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
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.