These studies demonstrate in vivo and in vitro protective effects of oxidized phospholipids on LPS-induced lung dysfunction.

With the discovery of postnatal stem cells within the brain, it has become important to understand how extracellular factors might affect the maturation of neuronal precursors in the postnatal brain. Neurotrophic factors are known to play a role in neuronal development but display pleiotrophic effects, in part because of their physiological interactions with other factors. One factor positioned to interact with neurotrophins in the brains of postnatal animals is atrial C-type natriuretic peptide (CNP). In this study, we used olfactory receptor neurons (ORNs) as a model, because their precursors demonstrate the most robust and functional postnatal neurogenesis of those systems thus far described. We examined the effects of brain-derived neurotrophic factor (BDNF) and nerve growth factor (NGF) and the interactions of these neurotrophins and CNP in postnatal olfactory neuronal precursors. Results obtained using mice with targeted deletion of the gene for BDNF indicated that BDNF is a neuroproliferation-inducing and survival factor for ORN precursors. These roles were confirmed in vitro using primary cultures of ORNs. NGF was found to be a proliferation-inducing factor but not a survival factor. The addition of CNP to either BDNF- or NGF-treated neuronal precursors resulted in an inhibition of proliferation and the promotion of maturation. These effects were accompanied by changes in cell-cycle proteins that suggest possible mechanisms for these effects. Thus, CNP may function in the postnatal brain to regulate the exit from the cell cycle in neuronal precursor cells.

Keywords: bacterial wall lipopolysaccharide; bronchoalveolar lavage; interleukin 6; interleukin 1␤; lung endothelial permeability Tissue inflammation and increased vascular leak are cardinal features of acute lung injury (ALI), a severe illness associated with a mortality of 30 to 50% (1). Despite recent advances in low tidal volume mechanical ventilation and a better understanding of the underlying inflammatory pathophysiology of ALI,

It has been known that factor XIa (XIa) can react covalently with antithrombin III (ATIII) to form two complexes with ratios of 2ATIII:1XIa and 1ATIII:1XIa. In the hands of these investigators, the M.W.s, as measured by SDS-PAGE, were 265 kDa and 225 kDa, respectively. In this investigation it has been observed that the addition of 1 µg or 5 µg heparin (H) to 3.1 ϫ 10-5 (mol ATIII for 5 minutes prior to the addition of 1.125 µ 10-5 µmol XIa for a 30-minute incubation led to an increase in the 265 kDa band of 113% and 223%, respectively. These results were statistically significant (p < .01). However, when H was premixed with XIa first, before the addition of AT III, statistical increases in the 265 kDa band were also seen (267% and 183%, respectively; p < .0005, n = 6). Protamine sulfate (PS) statistically significantly (p < .05) inhibited the formation of the 265 and 225 kDa XIa-ATIII complexes at the 5 µg PS level when premixed with ATIII or XIa, respectively, the decreases in the 265 kDa band being 39.1 and 34.4%, respectively for [(ATIII/PS) + XIA] and [(XIa/PS) + ATIII] mixtures, and 23.1 and 23.8% for the 225 kDa band with [(ATIII/PS) + XIa] and [(XIa/PS) + ATIII] mixtures. These results with PS indicate that PS inhibits complex formation between XIa and ATIII at the 2ATIII:1 XIa and 1ATIII:1 XIa levels, in contrast with its reported stimulation of complex formation between thrombin and ATIII.