Related Experiment Videos
Measurement of phospholipase D activity
A J Morris1, M A Frohman, J Engebrecht
1Department of Pharmacological Sciences, Stony Brook Health Sciences Center, New York 11794-8651, USA. andrew@pharm.sunysb.edu
Analytical Biochemistry
|November 5, 1997
Summary
Phospholipase D (PLD) enzymes cleave phosphatidylcholine, producing signaling molecules like phosphatidic acid. This review covers methods to measure PLD activity in vitro and in cells.
Area of Science:
- Biochemistry
- Cell Biology
- Enzymology
Background:
- Phospholipase D (PLD) enzymes catalyze the hydrolysis of phosphatidylcholine, yielding choline and phosphatidic acid.
- These enzymes also exhibit transphosphatidylation activity, transferring acyl chains to alcohols.
- PLD and its product, phosphatidic acid, are crucial in mammalian signal transduction pathways.
Purpose of the Study:
- To review the diverse roles of Phospholipase D (PLD) enzymes in biological systems.
- To highlight the significance of phosphatidic acid as a key signaling molecule in mammalian cells.
- To discuss methodologies for assessing PLD activity.
Main Methods:
- Literature review of biochemical and cell biological studies on PLD.
- Analysis of enzymatic assays for PLD activity determination.
- Examination of methods for measuring PLD in intact cellular systems.
Main Results:
- PLD enzymes are conserved across various organisms, from bacteria to vertebrates.
- Phosphatidic acid, a product of PLD, acts as a vital mediator in extracellular signal transduction.
- PLD activity is implicated in regulating critical cellular functions including protein trafficking, secretion, and cell morphology.
Conclusions:
- Phospholipase D plays a fundamental role in cellular signaling and regulation.
- Accurate determination of PLD activity is essential for understanding its biological functions.
- Further research into PLD enzymes and phosphatidic acid signaling holds promise for therapeutic applications.