Lipoxygenase-catalyzed polymerization of phenolic lipids suggests a new mechanism for allergic contact dermatitis induced by urushiol and its analogs.

Abstract

Lipoxygenase was found to catalyze the oxidative polymerization of phenolic lipids containing a (Z,Z)-pentadiene in the side chain, the model compounds of urushiol and its analog, yielding methanol-soluble and insoluble polymers. The structural analysis of the resulted polymers suggested that the polymerization occurred at both the phenol and the unsaturated side chain. The key step of the polymerization was the generation of the hydroperoxide at the unsaturated side chain by lipoxygenase. The decomposition of hydroperoxide and concomitant dehydrogenation of phenol ring catalyzed by lipoxygenase might produce radicals that could be coupled to form cross-linked polymers. This lipoxygenase-mediated reaction implies a new mechanism for contact allergy of urushiol and its analogs.

• Authors: Zuyong Xia, Tetsuo Miyakoshi, Takashi Yoshida
• Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 315 Issue 3 Pg. 704-9 (Mar 12 2004) ISSN: 0006-291X [Print] United States
• PMID: 14975758 (Publication Type: Journal Article)

Chemical References

• Catechols
• Lipids
• Phenols
• urushiol
• Hydrogen Peroxide
• Peroxidase
• Lipoxygenase

Topics

• Catalysis
• Catechols (adverse effects, chemistry, immunology, metabolism)
• Dermatitis, Allergic Contact (enzymology, etiology, metabolism)
• Hydrogen Peroxide (chemistry)
• Lipid Metabolism
• Lipids (chemistry)
• Lipoxygenase (metabolism)
• Magnetic Resonance Spectroscopy
• Molecular Weight
• Oxidation-Reduction
• Peroxidase (metabolism)
• Phenols (chemistry, metabolism)
• Solubility
• Soybeans (enzymology)