Marked activation of the N-acylphosphatidylethanolamine-hydrolyzing phosphodiesterase by divalent cations

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...

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Bibliographic Details
Published in:Biochimica et biophysica acta 2001-05, Vol.1532 (1), p.121-127
Main Authors: Ueda, Natsuo, Liu, Qian, Yamanaka, Kenji
Format: Article
Language:English
Subjects:
Anandamide
Animals
Catalysis
Cations, Divalent
Enzyme Activation
Heart
Male
N-Acylethanolamine
N-Acylphosphatidylethanolamine
Phosphodiesterase
Phospholipase D
Phosphoric Diester Hydrolases - metabolism
Rats
Rats, Wistar
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Summary: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°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+.
ISSN:1388-1981
0006-3002
1879-2618
DOI:10.1016/S1388-1981(01)00120-2