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Blood, 15 September 2006, Vol. 108, No. 6, pp. 2045-2054. Prepublished online as a Blood First Edition Paper on June 8, 2006; DOI 10.1182/blood-2004-02-007948. This Article Full Text Full Text (PDF) All Versions of this Article: blood-2004-02-007948v1 108/6/2045    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Balajthy, Z. Articles by Fésüs, L. Search for Related Content PubMed PubMed Citation Articles by Balajthy, Z. Articles by Fésüs, L. Related Collections Phagocytes Signal Transduction Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  PHAGOCYTES Tissue-transglutaminase contributes to neutrophil granulocyte differentiation and functions Zoltán Balajthy, Krisztián Csomós, György Vámosi, Attila Szántó, Michel Lanotte, and László Fésüs From the Department of Biochemistry and Molecular Biology, the Cell Biophysics Research Group of the Hungarian Academy of Sciences, and the Signalling and Apoptosis Research Group of the Hungarian Academy of Sciences, Department of Biochemistry and Molecular Biology, Research Center for Molecular Medicine, University of Debrecen, Hungary; and the Institut National de la Santé et de la Recherche Médicale (INSERM) Unité 685 (U685), Hôpital Saint Louis, Paris, France. Promyelocytic NB4 leukemia cells undergo differentiation to granulocytes following retinoic acid treatment. Here we report that tissue transglutaminase (TG2), a protein cross-linking enzyme, was induced, then partially translocated into the nucleus, and became strongly associated with the chromatin during the differentiation process. The transglutaminase-catalyzed cross-link content of both the cytosolic and the nuclear protein fractions increased while NB4 cells underwent cellular maturation. Inhibition of cross-linking activity of TG2 by monodansylcadaverin in these cells led to diminished nitroblue tetrazolium (NBT) positivity, production of less superoxide anion, and decreased expression of GP91PHOX, the membrane-associated subunit of NADPH oxidase. Neutrophils isolated from TG2–/– mice showed diminished NBT reduction capacity, reduced superoxide anion formation, and down-regulation of the gp91phox subunit of NADPH oxidase, compared with wild-type cells. It was also observed that TG2–/– mice exhibited increased neutrophil phagocytic activity, but had attenuated neutrophil chemotaxis and impaired neutrophil extravasation with higher neutrophil counts in their circulation during yeast extract–induced peritonitis. These results clearly suggest that TG2 may modulate the expression of genes related to neutrophil functions and is involved in several intracellular and extracellular functions of extravasating neutrophil. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: L. Falasca, M. G. Farrace, A. Rinaldi, L. Tuosto, G. Melino, and M. Piacentini Transglutaminase Type II Is Involved in the Pathogenesis of Endotoxic Shock J. Immunol., February 15, 2008; 180(4): 2616 - 2624. [Abstract] [Full Text] [PDF] T. Liu, A. E. L. Tee, A. Porro, S. A. Smith, T. Dwarte, P. Y. Liu, N. Iraci, E. Sekyere, M. Haber, M. D. Norris, et al. Activation of tissue transglutaminase transcription by histone deacetylase inhibition as a therapeutic approach for Myc oncogenesis PNAS, November 20, 2007; 104(47): 18682 - 18687. [Abstract] [Full Text] [PDF]

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