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A Sensitive and Versatile Fluorescent Activity Assay for ABHD6.

Juha R Savinainen¹, Dina Navia-Paldanius¹, Jarmo T Laitinen²

¹School of Medicine, Institute of Biomedicine/Physiology, University of Eastern Finland, Kuopio, Finland.

Methods in Molecular Biology (Clifton, N.J.)

|June 2, 2016

Summary

We developed a new fluorescent assay to measure the activity of alpha/beta-hydrolase domain-containing 6 (ABHD6) enzyme. This assay enables efficient screening of inhibitors for ABHD6, a serine hydrolase with implications in the brain.

Keywords:

2-AG hydrolase Endocannabinoid Fluorescence Glycerol Inhibitor Lipase Monoacylglycerol Natural substrate Screening

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Area of Science:

Biochemistry
Enzymology
Assay Development

Background:

Alpha/beta-hydrolase domain-containing 6 (ABHD6) is a serine hydrolase.
ABHD6 shares substrate similarity with monoacylglycerol lipase (MAGL), a key enzyme in 2-arachidonoyl glycerol (2-AG) metabolism in the brain.

Purpose of the Study:

To develop a sensitive fluorescent assay for ABHD6 activity.
To enable high-throughput screening of ABHD6 inhibitors.

Main Methods:

Utilized HEK293 cell lysates overexpressing human ABHD6.
Developed a 96-well-plate assay monitoring glycerol release from 1(3)-arachidonoyl glycerol (1(3)-AG) hydrolysis.
Coupled glycerol detection to an enzymatic cascade producing the fluorescent product resorufin.

Main Results:

Established a sensitive fluorescent assay for ABHD6 activity.
The assay allows parallel testing of up to 40 compounds per plate.
Demonstrated advantages over traditional mass spectrometry and liquid scintillation assays.

Conclusions:

The developed assay provides a sensitive and efficient method for quantifying ABHD6 activity.
This assay facilitates the discovery and development of ABHD6 inhibitors.
The method offers significant improvements in throughput and ease of use compared to existing techniques.