Surfactant Protein A Modulates Cell Surface Expression of CR3 on Alveolar Macrophages and Enhances CR3-mediated Phagocytosis

Gil, Malgorzata A; McCormack, Francis X.; LeVine, Ann Marie

doi:10.1074/jbc.m808643200

Cited by 41 publications

(27 citation statements)

References 40 publications

(33 reference statements)

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“…A number of SP-A-binding proteins and receptors have been recognized (reviewed in Chroneos et al, 2010); however, their functions and expression by cell type remain unexplored (Strayer et al, 1993;Stevens et al, 1995;Wissel et al, 1996;Gil et al, 2009). The binding of SP-A to the TLR4 protein has also been shown to occur under in vitro condition (Yamada et al, 2006); however, the in vivo evidence had been lacking and functional relevance remained largely unexplored.…”

Section: Discussionmentioning

confidence: 99%

A Toll-Like Receptor-4-Interacting Surfactant Protein-A-Derived Peptide Suppresses Tumor Necrosis Factor-α Release from Mouse JAWS II Dendritic Cells

Awasthi¹,

Brown²,

King³

et al. 2010

J Pharmacol Exp Ther

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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-␣ (TNF-␣) 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-␣ production against LPS. However, two of these peptides (SPA4: GDFRYSDGTPVNYTNWYRGE and SPA5: YVGLTEGPSPGDFRYSDFTP) decreased the TNF-␣ 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-␣ in JAWS II dendritic cells.

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Section: Discussionmentioning

confidence: 99%

A Toll-Like Receptor-4-Interacting Surfactant Protein-A-Derived Peptide Suppresses Tumor Necrosis Factor-α Release from Mouse JAWS II Dendritic Cells

Awasthi¹,

Brown²,

King³

et al. 2010

J Pharmacol Exp Ther

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“…Phospholipid vesicles containing dipalmitoyl phosphatidyl choline, the major phospholipid in pulmonary surfactant, induced expression of several macrophage innate immune receptors [162], a property that has also been noted for purified SP-A and SP-D [163][164][165][166][167][168]. In these cases, SP-D influences alveolar macrophage differentiation as indicated by expression of CD11c [169][170][171], while surfactant DPPC and SP-A induced expression and function of several innate immune receptors that so far include the complement receptor CR3 (CD11b), the scavenger receptors SR-A, CD36, and LOX-1, the mannose receptor, toll-like receptors, Fc receptors and the complement receptor CR1 [157,164,169,170]. Adoptive transfer experiments and studies in SP-D-inducible transgenic mice indicate that SP-D contributes to the local differentiation of freshly recruited monocytes in the alveolar space [169][170][171].…”

Section: Sp-b Sp-c and Surfactant Lipidsmentioning

confidence: 99%

Pulmonary Surfactant: An Immunological Perspective

Chroneos

Sever-Chroneos

Shepherd

2010

Cell Physiol Biochem

164

115

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“…It also can stimulate the expression of the other receptors involved in immunity response like complement receptor 3 and scavenger receptor [103,104]. Moreover, they can modulate the inflammatory response by regulating the cytokine production, the oxygen and nitrogen reactive species formation and functioning as chemo attractants for alveolar neutrophils and monocytes [105].…”

Section: Collectin Familymentioning

confidence: 99%

Macrophage Infection by Mycobacteria

Saleh¹

2016

Mycobact Dis

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Mycobacterium tuberculosis is the etiological agent of tuberculosis. It is a pathogen that continues to draw international concerns particularly due to the emergence of multi-drug resistance and to the difficulties associated with the diagnosis and treatment of latent tuberculosis. A key process in the pathogenesis of this disease is the interaction between this pathogen and host macrophages. Invasion of the macrophages protects the pathogen from attack by the immune system, allows it to multiply while protected within the macrophages, and alters the immune response as it influences the profiles of the cytokine and chemokine responses. Key to the intracellular survival of the pathogen within the macrophages is the specific interaction between the pathogen and its virulence factors with the host. This review provides an a summary of pertinent literature on the topic of macrophage receptors utilized by the pathogen, its survival strategies within the macrophage, and the general profile of immune signalling upon exposure to the pathogen. The importance of specific macrophage receptors and certain components of the pathogen to the direction of the immune response are also discussed.

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Surfactant Protein A Modulates Cell Surface Expression of CR3 on Alveolar Macrophages and Enhances CR3-mediated Phagocytosis

Abstract: Pulmonary surfactant protein A (SP-A

Cited by 41 publications

References 40 publications

A Toll-Like Receptor-4-Interacting Surfactant Protein-A-Derived Peptide Suppresses Tumor Necrosis Factor-α Release from Mouse JAWS II Dendritic Cells

A Toll-Like Receptor-4-Interacting Surfactant Protein-A-Derived Peptide Suppresses Tumor Necrosis Factor-α Release from Mouse JAWS II Dendritic Cells

Pulmonary Surfactant: An Immunological Perspective

Macrophage Infection by Mycobacteria

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