Effect of canine surfactant protein (SP‐A) on the respiratory burst of phagocytic cells

Weber, Hans; Heilmann, P.; Meyer, Barbara J; Maier, Konrad

doi:10.1016/0014-5793(90)81241-f

Cited by 38 publications

(21 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Katsura et al (13) demonstrated a dose-dependent inhibition by SP-A of rat AM superoxide production in response to both PMA and zymosan, and Weber et al (14) showed that SP-A inhibited the respiratory burst in canine AM by 50% in response to the chemical stimulus PMA. In contrast, van Iwaarden et al (11) reported that human SP-A treatment of rat AM increased the oxidative response to opsonized Staphylococcus aureus.…”

Section: Discussionmentioning

confidence: 99%

“…SP-A itself has been shown to induce superoxide production in rat alveolar macrophages (11), and to either increase (11,12) or decrease ROI production in response to agonists in rat and canine alveolar macrophages (13,14). Thus, while the data are not easily reconciled, they do suggest a role for SP-A in regulating the macrophage oxidative burst.…”

Section: T He Alveolar Macrophage (Am)mentioning

confidence: 99%

See 1 more Smart Citation

Pulmonary Surfactant Protein A Inhibits Macrophage Reactive Oxygen Intermediate Production in Response to Stimuli by Reducing NADPH Oxidase Activity

Crowther

Kutala²,

Kuppusamy³

et al. 2004

The Journal of Immunology

View full text Add to dashboard Cite

Alveolar macrophages are important host defense cells in the human lung that continuously phagocytose environmental and infectious particles that invade the alveolar space. Alveolar macrophages are prototypical alternatively activated macrophages, with up-regulated innate immune receptor expression, down-regulated costimulatory molecule expression, and limited production of reactive oxygen intermediates (ROI) in response to stimuli. Surfactant protein A (SP-A) is an abundant protein in pulmonary surfactant that has been shown to alter several macrophage (Mφ) immune functions. Data regarding SP-A effects on ROI production are contradictory, and lacking with regard to human Mφ. In this study, we examined the effects of SP-A on the oxidative response of human Mφ to particulate and soluble stimuli using fluorescent and biochemical assays, as well as electron paramagnetic resonance spectroscopy. SP-A significantly reduced Mφ superoxide production in response to the phorbol ester PMA and to serum-opsonized zymosan (OpZy), independent of any effect by SP-A on zymosan phagocytosis. SP-A was not found to scavenge superoxide. We measured Mφ oxygen consumption in response to stimuli using a new oxygen-sensitive electron paramagnetic resonance probe to determine the effects of SP-A on NADPH oxidase activity. SP-A significantly decreased Mφ oxygen consumption in response to PMA and OpZy. Additionally, SP-A reduced the association of NADPH oxidase component p47phox with OpZy phagosomes as determined by confocal microscopy, suggesting that SP-A inhibits NADPH oxidase activity by altering oxidase assembly on phagosomal membranes. These data support an anti-inflammatory role for SP-A in pulmonary homeostasis by inhibiting Mφ production of ROI through a reduction in NADPH oxidase activity.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: T He Alveolar Macrophage (Am)mentioning

confidence: 99%

Pulmonary Surfactant Protein A Inhibits Macrophage Reactive Oxygen Intermediate Production in Response to Stimuli by Reducing NADPH Oxidase Activity

Crowther

Kutala²,

Kuppusamy³

et al. 2004

The Journal of Immunology

View full text Add to dashboard Cite

show abstract

“…In vitro, SP-A directly stimulates lucigenin-dependent chemiluminescence (12) and produces a dosedependent enhancement of oxygen radical release from rat alveolar macrophages (29). In contrast, stimulated canine alveolar macrophages produce less superoxide anions in the presence of SP-A (30).…”

