Nitric oxide production by rat alveolar macrophages can be modulated in vitro by surfactant protein A

Blau, Hannah; Riklis, S.; Iwaarden, J. Freek van; McCormack, F X; Kalina, Moshe

doi:10.1152/ajplung.1997.272.6.l1198

Cited by 47 publications

(44 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Contrary to our current study, others have demonstrated a stimulatory influence of SP-A on AMs (39,40,66). The reasons why SP-A in some studies appears to stimulate AMs (39,40,66) and in others appears to dampen the AM response (36-38) is not clear.…”

Section: Discussioncontrasting

confidence: 99%

See 1 more Smart Citation

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

Section: Discussioncontrasting

confidence: 99%

“…The reasons why SP-A in some studies appears to stimulate AMs (39,40,66) and in others appears to dampen the AM response (36-38) is not clear. There is some evidence that the method of isolation and purification of SP-A may alter SP-A function (39).…”

Section: Discussionmentioning

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

show abstract

“…The most commonly observed alleles are 6A, 6A 2 , and 1A 5 for SP-A2 (10,24). Several studies have shown differences among human SP-A genetic variants expressed in vitro in their abilities to stimulate cytokine production (55,56) to bind carbohydrate (35) and lipids (16) and to enhance phagocytosis by alveolar macrophages (our unpublished observations).…”

mentioning

confidence: 63%

Human SP-A genetic variants and bleomycin-induced cytokine production by THP-1 cells: effect of ozone-induced SP-A oxidation

Huang

Wang

Phelps

et al. 2004

American Journal of Physiology-Lung Cellular and Molecular Phys

View full text Add to dashboard Cite

Surfactant protein A (SP-A) plays a role in innate host defense. Human SP-A is encoded by two functional genes (SP-A1 and SP-A2), and several alleles have been characterized for each gene. We assessed the effect of in vitro expressed human SP-A genetic variants, on TNF-α and IL-8 production by THP-1 cells in the presence of bleomycin, either before or after ozone-induced oxidation of the variants. The oligomerization of SP-A variants was also examined. We found 1) cytokine levels induced by SP-A2 (1A, 1A0) were significantly higher than those by SP-A1 (6A2, 6A4) in the presence of bleomycin. 2) In the presence of bleomycin, ozone-induced oxidation significantly decreased the ability of 1A and 1A/6A4, but not of 6A4, to stimulate TNF-α production. 3) The synergistic effect of bleomycin/SP-A, either before or after oxidation, can be inhibited to the level of bleomycin alone by surfactant lipids. 4) Differences in oligomerization were also observed between SP-A1 and SP-A2. The results indicate that differences among SP-A variants may partly explain the individual variability of pulmonary complications observed during bleomycin chemotherapy and/or in an environment that may promote protein oxidation.

show abstract

“…Surfactant protein A (SP-A), a 34-to 36-kDa glycoprotein, plays a major role in the modulation of innate host defense in the lung (7,16,21,41,48,52). SP-A has been shown to stimulate chemotaxis of macrophages (70), enhance phagocytosis (11,34,44,46,47,50,63), induce generation of reactive oxidants (61), regulate the nitric oxide production (1,23), and influence the proliferation of immune cells (2,38) and the production of proinflammatory cytokines (3,27,37,39,68,69). SP-A can bind to receptors on the macrophage membrane (35).…”

mentioning

confidence: 99%

SP-A1 and SP-A2 variants differentially enhance association ofPseudomonas aeruginosawith rat alveolar macrophages

Mikerov¹,

Umstead²,

Huang³

et al. 2005

American Journal of Physiology-Lung Cellular and Molecular Phys

125

View full text Add to dashboard Cite

aeruginosa. Two genes, SP-A1 and SP-A2, encode human SP-A. We hypothesized that genetically determined differences in the activity of SP-A1 and SP-A2 gene products exist. To test this, we studied association of a nonmucoid P. aeruginosa strain (ATCC 39018) with rat alveolar macrophages in the presence or absence of insect cellexpressed human SP-A variants. We used two trios, each consisting of SP-A1, SP-A2, and their coexpressed SP-A1/SP-A2 variants. We tested the 6A 2 and 6A 4 alleles (for SP-A1), the 1A 0 and 1A alleles (for SP-A2), and their respective coexpressed SP-A1/SP-A2 gene products. After incubation of alveolar macrophages with P. aeruginosa in the presence of the SP-A variants at 37°C for 1 h, the cell association of bacteria was assessed by light microscopy analysis. We found 1) depending on SP-A concentration and variant, SP-A2 variants significantly increased the cell association more than the SP-A1 variants (the phagocytic index for SP-A1 was ϳ52-95% of the SP-A2 activity); 2) coexpressed variants at certain concentrations were more active than single gene products; and 3) the phagocytic index for SP-A variants was ϳ18 -41% of the human SP-A from bronchoalveolar lavage. We conclude that human SP-A variants in vitro enhance association of P. aeruginosa with rat alveolar macrophages differentially and in a concentration-dependent manner, with SP-A2 variants having a higher activity compared with SP-A1 variants.

show abstract

Nitric oxide production by rat alveolar macrophages can be modulated in vitro by surfactant protein A

Cited by 47 publications

References 24 publications

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

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

Human SP-A genetic variants and bleomycin-induced cytokine production by THP-1 cells: effect of ozone-induced SP-A oxidation

SP-A1 and SP-A2 variants differentially enhance association ofPseudomonas aeruginosawith rat alveolar macrophages

Contact Info

Product

Resources

About