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Radiometric Assay of ABHD2 Activity
Domenico Fazio1, Emanuele Criscuolo2,3, Mauro Maccarrone2,4
1European Center for Brain Research/Santa Lucia Foundation IRCCS, Rome, Italy. dodo.fa@hotmail.it.
Methods in Molecular Biology (Clifton, N.J.)
|September 24, 2022
Summary
Alpha-beta hydrolase domain-containing protein 2 (ABHD2) cleaves 2-arachidonoylglycerol (2-AG). Progesterone activates ABHD2, a nonnuclear receptor, terminating hormone effects by releasing glycerol and arachidonic acid.
Area of Science:
- Biochemistry
- Enzymology
- Molecular Biology
Background:
- Alpha-beta hydrolase domain-containing protein 2 (ABHD2) is a serine hydrolase.
- ABHD2 hydrolyzes the endogenous cannabinoid 2-arachidonoylglycerol (2-AG).
- ABHD2 acts as a non-nuclear receptor for progesterone, terminating its biological effects.
Purpose of the Study:
- To characterize the enzymatic activity of ABHD2.
- To establish a method for quantifying ABHD2 activity.
Main Methods:
- Utilized a radioactive substrate, 2-oleoyl-[3H]glycerol, for enzymatic assays.
- Measured the release of [3H]glycerol to quantify ABHD2 activity.
- Employed established acylglycerol lipase activity assay techniques.
Main Results:
- Demonstrated the ability of ABHD2 to cleave acylglycerols.
- Quantified ABHD2 enzymatic activity through the detection of released [3H]glycerol.
- Validated the use of 2-oleoyl-[3H]glycerol as a substrate for ABHD2 activity measurement.
Conclusions:
- ABHD2 enzymatic activity can be reliably measured using a radioactive glycerol-releasing assay.
- The findings support the role of ABHD2 in lipid metabolism and hormone signaling pathways.
