Journal of Biochemistry Advance Access published online on September 19, 2008
Journal of Biochemistry, doi:10.1093/jb/mvn122
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
© 2008 The Japanese Biochemical Society
Expression and secretion of N-acylethanolamine-hydrolyzing acid amidase in human prostate cancer cells


Departments of 1 Biochemistry and 2 Urology, Kagawa University School of Medicine, Kagawa, Japan, 3 Department of Anesthesiology, the First Affiliated Hospital, and 4 Department of Stomatology, China Medical University, Shenyang, China
*Correspondence to Dr. Natsuo Ueda, Department of Biochemistry, Kagawa University School of Medicine, 1750-1 Ikenobe, Miki, Kagawa 761-0793, Japan, Tel.: +81-87-891-2102; fax: +81-87-891-2105; e-mail: nueda{at}med.kagawa-u.ac.jp
Received July 14, 2008; Accepted September 8, 2008
| Abstract |
|---|
N-Acylethanolamines (NAEs) are a class of bioactive lipid molecules in animal tissues, including the endocannabinoid anandamide and the anti-inflammatory substance N-palmitoylethanolamine. Enzymatic hydrolysis of NAEs is considered to be an important step to regulate their endogenous levels. Lysosomal NAE-hydrolyzing acid amidase (NAAA) as well as fatty acid amide hydrolase (FAAH) is responsible for this reaction. Here, we report relatively high expression of NAAA in human prostate cancer cells (PC-3, DU-145, and LNCaP) and prostate epithelial cells (PrEC), with the highest mRNA level in LNCaP cells. FAAH and the NAE-forming enzyme N-acylphosphatidylethanolamine-hydrolyzing phospholipase D (NAPE-PLD) were also detected in these cells. NAAA activity in LNCaP cells could be distinguished from coexisting FAAH activity, based on their different pH dependency profiles and specific inhibition of FAAH activiy by URB597. These results showed that both the enzymes were functionally active. We also found that NAAA was partly secreted from LNCaP cells, which underlined possible usefulness of this enzyme as a biomarker of prostate cancer.
Key Words: N-acylethanolamine, anandamide, endocannabinoid, LNCaP cell, lysosomal enzyme
Jun Wang and Li-Ying Zhao contributed equally to this work