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Activity of neutral and alkaline ceramidases on fluorogenic N-acylated coumarin-containing aminodiols.

Abstract：

:Ceramidases catalyze the cleavage of ceramides into sphingosine and fatty acids. Previously, we reported on the use of the RBM14 fluorogenic ceramide analogs to determine acidic ceramidase activity. In this work, we investigated the activity of other amidohydrolases on RBM14 compounds. Both bacterial and human purified neutral ceramidases (NCs), as well as ectopically expressed mouse neutral ceramidase hydrolyzed RBM14 with different selectivity, depending on the N-acyl chain length. On the other hand, microsomes from alkaline ceramidase (ACER)3 knockdown cells were less competent at hydrolyzing RBM14C12, RBM12C14, and RBM14C16 than controls, while microsomes from ACER2 and ACER3 overexpressing cells showed no activity toward the RBM14 substrates. Conversely, N-acylethanolamine-hydrolyzing acid amidase (NAAA) overexpressing cells hydrolyzed RBM14C14 and RBM14C16 at acidic pH. Overall, NC, ACER3, and, to a lesser extent, NAAA hydrolyze fluorogenic RBM14 compounds. Although the selectivity of the substrates toward ceramidases can be modulated by the length of the N-acyl chain, none of them was specific for a particular enzyme. Despite the lack of specificity, these substrates should prove useful in library screening programs aimed at identifying potent and selective inhibitors for NC and ACER3.

journal_name

J Lipid Res

journal_title

Journal of lipid research

authors

Casasampere M,Camacho L,Cingolani F,Casas J,Egido-Gabás M,Abad JL,Bedia C,Xu R,Wang K,Canals D,Hannun YA,Mao C,Fabrias G

doi

10.1194/jlr.D061564

subject

Has Abstract

pub_date

2015-10-01 00:00:00

pages

2019-28

issue

10

eissn

0022-2275

issn

1539-7262

pii

jlr.D061564

journal_volume

56

pub_type

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