Abstract
Regulation of the reactive oxygen species (ROS) producing NADPH oxidase, expressed in neutrophils, is essential for a balance between the proinflammatory antimicrobial host defence and the resolving reactivity that limits tissue destructing inflammatory processes. Peripheral blood neutrophils of healthy adults were isolated from buffy coats obtained from the blood bank at Sahlgrenska University Hospital, using a standard density-gradient centrifugation protocol. The neutrophils were activated by fMet-Leu-Phe (fMLF) a peptide recognized by formyl peptide receptor 1 (FPR1). Signals generated downstream of the agonist occupied FPR1 activate the NADPH oxidase in the neutrophil plasma membrane. The release of ROS by fMLF activated neutrophils was measured in real time using a very sensitive isoluminol-amplified chemiluminescence system, expressed in light units (Mega counts per minute; Mcpm), and the peak value levels of the responses were determined. The activation signals generated by FPR1 were inhibited (reduced peak values) by the agonist occupied EP(4), a neutrophil receptor for prostaglandin E(2) (PGE(2)). The inhibitory effect of PGE(2) was expected to be increased (positively modulated) by Resolvin D(5) (RvD(5)), generated from the omega-3 fatty acid docosahexaenoic acid and a member of the group of specialized pro-resolving lipids. The dataset presented in the article includes raw data on the effects of RvD(5) on the inhibitory activity of PGE(2). The reuse of data indicating a lack of inhibition of a negative allosteric modulator on ROS production in neutrophils is high and multifaceted across several different research domains such as drug development (drug effects lies elsewhere or should be re-evaluated) and immunological research (neutrophil studies and animal models and as reference for testing the robustness or specificity of other ROS-detecting assays or biosensors).