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Published on: March 28, 2017
Acyl transferase activities in dog lung microsomes
Journal of Lipid Research
|January 1, 1971
Summary
Dog lung microsomes contain acyl transferases crucial for producing dipalmitoyl phosphatidylcholine, a key component of pulmonary surfactant. These enzymes ensure sufficient saturated phospholipids for lung function and potentially other cellular needs.
Area of Science:
- Biochemistry
- Pulmonary Medicine
- Cellular Biology
Background:
- Mammalian lungs contain high levels of dipalmitoyl phosphatidylcholine (DPPC), a saturated phospholipid essential for pulmonary surfactant.
- Phospholipids typically have asymmetric fatty acid chains (one saturated, one unsaturated), unlike the saturated chains in DPPC.
Purpose of the Study:
- To investigate the acyl transferase system in dog lung microsomes.
- To determine the reactivity of various acyl-CoA derivatives with specific lyso-phosphatidylcholine substrates.
Main Methods:
- Studied acyl transferase activity using different acyl-CoA derivatives (16:0, 18:0, 16:1, 18:1).
- Assessed substrate reactivity with 1-lyso-2-acyl- and 1-acyl-2-lyso-phosphatidylcholine.
Main Results:
- Palmitoyl CoA (16:0) and stearoyl CoA (18:0) showed reactivity towards both lyso positions.
- Palmitoyl CoA exhibited approximately twice the specific activity compared to stearoyl CoA.
- Unsaturated acyl derivatives (16:1, 18:1) were more reactive with the 2-lyso position than saturated ones.
Conclusions:
- Acyl transferases in lung microsomes are likely vital for synthesizing DPPC for pulmonary surfactant.
- The acyl transferase system may also produce other phosphatidylcholine species for non-surfactant cellular functions.
