Abstract
Surfactant-associated protein A (SP-A) is involved in surfactant homeostasis arid host defense in the lung. We have previously demonstrated that SP-A specifically binds to and enhances the ingestion of bacillus Calmette-Guerin (BCG) organisms by macrophages. In the current study, we investigated the effect of SP-A on the generation of inflammatory mediators induced by BCG and the subsequent fate of ingested BCG organisms. Rat macrophages were incubated with BCG in the presence and absence of SP-A. Noningested BCG organisms were removed, and the release of tumor necrosis factor-α (TNF-α) and nitric oxide were measured at varying times. TNF-α and nitric oxide production induced by BCG were enhanced by SP-A. In addition, SP-A enhanced the BCG-induced increase in the level of inducible nitric oxide synthase protein. Addition of antibodies directed against SPR210, a specific macrophage SP-A receptor, inhibited the SP-A-enhanced mediator production. BCG in the absence of SP-A showed increased growth over a 5-day period, whereas inclusion of SP-A dramatically inhibited BCG growth. Inhibition of nitric oxide production blocked BCG killing in the presence and absence of SP-A. These results demonstrate that ingestion of SP-A-BCG complexes by rat macrophages leads to production of inflammatory mediators and increased mycobacterial killing.
| Original language | English (US) |
|---|---|
| Journal | American Journal of Physiology - Lung Cellular and Molecular Physiology |
| Volume | 279 |
| Issue number | 2 23-2 |
| State | Published - Sep 18 2000 |
Fingerprint
All Science Journal Classification (ASJC) codes
- Physiology
- Pulmonary and Respiratory Medicine
- Physiology (medical)
- Cell Biology
Cite this
}
Surfactant protein A enhances mycobacterial killing by rat macrophages through a nitric oxide-dependent pathway. / Weikert, Laura F.; Lopez, Joseph P.; Abdolrasulnia, Rasul; Chroneos, Zissis; Shepherd, Virginia L.
In: American Journal of Physiology - Lung Cellular and Molecular Physiology, Vol. 279, No. 2 23-2, 18.09.2000.Research output: Contribution to journal › Article
TY - JOUR
T1 - Surfactant protein A enhances mycobacterial killing by rat macrophages through a nitric oxide-dependent pathway
AU - Weikert, Laura F.
AU - Lopez, Joseph P.
AU - Abdolrasulnia, Rasul
AU - Chroneos, Zissis
AU - Shepherd, Virginia L.
PY - 2000/9/18
Y1 - 2000/9/18
N2 - Surfactant-associated protein A (SP-A) is involved in surfactant homeostasis arid host defense in the lung. We have previously demonstrated that SP-A specifically binds to and enhances the ingestion of bacillus Calmette-Guerin (BCG) organisms by macrophages. In the current study, we investigated the effect of SP-A on the generation of inflammatory mediators induced by BCG and the subsequent fate of ingested BCG organisms. Rat macrophages were incubated with BCG in the presence and absence of SP-A. Noningested BCG organisms were removed, and the release of tumor necrosis factor-α (TNF-α) and nitric oxide were measured at varying times. TNF-α and nitric oxide production induced by BCG were enhanced by SP-A. In addition, SP-A enhanced the BCG-induced increase in the level of inducible nitric oxide synthase protein. Addition of antibodies directed against SPR210, a specific macrophage SP-A receptor, inhibited the SP-A-enhanced mediator production. BCG in the absence of SP-A showed increased growth over a 5-day period, whereas inclusion of SP-A dramatically inhibited BCG growth. Inhibition of nitric oxide production blocked BCG killing in the presence and absence of SP-A. These results demonstrate that ingestion of SP-A-BCG complexes by rat macrophages leads to production of inflammatory mediators and increased mycobacterial killing.
AB - Surfactant-associated protein A (SP-A) is involved in surfactant homeostasis arid host defense in the lung. We have previously demonstrated that SP-A specifically binds to and enhances the ingestion of bacillus Calmette-Guerin (BCG) organisms by macrophages. In the current study, we investigated the effect of SP-A on the generation of inflammatory mediators induced by BCG and the subsequent fate of ingested BCG organisms. Rat macrophages were incubated with BCG in the presence and absence of SP-A. Noningested BCG organisms were removed, and the release of tumor necrosis factor-α (TNF-α) and nitric oxide were measured at varying times. TNF-α and nitric oxide production induced by BCG were enhanced by SP-A. In addition, SP-A enhanced the BCG-induced increase in the level of inducible nitric oxide synthase protein. Addition of antibodies directed against SPR210, a specific macrophage SP-A receptor, inhibited the SP-A-enhanced mediator production. BCG in the absence of SP-A showed increased growth over a 5-day period, whereas inclusion of SP-A dramatically inhibited BCG growth. Inhibition of nitric oxide production blocked BCG killing in the presence and absence of SP-A. These results demonstrate that ingestion of SP-A-BCG complexes by rat macrophages leads to production of inflammatory mediators and increased mycobacterial killing.
UR - http://www.scopus.com/inward/record.url?scp=0033843747&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0033843747&partnerID=8YFLogxK
M3 - Article
C2 - 10926544
AN - SCOPUS:0033843747
VL - 279
JO - American Journal of Physiology
JF - American Journal of Physiology
SN - 1040-0605
IS - 2 23-2
ER -