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Toxins 2010, 2(1), 95-115; doi:10.3390/toxins2010095
Article

Calprotectin (S100A8/S100A9) and Myeloperoxidase: Co-Regulators of Formation of Reactive Oxygen Species

1,4,* , 1,†, 1
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2
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3
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4
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1 Norwegian Defence Research Establishment, Division for Protection, P.O.B. 25, 2027 Kjeller, Norway 2 Institute of Medical Microbiology, National Hospital, 0027 Oslo, Norway 3 Department of Molecular Biosciences, University of Oslo, P.O. Box 1041 Blindern, NO-0316 Oslo, Norway 4 Department of Physiology, Institute of Basic Medical Sciences, University of Oslo, P.O.B. 1103 Blindern, N-0317, Oslo University of Oslo, Norway Deceased on 18 October 2009
* Author to whom correspondence should be addressed.
Received: 12 December 2009 / Accepted: 18 January 2010 / Published: 20 January 2010
(This article belongs to the collection Toxicity and Therapeutic Interventions in the Immune System)
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Abstract

Inflammatory mediators trigger polymorphonuclear neutrophils (PMN) to produce reactive oxygen species (ROS: O2-, H2O2, ∙OH). Mediated by myeloperoxidase in PMN, HOCl is formed, detectable in a chemiluminescence (CL) assay. We have shown that the abundant cytosolic PMN protein calprotectin (S100A8/A9) similarly elicits CL in response to H2O2 in a cell-free system. Myeloperoxidase and calprotectin worked synergistically. Calprotectin-induced CL increased, whereas myeloperoxidase-triggered CL decreased with pH > 7.5. Myeloperoxidase needed NaCl for CL, calprotectin did not. 4-hydroxybenzoic acid, binding ∙OH, almost abrogated calprotectin CL, but moderately increased myeloperoxidase activity. The combination of native calprotectin, or recombinant S100A8/A9 proteins, with NaOCl markedly enhanced CL. NaOCl may be the synergistic link between myeloperoxidase and calprotectin. Surprisingly- and unexplained- at higher concentration of S100A9 the stimulation vanished, suggesting a switch from pro-oxidant to anti-oxidant function. We propose that the ∙OH is predominant in ROS production by calprotectin, a function not described before.
Keywords: chemiluminescence; polymorphonuclear neutrophils (PMN); myeloperoxidase; calprotectin; S100A8/A9; NaOCl; albumin; cytidine deaminase; 4-hydroxy-benzoic acid chemiluminescence; polymorphonuclear neutrophils (PMN); myeloperoxidase; calprotectin; S100A8/A9; NaOCl; albumin; cytidine deaminase; 4-hydroxy-benzoic acid
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).
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Bøyum, A.; Skrede, K.K.; Myhre, O.; Tennfjord, V.-A.; Neurauter, C.G.; Tolleshaug, H.; Knudsen, E.; Opstad, P.K.; Bjørås, M.; Benestad, H.B. Calprotectin (S100A8/S100A9) and Myeloperoxidase: Co-Regulators of Formation of Reactive Oxygen Species. Toxins 2010, 2, 95-115.

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