Section: Introductionmentioning

confidence: 99%

Surfactant protein-A enhances respiratory syncytial virus clearance in vivo

LeVine¹,

Gwozdz²,

Stark³

et al. 1999

J. Clin. Invest.

264

184

View full text Add to dashboard Cite

To determine the role of surfactant protein-A(SP-A) in antiviral host defense, mice lacking SP-A (SP-A -/-) were produced by targeted gene inactivation. SP-A -/-and control mice (SP-A +/+ ) were infected with respiratory syncytial virus (RSV) by intratracheal instillation. Pulmonary infiltration after infection was more severe in SP-A -/-than in SP-A +/+ mice and was associated with increased RSV plaque-forming units in lung homogenates. Pulmonary infiltration with polymorphonuclear leukocytes was greater in the SP-A -/-mice. Levels of proinflammatory cytokines tumor necrosis factor-α and interleukin-6 were enhanced in lungs of SP-A -/-mice. After RSV infection, superoxide and hydrogen peroxide generation was deficient in macrophages from SP-A -/-mice, demonstrating a critical role of SP-A in oxidant production associated with RSV infection. Coadministration of RSV with exogenous SP-A reduced viral titers and inflammatory cells in the lung of SP-A -/-mice. These findings demonstrate that SP-A plays an important host defense role against RSV in vivo.

show abstract

“…It is also thought that SP-A plays an important role in the modulation of the inflammatory and immunological response (35). Recent studies suggest that SP-A alters oxygen radical production (36,37) and blocks the costimulatory signals crucial for in vitro T-lymphocyte cell activation (38). AMs incubated with SP-A have a decrease in superoxide production, indicating a dampening of the respiratory burst (36,38) and suggesting that SP-A has a protective role against the oxidant injury caused by AMs in the lung.…”

mentioning

confidence: 99%

Surfactant protein A suppresses reactive nitrogen intermediates by alveolar macrophages in response to Mycobacterium tuberculosis

Pasula¹,

Wright²,

Kachel³

et al. 1999

J. Clin. Invest.

View full text Add to dashboard Cite

Mycobacterium tuberculosis attaches to, enters, and replicates within alveolar macrophages (AMs). Our previous studies suggest that surfactant protein A (SP-A) can act as a ligand in the attachment of M. tuberculosis to AMs. Reactive nitrogen intermediates (RNIs) play a significant role in the killing of mycobacteria. We have demonstrated that RNI levels generated by AMs were significantly increased when interferon-γ-primed AMs were incubated with M. tuberculosis. However, the RNI levels were significantly suppressed in the presence of SP-A (10 µg/ml). The specificity of SP-A's effect was demonstrated by the use of F(ab′) 2 fragments of anti-SP-A monoclonal antibodies and by the use of mannosyl-BSA, which blocked the suppression of RNI levels by SP-A. Furthermore, incubation of deglycosylated SP-A with M. tuberculosis failed to suppress RNI by AMs, suggesting that the oligosaccharide component of SP-A, which binds to M. tuberculosis, is necessary for this effect. These results show that SP-A-mediated binding of M. tuberculosis to AMs significantly decreased RNI levels, suggesting that this may be one mechanism by which M. tuberculosis diminishes the cytotoxic response of activated AMs.

show abstract

Effect of canine surfactant protein (SP‐A) on the respiratory burst of phagocytic cells

Cited by 38 publications

References 27 publications

Pulmonary Surfactant Protein A Inhibits Macrophage Reactive Oxygen Intermediate Production in Response to Stimuli by Reducing NADPH Oxidase Activity

Pulmonary Surfactant Protein A Inhibits Macrophage Reactive Oxygen Intermediate Production in Response to Stimuli by Reducing NADPH Oxidase Activity

Surfactant protein-A enhances respiratory syncytial virus clearance in vivo

Surfactant protein A suppresses reactive nitrogen intermediates by alveolar macrophages in response to Mycobacterium tuberculosis

Contact Info

Product

Resources

About