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• Bøyum, A
• Skrede, K
• Myhre, O
• Tennfjord, V
• Neurauter, C
• Tolleshaug, H
• Knudsen, E
• Opstad, P
• Bjørås, M
• Benestad, H
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• Bøyum, A
• Skrede, K
• Myhre, O
• Tennfjord, V
• Neurauter, C
• Tolleshaug, H
• Knudsen, E
• Opstad, P
• Bjørås, M
• Benestad, H
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• Bøyum, A
• Skrede, K
• Myhre, O
• Tennfjord, V
• Neurauter, C
• Tolleshaug, H
• Knudsen, E
• Opstad, P
• Bjørås, M
• Benestad, H

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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

Arne Bøyum ^1,4,* , Knut Kristian Skrede ^1,† , Oddvar Myhre ¹ , Vivi-Ann Tennfjord ¹ , Christine Gran Neurauter ² , Helge Tolleshaug ³ , Eirunn Knudsen ⁴ , Per Kristian Opstad ¹ , Magnar Bjørås ²  and Haakon B. Benestad ⁴

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 Special Issue Toxicity and Therapeutic Interventions in the Immune System)

Download PDF Full-Text [616 KB, uploaded 20 January 2010 16:32 CET]

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

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