Linked Life Data

12364461

Source:http://linkedlifedata.com/resource/pubmed/id/12364461

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2002-10-4
pubmed:abstractText
Arylalkylamine N-acetyltransferase (AANAT; serotonin N-acetyltransferase, EC 2.3.1.87) plays a unique transduction role in vertebrate physiology as the key interface between melatonin production and regulatory mechanisms. Circulating melatonin is elevated at night in all vertebrates, because AANAT activity increases in the pineal gland in response to signals from the circadian clock. Circadian regulation of melatonin synthesis is implicated in a variety of human problems, including jet lag, shift work, insomnia, and abnormal activity rhythms in blind persons. In this report AANAT was studied in the rhesus macaque to better understand human melatonin regulation. AANAT mRNA is abundant in the pineal gland and retina, but not elsewhere; AANAT mRNA is uniformly distributed in the pineal gland, but is limited primarily to the photoreceptor outer segments in the retina. Day and night levels of pineal and retinal AANAT mRNA are similar. In contrast, AANAT activity and protein increase more than 4-fold at night in both tissues. The activity of hydroxyindole-O-methyltransferase, the last enzyme in melatonin synthesis, is tonically high in the pineal gland, but is nearly undetectable in the retina; hydroxyindole O-methyltransferase mRNA levels exhibited a similar pattern. This supports the view that the source of circulating melatonin in primates is the pineal gland. The discovery in this study that rhesus pineal AANAT mRNA is high at all times is of special importance because it shows that posttranscriptional control of this enzyme plays a dominant role in regulating melatonin synthesis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-972X
pubmed:author
pubmed:issnType
Print
pubmed:volume
87
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4699-706
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:12364461-Acetylserotonin O-Methyltransferase, pubmed-meshheading:12364461-Amino Acid Sequence, pubmed-meshheading:12364461-Animals, pubmed-meshheading:12364461-Arylalkylamine N-Acetyltransferase, pubmed-meshheading:12364461-Arylamine N-Acetyltransferase, pubmed-meshheading:12364461-Blotting, Northern, pubmed-meshheading:12364461-Circadian Rhythm, pubmed-meshheading:12364461-Cloning, Molecular, pubmed-meshheading:12364461-Humans, pubmed-meshheading:12364461-In Situ Hybridization, pubmed-meshheading:12364461-Macaca mulatta, pubmed-meshheading:12364461-Melatonin, pubmed-meshheading:12364461-Molecular Sequence Data, pubmed-meshheading:12364461-Pineal Gland, pubmed-meshheading:12364461-RNA, Messenger, pubmed-meshheading:12364461-Retina, pubmed-meshheading:12364461-Sequence Alignment
pubmed:year
2002
pubmed:articleTitle
Melatonin synthesis enzymes in Macaca mulatta: focus on arylalkylamine N-acetyltransferase (EC 2.3.1.87).
pubmed:affiliation
Section on Neuroendocrinology, Laboratory of Developmental Neurobiology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892-4480, USA.
pubmed:publicationType
Journal Article, Comparative Study