Modulation of Interleukin-15-Induced Human Neutrophil Responses by the Plant Lectin Viscum album Agglutinin-I
| Autor: | Denis Girard, Martin Pelletier, Claude Ratthé, Anik Savoie, Valérie Lavastre, Katarina Hostanska, Reinhard Saller |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Neutrophils
Phagocytosis Immunology Ribosome Inactivating Proteins Apoptosis Granulocyte Biology Adjuvants Immunologic medicine Viscum album Humans Immunology and Allergy Phosphorylation Fragmentation (cell biology) Gelsolin Plant Proteins Toxins Biological Interleukin-15 Dose-Response Relationship Drug biology.organism_classification Cell biology Ribosome Inactivating Proteins Type 2 medicine.anatomical_structure Biochemistry Interleukin 15 Protein Biosynthesis Interleukin-2 Plant Preparations |
| Zdroj: | Clinical Immunology. 101:229-236 |
| ISSN: | 1521-6616 |
| Popis: | The plant lectin Viscum album agglutinin-I (VAA-I) and the interleukin-15 (IL-15) cytokine are two molecules with potential therapeutic properties known to modulate neutrophil functions when used separately. This study was conducted in order to better understand the mode of action of VAA-I and to elucidate how VAA-I could modulate IL-15-induced neutrophil responses. We found that VAA-I cannot induce phosphorylation events in human neutrophils. However, it enhances phagocytosis by itself without altering IL-15-induced phagocytosis. VAA-I was found to reverse the ability of IL-15 to delay neutrophil apoptosis and this was correlated with an inhibition of IL-15-induced de novo protein synthesis. In addition, we also found that IL-15 cannot reverse or attenuate the caspase-induced gelsolin fragmentation observed during apoptosis as assessed by immunoblotting. We conclude that VAA-I can be used to modulate some, but not all, IL-15-induced neutrophil responses and that it acts independent of phosphorylation events. |
| Databáze: | OpenAIRE |
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