cytoplasmic actin as an abundant glutaminyl substrate for tissue transglutaminase in HL-60 and U937 cells undergoing apoptosis

Zoltán Nemes, Róza Adány, Margit Balázs, Peter Boross, László Fésüs

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A lysine derivative, 3-[N(α)[N(ε)[2',4'-dinitrophenyl]-amino-n- hexanoyl-L-lysylamido]-propane-1-ol, a novel amine substrate of transglutaminases, was synthesized and delivered into intact HL-60 and U937 human leukemia cells to probe the function of the intracellular enzyme. The novel substrate compound was covalently incorporated into intracellular proteins in these cells expressing high levels of tissue transglutaminase and undergoing apoptosis following the induction of their differentiation with dimethyl sulfoxide and retinoic acid. Immunoaffinity purification and microsequencing of labeled proteins identified cytoplasmic actin as the main endogenous glutaminyl substrate in these cells. As shown by confocal image analysis, cells revealed distinct labeling of the microfilament meshwork structures by the novel compound as the result of the intracellular action of transglutaminase.

Original languageEnglish
Pages (from-to)20577-20583
Number of pages7
JournalJournal of Biological Chemistry
Issue number33
Publication statusPublished - Aug 15 1997


ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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