s-nitrosylation of surfactant protein-d controls inflammatory function表面活性剂s-nitrosylation protein-d控制炎症功能.pdfVIP

PLoS BIOLOGY S-Nitrosylation of Surfactant Protein-D Controls Inflammatory Function 1 2 2 3 3 4 Chang-Jiang Guo , Elena N. Atochina-Vasserman , Elena Abramova , Joseph P. Foley , Aisha Zaman , Erika Crouch , Michael F. Beers2, Rashmin C. Savani3,5, Andrew J. Gow1* 1 Department of Pharmacology and Toxicology, Ernest Mario School of Pharmacy, Rutgers, The State University of New Jersey, Piscataway, New Jersey, United States of America, 2 Division of Pulmonary and Critical Care Medicine, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania, United States of America, 3 Division of Neonatology, Department of Pediatrics, Joseph Stokes Jr. Research Institute of The Children’s Hospital of Philadelphia, Philadelphia, Pennsylvania, United States of America, 4 Department of Pathology and Immunology, Washington University, St. Louis, Missouri, United States of America, 5 Division of Neonatal-Perinatal Medicine, Division of Pulmonary and Vascular Biology, University of Texas Southwestern at Dallas, Dallas, Texas, United States of America The pulmonary collectins, surfactant proteins A and D (SP-A and SP-D) have been implicated in the regulation of the innate immune system within the lung. In particular, SP-D appears to have both pro- and anti-inflammatory signaling functions. At present, the molecular mechanisms involved in switching between these functions remain unclear. SP-D differs in its quaternary structure from SP-A and the other members of the collectin family, such as C1q, in that it forms large multimers held together by the N-terminal domain, rather than aligning the triple helix domains in the traditional ‘‘bunch o