Surfactant protein A is defective in abrogating inflammation in asthma.
Surfactant protein A (SP-A) regulates a variety of immune cell functions. We determined the ability of SP-A derived from normal and asthmatic subjects to modulate the inflammatory response elicited by Mycoplasma pneumoniae, a pathogen known to exacerbate asthma. Fourteen asthmatic and 10 normal control subjects underwent bronchoscopy with airway brushing and bronchoalveolar lavage (BAL). Total SP-A was extracted from BAL. The ratio of SP-A1 to total SP-A (SP-A1/SP-A) and the binding of total SP-A to M. pneumoniae membranes were determined. Airway epithelial cells from subjects were exposed to either normal or asthmatic SP-A before exposure to M. pneumoniae. IL-8 protein and MUC5AC mRNA were measured. Total BAL SP-A concentration did not differ between groups, but the percentage SP-A1 was significantly increased in BAL of asthmatic compared with normal subjects. SP-A1/SP-A significantly correlated with maximum binding of total SP-A to M. pneumoniae, but only in asthma. SP-A derived from asthmatic subjects did not significantly attenuate IL-8 and MUC5AC in the setting of M. pneumoniae infection compared with SP-A derived from normal subjects. We conclude that SP-A derived from asthmatic subjects does not abrogate inflammation effectively, and this dysfunction may be modulated by SP-A1/SP-A.
Duke Scholars
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- Transfection
- Respiratory System
- Recombinant Proteins
- RNA, Messenger
- Pulmonary Surfactant-Associated Protein A
- Protein Binding
- Polymerase Chain Reaction
- Plasmids
- Mycoplasma pneumoniae
- Mucin 5AC
Citation
Published In
DOI
EISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Transfection
- Respiratory System
- Recombinant Proteins
- RNA, Messenger
- Pulmonary Surfactant-Associated Protein A
- Protein Binding
- Polymerase Chain Reaction
- Plasmids
- Mycoplasma pneumoniae
- Mucin 5AC