Lung surfactant and reactive oxygen-nitrogen species: antimicrobial activity and host-pathogen interactions

Citation
Jm. Hickman-davis et al., Lung surfactant and reactive oxygen-nitrogen species: antimicrobial activity and host-pathogen interactions, AM J P-LUNG, 281(3), 2001, pp. L517-L523
Citations number
54
Categorie Soggetti
da verificare
Journal title
AMERICAN JOURNAL OF PHYSIOLOGY-LUNG CELLULAR AND MOLECULAR PHYSIOLOGY
ISSN journal
10400605 → ACNP
Volume
281
Issue
3
Year of publication
2001
Pages
L517 - L523
Database
ISI
SICI code
1040-0605(200109)281:3<L517:LSAROS>2.0.ZU;2-C
Abstract
Surfactant protein (SP) A and SP-D are members of the collectin superfamily . They are widely distributed within the lung, are capable of antigen recog nition, and can discern self versus nonself. SPs recognize bacteria, fungi, and viruses by binding mannose and N-acetylglucosamine residues on microbi al cell walls. SP-A has been shown to stimulate the respiratory burst as we ll as nitric oxide synthase expression by alveolar macrophages. Although ni tric oxide (NO .) is a well-recognized microbicidal product of macrophages, the mechanism(s) by which NO . contributes to host defense remains undefin ed. The purpose of this symposium was to present current research pertainin g to the specific role of SPs and reactive oxygen-nitrogen species in innat e immunity. The symposium focused on the mechanisms of NO-mediated toxicity for bacterial, human, and animal models of SP-A- and NO-mediated pathogen killing, microbial defense mechanisms against reactive oxygen-nitrogen spec ies, specific examples and signaling pathways involved in the SP-A-mediated killing of pulmonary pathogens, the structure and binding of SP-A and SP-D to bacterial targets, and the immunoregulatory functions of SP-A.