ArticleThe Journal of pharmacology and experimental therapeutics2011
A toll-like receptor-4-interacting surfactant protein-A-derived peptide suppresses tumor necrosis factor-α release from mouse JAWS II dendritic cells.
Article in The Journal of pharmacology and experimental therapeutics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 27 citations in OpenAlex.
- The implication of dendritic cells in lung diseases: Immunological role of toll-like receptor 4.Genes & diseases · 2024Review
- Stability and structure-activity relationship of the SPA4 peptide under ambient and stressed conditions of lung injury.RSC advances · 2023Article
- Effects of SPA4 peptide on lipopolysaccharide-disrupted lung epithelial barrier, injury, and function in a human cell system and mouse model of lung injury.Physiological reports · 2022Article
- Antimicrobial peptides could antagonize uncontrolled inflammationFrontiers in bioengineering and biotechnology · 2022Review
- The Role of Toll-like Receptors (TLRs) Mediated Inflammation in Pancreatic Cancer Pathophysiology.International journal of molecular sciences · 2021Review
- Mechanism of Anti-Inflammatory Activity of TLR4-Interacting SPA4 Peptide.ImmunoHorizons · 2021Article
- A cutting-edge immunoinformatics approach for design of multi-epitope oral vaccine against dreadful human malaria.International journal of biological macromolecules · 2020Article
- A 20-Mer Peptide Derived from the Lectin Domain ofInfection and immunity · 2020Article
- Lung and general health effects of Toll-like receptor-4 (TLR4)-interacting SPA4 peptide.BMC pulmonary medicine · 2020Article
- Article
- Structure, genetics and function of the pulmonary associated surfactant proteins A and D: The extra-pulmonary role of these C type lectins.Annals of anatomy = Anatomischer Anzeiger : official organ of the Anatomische Gesellschaft · 2017Review
- Toll-like receptor 4-interacting SPA4 peptide suppresses the NLRP3 inflammasome in response to LPS and ATP stimuli.Journal of leukocyte biology · 2015Article
- Pulmonary surfactant protein a is expressed in mouse retina by Müller cells and impacts neovascularization in oxygen-induced retinopathy.Investigative ophthalmology & visual science · 2014Article
- Toll-like receptor-4 modulation for cancer immunotherapy.Frontiers in immunology · 2014Review
- Preclinical evaluation of 4-[3,5-bis(2-chlorobenzylidene)-4-oxo-piperidine-1-yl]-4-oxo-2-butenoic acid, in a mouse model of lung cancer xenograft.British journal of pharmacology · 2013Article
- Host-Viral Interactions: Role of Pattern Recognition Receptors (PRRs) in Human Pneumovirus Infections.Pathogens (Basel, Switzerland) · 2013Article
- Role of innate immunity in neonatal infection.American journal of perinatology · 2013Review
- Defensin DEFB103 bidirectionally regulates chemokine and cytokine responses to a pro-inflammatory stimulus.Scientific reports · 2013Article
- A TLR4-interacting peptide inhibits lipopolysaccharide-stimulated inflammatory responses, migration and invasion of colon cancer SW480 cells.Oncoimmunology · 2012Article
- Surfactant protein-A and toll-like receptor-4 modulate immune functions of preterm baboon lung dendritic cell precursor cells.Cellular immunology · 2011Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Surfactant protein-A (SP-A) and Toll-like receptor-4 (TLR4) proteins are recognized as pathogen-recognition receptors. An exaggerated activation of TLR4 induces inflammatory response, whereas SP-A protein down-regulates inflammation. We hypothesized that SP-A-TLR4 interaction may lead to inhibition of inflammation. In this study, we investigated interaction between native baboon lung SP-A and baboon and human TLR4-MD2 proteins by coimmunoprecipitation/immunoblotting and microwell-based methods. The interaction between SP-A and TLR4-MD2 proteins was then analyzed using a bioinformatics approach. In the in silico model of SP-A-TLR4-MD2 complex, we identified potential binding regions and amino acids at the interface of SP-A-TLR4. Using this information, we synthesized a library of human SP-A-derived peptides that contained interacting amino acids. Next, we tested whether the TLR4-interacting SP-A peptides would suppress inflammatory cytokines. The peptides were screened for any changes in the tumor necrosis factor-α (TNF-α) response against lipopolysaccharide (LPS) stimuli in the mouse JAWS II dendritic cell line. Different approaches used in this study suggested binding between SP-A and TLR4-MD2 proteins. In cells pretreated with peptides, three of seven peptides increased TNF-α production against LPS. However, two of these peptides (SPA4: GDFRYSDGTPVNYTNWYRGE and SPA5: YVGLTEGPSPGDFRYSDFTP) decreased the TNF-α production in LPS-challenged JAWS II dendritic cells; SPA4 peptide showed more pronounced inhibitory effect than SPA5 peptide. In conclusion, we identify a human SP-A-derived peptide (SPA4 peptide) that interacts with TLR4-MD2 protein and inhibits the LPS-stimulated release of TNF-α in JAWS II dendritic cells.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.