Heme oxygenase and cyclooxygenase in the central nervous system: A functional interplay (Articolo in rivista)

Type
Label
  • Heme oxygenase and cyclooxygenase in the central nervous system: A functional interplay (Articolo in rivista) (literal)
Anno
  • 2006-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1002/jnr.21049 (literal)
Alternative label
  • Mancuso, C (Mancuso, Cesare); Perluigi, M (Perluigi, Marzia); Cini, C (Cini, Chiara); De Marco, C (De Marco, Carlo); Stella, AMG (Stella, Anna Maria Giuffrida); Calabrese, V (Calabrese, Vittorio) (2006)
    Heme oxygenase and cyclooxygenase in the central nervous system: A functional interplay
    in Journal of neuroscience research; WILEY-LISS, DIV JOHN WILEY & SONS INC, 111 RIVER ST, HOBOKEN, NJ 07030 (Stati Uniti d'America)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Mancuso, C (Mancuso, Cesare); Perluigi, M (Perluigi, Marzia); Cini, C (Cini, Chiara); De Marco, C (De Marco, Carlo); Stella, AMG (Stella, Anna Maria Giuffrida); Calabrese, V (Calabrese, Vittorio) (literal)
Pagina inizio
  • 1385 (literal)
Pagina fine
  • 1391 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 84 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 7 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 7 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1. Catania Univ, Fac Med, Dept Chem, Sect Biochem & Mol Biol, I-95100 Catania, Italy 2. Univ Roma La Sapienza, Dept Biochem Sci, I-00161 Rome, Italy 3. Univ Sacred Heart, Sch Med, Inst Pharmacol, I-00168 Rome, Italy (literal)
Titolo
  • Heme oxygenase and cyclooxygenase in the central nervous system: A functional interplay (literal)
Abstract
  • Heme oxygenase (HO) and cyclooxygenase (COX) are two hemeproteins involved in the regulation of several functions in the nervous system. Heme oxygenase is the enzyme responsible for the degradation of heme into ferrous iron, carbon monoxide (CO), and biliverdin, the latter being further reduced in bilirubin (BR) by biliverdin reductase. Heme oxygenase-derived CO is a gaseous neuromodulator and plays an important role in the synaptic plasticity, learning and memory processes, as well as in the regulation of hypothalamic neuropeptide release, whereas BR is an endogenous molecules with antioxiclant and anti-nitrosative activities. Cyclooxygenase is considered a pro-inflammatory enzyme as free radicals and prostaglandins (PGs) are produced during its catalytic cycle. Although PGs are also involved in a variety of physiologic conditions including angiogenesis, hemostasis, or regulation of kidney function, upregulation of COX and increase in PGs levels are a common feature of neuroinflammation. In the brain, a functional interplay exists between HO and COX. Heme oxygenase regulates COX activity by reducing the intracellular heme content or by generating CO, which stimulates PGE(2) release. Increased levels of PGs, free radicals, and the associated oxidative stress serve in the brain as a trigger for the induction of HO isoforms which increases cellular antioxiclant defenses to counteract oxidative damage. The importance of the interaction between HO and COX in the regulation of physiologic brain functions, and its relevance to neuroprotective or neurodegenerative mechanisms are discussed. (literal)
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