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A more recent version of this article appeared on June 1, 2007

Published online before print March 16, 2007
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© by The Society for Leukocyte Biology
Journal of Leukocyte Biology, doi:10.1189/jlb.1106672


Received for publication November 12, 2006.
Revised January 30, 2007.
Accepted for publication February 12, 2007.


Article

Catalase potentiates retinoic acid-induced THP-1 monocyte differentiation into macrophage through inhibition of peroxisome proliferator-activated receptor {gamma}

Qiurong Ding , Ting Jin , Zhenzhen Wang , and Yan Chen @

Institute for Nutritional Sciences, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Graduate School of the Chinese Academy of Sciences, Shanghai, China

@ To whom correspondence should be addressed. E-mail: ychen3{at}sibs.ac.cn.


   Abstract

Macrophage differentiation plays a pivotal role in cardiovascular diseases and many other physiological processes. However, the role of reaction oxygen species in macrophage differentiation has not been elucidated. Here, we report functional characterization of catalase, an enzyme that degrades hydrogen peroxide (H2O2), in THP-1 monocyte differentiation. Treatment of THP-1 cells with catalase was able to synergize with all-trans retinoic acid (ATRA) to enhance macrophage differentiation, demonstrated by changes of cell adherence, cell cycle arrest, nitroblue tetrazolium reduction, and expression of differentiation markers including CD68, CD11b, and matrix metalloproteinase 9 (MMP9). ATRA could stimulate retinoic acid (RA) receptor-mediated transcription, but this was not affected by catalase. However, ATRA and catalase were capable of reducing transcriptional activity mediated by peroxisome proliferator-activated receptor {gamma} (PPAR{gamma}). Consistently, PPAR{gamma} antagonists enhanced, and PPAR{gamma} agonists inhibited MMP9 expression stimulated by ATRA and catalase in THP-1 cells. Therefore, these data indicate that catalase is able to potentiate ATRA-induced macrophage differentiation by inhibition of PPAR{gamma} activity, underscoring an important interplay between H2O2, RA, and PPAR{gamma} in macrophages.

Key Words: PPAR • ROS




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