Recognition of S100 proteins by Signal Inhibitory Receptor on Leukocytes-1 negatively regulates human neutrophils
Rumpret, Matevž; von Richthofen, Helen J.; van der Linden, Maarten; Westerlaken, Geertje H.A.; Talavera Ormeño, Cami; Low, Teck Y.; Ovaa, Huib; Meyaard, Linde
(2021) European Journal of Immunology, volume 51, issue 9, pp. 2210 - 2217
(Article)
Abstract
Signal inhibitory receptor on leukocytes-1 (SIRL-1) is an inhibitory receptor with a hitherto unknown ligand, and is expressed on human monocytes and neutrophils. SIRL-1 inhibits myeloid effector functions such as reactive oxygen species (ROS) production. In this study, we identify S100 proteins as SIRL-1 ligands. S100 proteins are composed of
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two calcium-binding domains. Various S100 proteins are damage-associated molecular patterns (DAMPs) released from damaged cells, after which they initiate inflammation by ligating activating receptors on immune cells. We now show that the inhibitory SIRL-1 recognizes individual calcium-binding domains of all tested S100 proteins. Blocking SIRL-1 on human neutrophils enhanced S100 protein S100A6-induced ROS production, showing that S100A6 suppresses neutrophil ROS production via SIRL-1. Taken together, SIRL-1 is an inhibitory receptor recognizing the S100 protein family of DAMPs. This may help limit tissue damage induced by activated neutrophils.
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Keywords: DAMP, immune regulation, inhibitory receptor, S100, SIRL-1, Reactive Oxygen Species/metabolism, Receptors, Immunologic/antagonists & inhibitors, Neutrophil Activation/immunology, Humans, Alarmins/immunology, Inflammation/immunology, S100 Proteins/immunology, Neutrophils/immunology, Monocytes/immunology, Signal Transduction/immunology, Immunology and Allergy, Immunology, Journal Article, Research Support, Non-U.S. Gov't
ISSN: 0014-2980
Publisher: Wiley-VCH Verlag
Note: Publisher Copyright: © 2021 The Authors. European Journal of Immunology published by Wiley-VCH GmbH
(Peer reviewed)