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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.
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Submitted February 9, 2004
Accepted May 9, 2006
Tissue-transglutaminase contributes to neutrophil
granulocyte differentiation and functions
Zoltan Balajthy*, Krisztian Csomos, Gyorgy Vamosi, Attila Szanto, Michel Lanotte, and Laszlo Fesus
University of Debrecen, Medical and Health Science Center
INSERM U-685
* Corresponding author; email: zoli{at}indi.biochem.dote.hu.
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-catalysed 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, as compared to 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 intra- and extracellular
functions of extravasating neutrophil.
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