Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1999-11-17
pubmed:abstractText
In Drosophila melanogaster strain Canton S, the catalase inhibitor 3-amino-1,2,4-triazole was used to enhance oxidative stress from endogenous sources. This treatment was chosen as an alternative to direct administration of oxidants, which would cause damage and interact with melatonin already in the extracellular space before they reach the intracellular compartments. Male flies were kept in constant darkness and fed 1% sucrose as the only diet, with or without additions of melatonin (2 mM), inhibitor (100 mM), or combinations of both. After 20 or 24 hr, most of the animals exposed to 3-amino-1,2,4-triazole only had died, whereas a large number of flies had survived the inhibitor treatment in the presence of melatonin. Protein carbonyl, an indicator of oxidative protein modification, and lipid peroxidation, as determined by the formation of malondialdehyde and 4-hydroxyalkenal, were measured in flies treated for 20 hr. Melatonin alone did not substantially change these parameters, but prevented the increase in protein carbonyl caused by the catalase inhibitor. The effect of 3-amino-1,2,4-triazole on lipid peroxidation was relatively minor, but a clear-cut inhibition was found after simultaneous administration of melatonin. The preferential suppression of oxidative damage of proteins, as compared to lipids, indicates a particular protective role for melatonin in the aqueous phase of cellular compartments.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0742-3098
pubmed:author
pubmed:issnType
Print
pubmed:volume
27
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
154-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Antioxidative effects of melatonin in Drosophila melanogaster: antagonization of damage induced by the inhibition of catalase.
pubmed:affiliation
Institut für Zoologie und Anthropologie, Universität Göttingen, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't