Involvement of acid ceramidase in the degradation of bioactive N-acylethanolamines

Kazuhito Tsuboi, Tatsuya Tai, Ryouhei Yamashita, Hanif Ali, Takashi Watanabe, Toru Uyama, Yoko Okamoto, Keisuke Kitakaze, Yasuhiro Takenouchi, Shinji Go, Iffat Ara Sonia Rahman, Hitoshi Houchi, Tamotsu Tanaka, Yasuo Okamoto, Akira Tokumura, Junko Matsuda, Natsuo Ueda. Biochim Biophys Acta Mol Cell Biol Lipids. 2021 Sep;1866(9):158972.

Laboratory studyHumansOther animals

Design

Laboratory study

Subjects

Purified recombinant human acid ceramidase; HEK293 and LNCaP human cell lines; tissue from mice lacking saposin D and wild-type mice

Dose used in the study

Not applicable; palmitoylethanolamide was not given

Duration

Not stated in the abstract

What was measured

Hydrolysis of N-acylethanolamines by acid ceramidase; cellular N-acylethanolamine levels after overexpressing or silencing the enzyme; hydrolysing activity in mouse tissue.

What the authors reported

This laboratory study found:

• Purified human acid ceramidase hydrolysed several N-acylethanolamines, with lauroylethanolamide the most reactive.
• Overexpressing the enzyme lowered N-acylethanolamine levels in cells, and silencing it raised them.
• Tissue from mice lacking saposin D had much lower hydrolysing activity.
• The authors propose acid ceramidase as a third enzyme that degrades N-acylethanolamines including palmitoylethanolamide.

Limits of this study

A cell and enzyme study; it cannot show any effect in people or animals treated in practice. Funding and conflicts not stated in the abstract.

Source

PubMed 34033896 · doi:10.1016/j.bbalip.2021.158972

Entry checked against the abstract on PubMed on 2026-09-22. The dose shown is the dose the researchers used. It is not a recommendation. How to read this page.