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Monoacylglycerol hydrolase in human platelets.

K Bry, L C Andersson, T Kuusi

Biochimica Et Biophysica Acta

|October 26, 1979

Summary

Researchers identified monoacylglycerol hydrolase (MGH) in human platelets, differentiating it from other blood cells and plasma lipases. This platelet enzyme shows specific activity and stability characteristics.

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Area of Science:

Biochemistry
Hematology
Enzymology

Background:

Monoacylglycerol hydrolase (MGH) plays a role in lipid metabolism.
The presence and characteristics of MGH in human platelets were previously uncharacterized.

Purpose of the Study:

To identify and characterize monoacylglycerol hydrolase (MGH) activity in human platelets.
To determine if MGH is present in other human blood cells.
To investigate the properties of platelet MGH, including its release, solubilization, and optimal activity conditions.

Main Methods:

Assay of monoacylglycerol hydrolase activity in human platelet preparations.
Comparison of activity in platelets versus other blood cells (e.g., erythrocytes, leukocytes).
Investigation of enzyme release using heparin treatment.
Enzyme solubilization using Triton X-100.
Determination of optimal pH, ionic strength, and temperature for enzyme activity.
Assessment of inhibitor (HgCl2, NaF) and stabilizer (2-mercaptoethanol) effects.

Main Results:

Monoacylglycerol hydrolase (MGH) activity was detected exclusively in human platelets, not in other blood cells.
Platelet MGH was not released by heparin, indicating it is distinct from postheparin plasma lipases.
The enzyme was solubilized by Triton X-100.
Optimal activity was observed at pH 7-8, 0.1-0.3 M NaCl, and 37°C.
Enzyme activity was inhibited by HgCl2, not affected by NaF, and stabilized by 2-mercaptoethanol.

Conclusions:

Human platelets possess a unique monoacylglycerol hydrolase (MGH).
This platelet MGH is biochemically distinct from heparin-releasable plasma lipases.
The characterized properties provide a basis for understanding MGH function in platelets and potential therapeutic targeting.

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