Poster (Scientific congresses and symposiums)
A water-soluble salt of curcumin (NDS27) inhibits myeloperoxidase and NADPH oxidase activities, two major enzymes of neutrophils.
Derochette, Sandrine; Mouithys-Mickalad, Ange; Deby-Dupont, Ginette et al.
20138th International Human Peroxidase Meeting
 

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Keywords :
Protéine kinase C; NADPH oxydase; Myéloperoxydase; Neutrophiles; Curcumine
Abstract :
[en] Neutrophils (PMNs) produce reactive oxygen species (ROS) to kill pathogenic agents. After appropriate stimulation, leading to the activation of protein kinase C (PKC), the cytosolic subunits of the NADPH oxidase (Nox2) are phosphorylated and translocated to the membrane flavocytochrome b558, forming the active enzyme which produces superoxide anion (O2●-). From O2●- derives H2O2 used by the PMNs myeloperoxidase (MPO) to form strong oxidant species. Many human and animal pathologies with fatal issue are associated with uncontrolled activation of PMNs. The modulation of enzymes implied in ROS production is thus a primary target to manage excessive inflammatory events. For this purpose, we evaluated the effects of NDS27, a water-soluble salt of curcumin combined with hydroxypropyl-β-cyclodextrin, on the activities of PKC, Nox2 and MPO. PKC activation was determined by western blotting with specific antibodies against phosphorylated PKC in extracts from PMNs after their incubation or not with NDS27. A cell-free assay was used to evaluate the effect of NDS27 before or after the assembly of Nox2 subunits. MPO activity was tested by the SIEFED technique in which NDS27 was pre-incubated with the enzyme and discarded before its activity measurement. An inhibition of PKC phosphorylation and Nox2 activity were observed at respectively 10-4 and 10-5 M of NDS27. The Nox2 inhibition was more pronounced when NDS27 was added before the assembly stimulation, suggesting a direct action of NDS27 on the subunits translocation. NDS27 also dose-dependently decreased the activity of MPO (21 % at 10-5 M), indicating an interaction with the enzyme structure. Our results demonstrated that NDS27 is a potent inhibitor of the two major enzymes responsible for ROS production in PMNs, and also acts on the activation cascade of Nox2. The modulatory effect of NDS27 towards the oxidant activity of PMNs opens therapeutic perspectives to control pathologies with excessive inflammatory reactions.
Research center :
CORD - Centre de l'Oxygène, Recherche et Développement - ULiège
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Derochette, Sandrine ;  Université de Liège - ULiège > Centre de l'oxygène : Recherche et développement (C.O.R.D.)
Mouithys-Mickalad, Ange ;  Université de Liège - ULiège > Centre de l'oxygène : Recherche et développement (C.O.R.D.)
Deby-Dupont, Ginette
Neven, Philippe
Serteyn, Didier  ;  Université de Liège - ULiège > Département clinique des animaux de compagnie et des équidés > Anesthésiologie gén. et pathologie chirurg. des grds animaux
Franck, Thierry  ;  Université de Liège - ULiège > Département clinique des animaux de compagnie et des équidés > Anesthésiologie gén. et pathologie chirurg. des grds animaux
Language :
English
Title :
A water-soluble salt of curcumin (NDS27) inhibits myeloperoxidase and NADPH oxidase activities, two major enzymes of neutrophils.
Alternative titles :
[fr] Le NDS27, une forme hydrosoluble de la curcumine, inhibe l'activité de la myéloperoxidase et de la NADPH oxydase, deux enzymes majeures des neutrophiles
Publication date :
11 September 2013
Number of pages :
A0
Event name :
8th International Human Peroxidase Meeting
Event place :
Sydney, Australia
Event date :
du 09 septembre 2013 au 12 septembre 2013
Audience :
International
Name of the research project :
Purification de la NADPH oxydase des neutrophiles équins : mise au point de nouveaux outils pour la quantification et la mesure spécifique de son activité et pour la recherche d'inhibiteurs de l'enzyme
Funders :
FRIA - Fonds pour la Formation à la Recherche dans l'Industrie et dans l'Agriculture [BE]
Available on ORBi :
since 26 September 2013

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