CPY4 ω-oxidises 14(S)-HDHA to MaR-L1

Stable Identifier
Reaction [transition]
Homo sapiens
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Cytochrome P450 (CYP) enzymes are thought to ω-hydroxylate (position 22) 14(S)-hydroxy-docosahexaenoic acid (14(S)-HDHA) to 14(S),22-dihydroxy-docosahexaenoic acid, namely maresin-like mediator 1 (MaR-L1) (Hong et al. 2014). CYP inhibition was found to decrease the amount of MaR-L1 formed (Hong et al. 2014). The exact CYP responsible for MaR-L1 formation is unknown but is likely to be a member of the CYP4 family as those enzymes mediate the ω-hydroxylation of fatty acids and eicosanoids (Kikuta et al. 2002). Diabetes results in delayed- or non-healing of wounds and is associated with impaired macrophage function (Brem & Tomic-Canic 2007). Leukocytes and platelets play critical roles in wound healing by mechanisms as yet unknown. Maresin-like mediators MaR-L1 and Mar-L2 are produced by leukocytes and platelets and have been shown (in vitro) to restore reparative functions of diabetic macrophages in wounds (Hong et al. 2014).

Literature References
PubMed ID Title Journal Year
25200603 Maresin-like lipid mediators are produced by leukocytes and platelets and rescue reparative function of diabetes-impaired macrophages

Alapure, BV, Lu, Y, Tian, H, Bunnell, BA, Wang, Q, Hong, S, Laborde, JM

Chem. Biol. 2014
Catalyst Activity

monooxygenase activity of CYP4 [endoplasmic reticulum membrane]

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