A novel lysophosphatidylcholine acyl transferase activity is expressed by peroxiredoxin 6.

Journal of Lipid Research
Aron B FisherSheldon I Feinstein

Abstract

The phospholipase A2(PLA2) activity of peroxiredoxin (Prdx)6 has important physiological roles in the synthesis of lung surfactant and in the repair of peroxidized cell membranes. These functions require the activity of a lysophospholipid acyl transferase as a critical component of the phospholipid remodeling pathway. We now describe a lysophosphatidylcholine acyl transferase (LPCAT) activity for Prdx6 that showed a strong preference for lysophosphatidylcholine (LPC) as the head group and for palmitoyl CoA in the acylation reaction. The calculated kinetic constants for acylation wereKm18 μM andVmax30 nmol/min/mg protein; theVmaxwas increased 25-fold by phosphorylation of the protein whileKmwas unchanged. Study of recombinant protein in vitro and in mouse pulmonary microvascular endothelial cells infected with a lentiviral vector construct indicated that amino acid D31 is crucial for LPCAT activity. A linear incorporation of labeled fatty acyl CoA into dipalmitoyl phosphatidylcholine (PC) indicated that LPC generated by Prdx6 PLA2activity remained bound to the enzyme for the reacylation reaction. Prdx6 is the first LPCAT enzyme with demonstrated cytoplasmic localization. Thus, Prdx6 is a complete enzyme comprising both PLA2and L...Continue Reading

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Citations

Oct 30, 2016·Annals of Anatomy = Anatomischer Anzeiger : Official Organ of the Anatomische Gesellschaft·Bárbara OlmedaJesus Pérez-Gil
May 3, 2018·Journal of Lipid Research·Aron B Fisher
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Apr 3, 2019·Antioxidants·Sheldon I Feinstein
May 30, 2020·International Journal of Molecular Sciences·Olga CañadasJesús Pérez-Gil
Feb 26, 2020·Antioxidants·Pei You WuCristian O'Flaherty
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Jan 16, 2021·Antioxidants·Yoo-Jin Park, Myung-Geol Pang
Oct 10, 2020·Redox Biology·María José López-GruesoCarmen Alicia Padilla
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