Skip Navigation
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.


The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Your Environment. Your Health.

Publication Detail

Title: S-nitrosylation of surfactant protein D as a modulator of pulmonary inflammation.

Authors: Atochina-Vasserman, Elena N

Published In Biochim Biophys Acta, (2012 Jun)

Abstract: Surfactant protein D (SP-D) is a member of the family of proteins termed collagen-like lectins or "collectins" that play a role in non-antibody-mediated innate immune responses [1]. The primary function of SP-D is the modulation of host defense and inflammation [2].This review will discuss recent findings on the physiological importance of SP-D S-nitrosylation in biological systems and potential mechanisms that govern SP-D mediated signaling.SP-D appears to have both pro- and anti-inflammatory signaling functions. SP-D multimerization is a critical feature of its function and plays an important role in efficient innate host defense. Under baseline conditions, SP-D forms a multimer in which the N-termini are hidden in the center and the C-termini are on the surface. This multimeric form of SP-D is limited in its ability to activate inflammation. However, NO can modify key cysteine residues in the hydrophobic tail domain of SP-D resulting in a dissociation of SP-D multimers into trimers, exposing the S-nitrosylated N-termini. The exposed S-nitrosylated tail domain binds to the calreticulin/CD91 receptor complex and initiates a pro-inflammatory response through phosphorylation of p38 and NF-κB activation [3,4]. In addition, the disassembled SP-D loses its ability to block TLR4, which also results in activation of NF-κB.Recent studies have highlighted the capability of NO to modify SP-D through S-nitrosylation, causing the activation of a pro-inflammatory role for SP-D [3]. This represents a novel mechanism both for the regulation of SP-D function and NO's role in innate immunity, but also demonstrates that the S-nitrosylation can control protein function by regulating quaternary structure. This article is part of a Special Issue entitled Regulation of Cellular Processes by S-nitrosylation.

PubMed ID: 22183030 Exiting the NIEHS site

MeSH Terms: Animals; Calreticulin/metabolism; Gene Expression Regulation; Humans; Immunity, Innate; Inflammation/metabolism*; Low Density Lipoprotein Receptor-Related Protein-1/metabolism; Macrophages/immunology; Macrophages/physiology; Mice; NF-kappa B/metabolism; Nitric Oxide/metabolism*; Nitrosation; Phosphorylation; Pneumonia/immunology; Pneumonia/metabolism*; Protein Structure, Quaternary; Protein Structure, Tertiary; Pulmonary Surfactant-Associated Protein D/chemistry; Pulmonary Surfactant-Associated Protein D/metabolism*; Rats; Signal Transduction; Toll-Like Receptor 4/metabolism; p38 Mitogen-Activated Protein Kinases/metabolism

to Top