Linked Life Data

12047899

Source:http://linkedlifedata.com/resource/pubmed/id/12047899

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2002-6-5
pubmed:abstractText
N-acylethanolamines including anandamide (an endogenous ligand of cannabinoid receptors) are biosynthesized from N-acyl-phosphatidylethanolamine (PE) by a phosphodiesterase of the phospholipase D type. The enzyme partially purified from the particulate fraction of rat heart hydrolyzed N-palmitoyl-PE to N-palmitoylethanolamine with a specific activity of 50 nmol/min per mg protein at 37 degrees C in the presence of 10 mM CaCl2. We found that the enzyme was highly activated in dose-dependent manner by polyamines like spermine, spermidine, and putrescine. Spermine was the most potent with an EC50 value around 0.1 mM, and increased the specific enzyme activity 27 fold up to 53 nmol/min per mg protein. However, a synergistic effect of spermine and the known activator (Ca2+ or Triton X-100) was not observed. The spermine-stimulated enzyme was also active with N-arachidonoyl-PE (a precursor of anandamide). Thus, polyamines may function as endogenous activators to control the biosynthesis of anandamide and other N-acylethanolamines.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0009-3084
pubmed:author
pubmed:issnType
Print
pubmed:volume
115
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
77-84
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Activation of N-acylethanolamine-releasing phospholipase D by polyamines.
pubmed:affiliation
Department of Biochemistry, Kagawa Medical University, 1750-1 Ikenobe, Miki, Kagawa, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't