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Diglyceride kinase in human platelets.

F L Call, M Rubert

Journal of Lipid Research

|July 1, 1973

Summary

Human platelets possess diglyceride kinase, an enzyme crucial for producing phosphatidic acid. Enzyme activity in patients with kidney or liver failure was comparable to that in healthy individuals.

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Area of Science:

Biochemistry
Molecular Biology
Hematology

Background:

Platelets play a vital role in hemostasis and thrombosis.
Diglyceride kinase (DGK) is an enzyme involved in phospholipid metabolism.
Understanding DGK activity in platelets is important for various physiological processes.

Purpose of the Study:

To characterize the diglyceride kinase enzyme in human platelets.
To determine the kinetic properties and optimal conditions for platelet DGK activity.
To investigate potential alterations in DGK activity in patients with renal and hepatic failure.

Main Methods:

Platelet homogenates were prepared and fractionated.
Enzyme activity was assayed using diacylglycerol and adenosine 5'-triphosphate.
Kinetic parameters (Km) and pH optimum were determined.
DGK activity was compared between normal subjects and patients with renal/hepatic failure.

Main Results:

The majority of platelet diglyceride kinase is particulate-bound, with higher activity in membrane fractions.
Optimal enzyme activity requires both deoxycholate and magnesium.
The K(m) values for adenosine 5'-triphosphate and diacylglycerol were determined.
The pH optimum for the enzyme activity was found to be between 6.6 and 6.8.
Platelet DGK activity was similar in normal subjects and patients with renal and hepatic failure.

Conclusions:

Human platelets contain a particulate-bound diglyceride kinase with specific kinetic properties.
The enzyme's activity is not significantly altered in patients with renal and hepatic failure.
These findings contribute to the understanding of phospholipid metabolism in platelets and its potential clinical relevance.

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