Erythroid DAMPs drive inflammation in SCD.

In this issue of Blood , Chen et al show that heme is released during erythrocyte hemolysis in sickle cell disease, activating the innate immune response and triggering the release of neutrophil extracellular traps (NETs) to promote lung injury.[1][1] ![Figure][2] Hemolysis releases

[1]  D. Wagner,et al.  Heme-induced neutrophil extracellular traps contribute to the pathogenesis of sickle cell disease. , 2014, Blood.

[2]  A. Schäffer,et al.  Inherited biallelic CSF3R mutations in severe congenital neutropenia. , 2014, Blood.

[3]  M. Gladwin,et al.  An official American Thoracic Society clinical practice guideline: diagnosis, risk stratification, and management of pulmonary hypertension of sickle cell disease. , 2014, American journal of respiratory and critical care medicine.

[4]  M. Gladwin,et al.  Haemoglobinuria is associated with chronic kidney disease and its progression in patients with sickle cell anaemia , 2014, British journal of haematology.

[5]  A. Alayash,et al.  Heme triggers TLR4 signaling leading to endothelial cell activation and vaso-occlusion in murine sickle cell disease. , 2014, Blood.

[6]  M. Gladwin,et al.  An official American Thoracic Society clinical practice guideline: diagnosis, risk stratification, and management of pulmonary hypertension of sickle cell disease. , 2014, American journal of respiratory and critical care medicine.

[7]  S. Ofori-Acquah,et al.  Extracellular hemin crisis triggers acute chest syndrome in sickle mice. , 2013, The Journal of clinical investigation.

[8]  Z. Werb,et al.  Platelets induce neutrophil extracellular traps in transfusion-related acute lung injury. , 2012, The Journal of clinical investigation.

[9]  Tamir Kanias,et al.  Hemolysis and cell-free hemoglobin drive an intrinsic mechanism for human disease. , 2012, The Journal of clinical investigation.

[10]  C. O'Shea,et al.  The WSXWS motif in cytokine receptors is a molecular switch involved in receptor activation: insight from structures of the prolactin receptor. , 2012, Structure.

[11]  D. Link,et al.  A truncation mutant of Csf3r cooperates with PML-RARα to induce acute myeloid leukemia in mice. , 2011, Experimental hematology.

[12]  C. Klein.  Genetic defects in severe congenital neutropenia: emerging insights into life and death of human neutrophil granulocytes. , 2011, Annual review of immunology.

[13]  D. Link,et al.  Prevalence of mutations in ELANE, GFI1, HAX1, SBDS, WAS and G6PC3 in patients with severe congenital neutropenia , 2009, British journal of haematology.

[14]  V. Wahn,et al.  Novel cell death program leads to neutrophil extracellular traps. , 2007, The Journal of cell biology.

[15]  M. Ballmaier,et al.  Incidence of CSF3R mutations in severe congenital neutropenia and relevance for leukemogenesis: Results of a long-term survey. , 2007, Blood.

[16]  F. Martinon,et al.  Gout-associated uric acid crystals activate the NALP3 inflammasome , 2006, Nature.

[17]  Philip S Rosenberg,et al.  The incidence of leukemia and mortality from sepsis in patients with severe congenital neutropenia receiving long-term G-CSF therapy. , 2005, Blood.

[18]  L. Druhan,et al.  Novel mechanism of G-CSF refractoriness in patients with severe congenital neutropenia. , 2005, Blood.

[19]  J. Krishnan,et al.  Pulmonary hypertension as a risk factor for death in patients with sickle cell disease. , 2004, The New England journal of medicine.

[20]  M. Gladwin,et al.  Cell-free hemoglobin limits nitric oxide bioavailability in sickle-cell disease , 2002, Nature Medicine.

[21]  D. Link,et al.  Impaired production and increased apoptosis of neutrophils in granulocyte colony-stimulating factor receptor-deficient mice. , 1996, Immunity.