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Details on Person Cytochrome P450 (CYP) enzymes are thought to ω-hydroxylate (...
| Class:Id | Summation:9027312 |
|---|---|
| _displayName | Cytochrome P450 (CYP) enzymes are thought to ω-hydroxylate (... |
| _timestamp | 2017-11-14 12:43:08 |
| created | [InstanceEdit:9027299] Jassal, Bijay, 2017-10-30 |
| literatureReference | [LiteratureReference:2161850] Prostaglandin and leukotriene omega-hydroxylases [LiteratureReference:9027020] Cellular and molecular basis of wound healing in diabetes |
| modified | [InstanceEdit:9028878] Jassal, Bijay, 2017-11-13 [InstanceEdit:9029003] Jassal, Bijay, 2017-11-14 |
| text | 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). |
| (summation) | [Reaction:9027042] CPY4 ω-oxidises 14(S)-HDHA to MaR-L1 [Homo sapiens] |
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No pathways have been reviewed or authored by Cytochrome P450 (CYP) enzymes are thought to ω-hydroxylate (... (9027312)
