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Bacterial Lipopolysaccharide Enhances Chemoattractant‐Induced Elastase Secretion by Human Neutrophils
Author(s) -
Fittschen C.,
Sandhaus R.A.,
Worthen G.S.,
Henson P.M.
Publication year - 1988
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.43.6.547
Subject(s) - elastase , lipopolysaccharide , chemotaxis , secretion , myeloperoxidase , leukotriene b4 , biology , neutrophil elastase , platelet activating factor , pancreatic elastase , lipid a , immunology , biochemistry , inflammation , enzyme , receptor
Bacterial lipopolysaccharide (LPS) has previously been shown to enhance a number of chemoattractant‐induced responses by human neutrophils. The possible role of elastase, a neutral protease with broad substrate specificity, in neutrophil‐mediated vascular injury of a variety of diseases prompted us to examine a) whether or not LPS enhances the direct chemoattractant‐induced secretion of elastase, b) the quantitative requirements of LPS and chemotactic factors, and c) some structural requirements of LPS for this effect. Our results show that LPS at 10 ng/ml and above, enhanced formyl‐methionyl‐leucyl‐phenylalanine‐induced neutrophil secretion of elastase, as well as secretion of myeloperoxidase and vitamin B 12 ‐binding protein. This effect was independent of cytochalasins or surface stimulation, and thus may occur during chemotactic factor stimulation in vivo. LPS also enhanced neutrophil secretory responses to the complement fragments C5a, C5a des arg, and, to a lesser degree, to leukotriene B 4 and platelet‐activating factor. This enhancement effect appeared to require the presence of the lipid A moiety and/or parts of the core polysaccharide but not the O‐antigen portion of the LPS molecule. Our findings identify a possible LPS‐dependent mechanism of neutrophil elastase‐mediated tissue injury in Gram‐negative infections.