Linked Life Data

11420181

Source:http://linkedlifedata.com/resource/pubmed/id/11420181

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2001-6-22
pubmed:abstractText
N-Acylethanolamines including anandamide (an endogenous ligand for cannabinoid receptors) are released from N-acylphosphatidylethanolamine (N-acyl-PE) by the catalysis of a phosphodiesterase of the phospholipase D type. The enzyme was solubilized from the particulate fractions of rat heart with the aid of octyl glucoside, and partially purified by anion-exchange chromatography. The enzyme hydrolyzed N-palmitoyl-PE with a specific activity of 17 nmol/min/mg protein at 37 degrees C. The enzyme activity increased dramatically up to 30-fold by millimolar order of Ca(2+). Ca(2+) could be replaced with other divalent cations such as Co(2+), Mg(2+), Mn(2+), Ba(2+), Sr(2+) and Ni(2+). The hydrolysis of N-arachidonoyl-PE (a precursor of anandamide) was also markedly stimulated by Ca(2+).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
1532
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
121-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Marked activation of the N-acylphosphatidylethanolamine-hydrolyzing phosphodiesterase by divalent cations.
pubmed:affiliation
Department of Biochemistry, Tokushima University, School of Medicine, Kuramoto-cho, 770-8503, Tokushima, Japan. nueda@kms.ac.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't