resolvin-d5 and Sepsis

resolvin-d5 has been researched along with Sepsis* in 1 studies

Other Studies

1 other study(ies) available for resolvin-d5 and Sepsis

Article	Year
Fibrinogen-like protein 2 controls sepsis catabasis by interacting with resolvin Dp5. Science advances, 2019, Volume: 5, Issue:11 The mechanisms that drive programmed resolution of inflammation remain elusive. Here, we report the temporal regulation of soluble (s) and transmembrane (m) fibrinogen-like protein 2 (Fgl2) during inflammation and show that both sFgl2 and mFgl2 correlate with the outcome. The expression and ectodomain shedding of Fgl2 are respectively promoted by miR-466l and metalloproteinases (ADAM10 and ADAM17) during inflammation resolution. Deficiency of Fgl2 enhances polymorphonuclear neutrophil (PMN) infiltration but impairs macrophage (MΦ) maturation and phagocytosis and inhibits the production of n-3 docosapentaenoic acid-derived resolvin 5 (RvDp5). In contrast, administration of sFgl2 blunts PMN infiltration as well as promotes PMN apoptosis and RvDp5 biosynthesis. By activating ALX/FPR2, RvDp5 enhances sFgl2 secretion via ADAM17 and synergistically accelerates resolution of inflammation. These results uncover a previously unknown endogenous programmed mechanism by which Fgl2 regulates resolution of inflammation and shed new light on clinical sepsis treatments. Topics: ADAM10 Protein; ADAM17 Protein; Adult; Animals; Docosahexaenoic Acids; Fibrinogen; Humans; Inflammation; Macrophages; Mice, Inbred C57BL; Mice, Knockout; MicroRNAs; Middle Aged; Neutrophils; Sepsis; Young Adult	2019

Article

Year

Fibrinogen-like protein 2 controls sepsis catabasis by interacting with resolvin Dp5.

Science advances, 2019, Volume: 5, Issue:11

The mechanisms that drive programmed resolution of inflammation remain elusive. Here, we report the temporal regulation of soluble (s) and transmembrane (m) fibrinogen-like protein 2 (Fgl2) during inflammation and show that both sFgl2 and mFgl2 correlate with the outcome. The expression and ectodomain shedding of Fgl2 are respectively promoted by miR-466l and metalloproteinases (ADAM10 and ADAM17) during inflammation resolution. Deficiency of Fgl2 enhances polymorphonuclear neutrophil (PMN) infiltration but impairs macrophage (MΦ) maturation and phagocytosis and inhibits the production of n-3 docosapentaenoic acid-derived resolvin 5 (RvDp5). In contrast, administration of sFgl2 blunts PMN infiltration as well as promotes PMN apoptosis and RvDp5 biosynthesis. By activating ALX/FPR2, RvDp5 enhances sFgl2 secretion via ADAM17 and synergistically accelerates resolution of inflammation. These results uncover a previously unknown endogenous programmed mechanism by which Fgl2 regulates resolution of inflammation and shed new light on clinical sepsis treatments.

Topics: ADAM10 Protein; ADAM17 Protein; Adult; Animals; Docosahexaenoic Acids; Fibrinogen; Humans; Inflammation; Macrophages; Mice, Inbred C57BL; Mice, Knockout; MicroRNAs; Middle Aged; Neutrophils; Sepsis; Young Adult

2019