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J Biol Chem, Vol. 274, Issue 33, 22907-22910, August 13, 1999

COMMUNICATION
Intracellular Fragmentation of Bone Resorption Products by Reactive Oxygen Species Generated by Osteoclastic Tartrate-resistant Acid Phosphatase

Jussi M. Halleen, Seija Räisänen, Jari J. Salo^§, Sakamuri V. Reddy^¶, G. David Roodman^¶, Teuvo A. Hentunen, Petri P. Lehenkari, Helena Kaija^**, Pirkko Vihko, and H. Kalervo Väänänen

From the  Institute of Biomedicine, Department of Anatomy, University of Turku, FIN-20520 Turku, Finland, ^§ Department of Orthopaedics and Traumatology, Helsinki University Central Hospital, FIN-00260 Helsinki, Finland, ^¶ Department of Medicine and Hematology, University of Texas Health Science Center, San Antonio, Texas 78284-7880,  Bone and Mineral Centre, The Rayne Institute, London WC1E 6JJ, United Kingdom, ^** Biocenter Oulu and World Health Organization Collaborating Centre for Research on Reproductive Health, University of Oulu, FIN-90220 Oulu, Finland, and ^§§ Department of Biosciences, University of Helsinki, FIN-00014 Helsinki, Finland

Tartrate-resistant acid phosphatase (TRAP) is highly expressed in bone-resorbing osteoclasts and activated macrophages. It has been suggested that a redox-active iron in the binuclear iron center of TRAP could have the capacity to react with hydrogen peroxide to produce highly destructive reactive oxygen species (ROS). Here we show that TRAP can generate ROS in vitro and that cells over-expressing TRAP produce higher amounts of intracellular ROS than their parent cells. We further demonstrate that these ROS can be targeted to destroy collagen and other proteins. In resorbing osteoclasts, TRAP was found in transcytotic vesicles transporting matrix degradation products through the cell, suggesting that TRAP-facilitated fragmentation of endocytosed material takes place in a specific cellular compartment. These results suggest that bone matrix degradation occurs not only extracellularly in the resorption lacunae but also intracellularly in the transcytotic vesicles. We propose that proteins containing redox-active iron could represent a novel mechanism of physiological fragmentation of organic molecules. This mechanism could be important in tissue remodeling and as a defense mechanism of phagocytosing cells.

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