Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2001-2-2
pubmed:abstractText
In the presence of hydrogen peroxide, horseradish peroxidase (HRP) catalyzes the production of N(1)-acetyl-N(2)-formyl-5-methoxykynuramine from melatonin. This reaction consumes oxygen and exhibits chemiluminescence in the 440-540 nm region. The excited cleavage product derived from the thermolysis of an intermediate dioxetane is suggested to be the emitting species. Chemiluminescence and the indole ring cleavage product were also observed when HRP/H(2)O(2) was replaced by phorbol myristate acetate or opsonized zymosan-activated neutrophils. Azide, a myeloperoxidase inhibitor, strongly suppressed melatonin oxidation. Superoxide dismutase has a strong inhibitory effect on light emission but catalase and uric acid are without effect on the emission. The oxidation of melatonin by activated neutrophils may be relevant to the in vivo functions of myeloperoxidase and melatonin. The possible biological implication of melatonin oxidation by neutrophils, especially in inflammatory conditions, is discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-291X
pubmed:author
pubmed:copyrightInfo
Copyright 2000 Academic Press.
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
279
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
657-62
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Myeloperoxidase-catalyzed oxidation of melatonin by activated neutrophils.
pubmed:affiliation
Departamento de Análises Clínicas e Toxicológicas, Faculdade de Ciências Farmacêuticas, São Paulo, CEP 05508-900, Brazil.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't