Activation of human monocyte chemiluminescence response by acylpoly(1,3)galactosides derived from Klebsiella pneumoniae
| Autor: | Z. Hmama, F Faure-Barba, H Binz, E Kouassi, Gerard Normier, Gerard Lina, Jean-Pierre Revillard, J. Vial |
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| Rok vydání: | 1992 |
| Předmět: |
Lipopolysaccharides
Lipopolysaccharide Immunology Molecular Sequence Data Macrophage-1 Antigen Polymyxin B Sulfate In Vitro Techniques Monocytes Lipid A chemistry.chemical_compound medicine Immunology and Allergy Humans Magnesium Polymyxin B Respiratory Burst biology Molecular Structure Monocyte Zymosan Polysaccharides Bacterial Galactosides Cell Biology Galactoside Respiratory burst Klebsiella pneumoniae medicine.anatomical_structure Integrin alpha M chemistry Biochemistry Carbohydrate Sequence Luminescent Measurements biology.protein Calcium Proteoglycans |
| Zdroj: | Scopus-Elsevier |
| ISSN: | 0741-5400 |
| Popis: | The stimulating activity of several preparations isolated from a membrane proteoglycan of a nonen- capsulated smooth strain of Klebsiella pneumoniae (Kp- MPG) on the oxidative burst of human blood monocytes was assessed by luminol-enhanced chemiluminescence (CL). Five Kp derivatives were studied: a 34-kd acyl- poly(l,3)galactoside (APG), obtained by drastic alkaline hydrolysis and purified by chromatography; an APG preparation subjected to acid hydrolysis that removed the core part and all fatty acids, leaving intact the galactose chain of APG (GC-APG); an APG preparation subjected to mild oxidation (ox APG); a preparation obtained by mild alkaline hydrolysis of Kp-MPG, containing additional ester-linked C14 and C16 fatty acids bound to the APG molecule (EFA-APG); and a polymer of the latter compound, APG pol. EFA-APG directly stimulated monocyte CL, whereas Kp-MPG, APG pol, and the whole bacterial cells had little or no activity. APG itself and ox APG induced a weaker response than EFA-APG. Polymyxin B sulfate completely inhibited the CL response to bacterial lipopolysaccharide (LPS) but not to EFA-APG. The stimulating action of EFA-APG on blood monocytes was dependent on the extracellular levels of both calcium and magnesium. Preincubation of monocytes with monoclonal antibody anti-Mac-1 directed against CDllb, the αchain of complement receptor type 3 (CR3; CDllb/CD18), strongly inhibited CL activation by EFA-APG and to a lesser extent CL activation by un- opsonized zymosan and rough LPS. Altogether, these findings provide indirect evidence for the contribution of the CDllb/CD18 integrin in the functional interaction of EFA-APG with monocyte membranes. They demonstrate the role of fatty acids in the triggering of monocyte oxidative burst, while the polysaccharide chain itself does not contribute to induction of the CL response in this model. In keeping with the effects of EFA-APG and APG, we show that the monocyte CL response was triggered by bacterial LPS from the rough strain of Salmonella minnesota Re 595 and its lipid A, but not by LPS from smooth strains, again suggesting a critical role for the lipid moiety. |
| Databáze: | OpenAIRE |
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