6533b853fe1ef96bd12ac32e

RESEARCH PRODUCT

Heme oxygenase-1 induction by nitric oxide in RAW 264.7 macrophages is upregulated by a cyclo-oxygenase-2 inhibitor.

Aida HabibAna María VicenteMarilyne LebretSylviane Levy-toledanoMaría José AlcarazChristophe CréminonJacques Maclouf

subject

BiophysicsSpermineNitric OxideBiochemistryNitric oxideCell Linechemistry.chemical_compoundMiceDownregulation and upregulationMacrophageAnimalsCyclooxygenase InhibitorsRNA MessengerMolecular BiologyHemeCyclooxygenase 2 InhibitorsMacrophagesMembrane ProteinsLong-term potentiationDrug SynergismMolecular biologyUp-RegulationHeme oxygenaseIsoenzymeschemistryBiochemistryCell cultureCyclooxygenase 2Prostaglandin-Endoperoxide SynthasesHeme Oxygenase (Decyclizing)PyrazolesNitrogen OxidesSpermineHeme Oxygenase-1

description

Unstimulated RAW 264.7 macrophages express negligible heme oxygenase-1 (HO-1) protein but incubation with the nitric oxide (NO) donor spermine nonoate (SPNO) induced HO-1 and weakly cyclo-oxygenase-2 (COX-2) protein. This effect was potentiated by coincubation with the COX-2 selective inhibitor, SC58125. Cells incubated with SPNO showed a strong increase in HO-1 mRNA levels after 4 h with a significant potentiation in the presence of SC58125, which did not modify HO-1 mRNA stability. The induction of HO-1 by NO and its potentiation by anti-inflammatory agents may play a role in inflammatory and immune responses.

10.1016/s0304-4165(01)00112-xhttps://pubmed.ncbi.nlm.nih.gov/11287117