Enzymatic formation of apo-carotenoids from the xanthophyll carotenoids lutein, zeaxanthin and β-cryptoxanthin by ferret carotene-9′,10′-monooxygenase

[Display omitted] ▸ Vertebrate CMO2 enzymatically cleaves xanthophylls at the 9,10 and 9′,10′ double bond. ▸ Lutein and zeaxanthin are preferentially cleaved over β-cryptoxanthin. ▸ 3-OH-β-apo-10′-carotenal is oxidized to 3-OH-β-apo-10′-carotenoic acid. Xanthophyll carotenoids, such as lutein, zeaxa...

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Vydáno v:	Archives of biochemistry and biophysics Ročník 506; číslo 1; s. 109 - 121
Hlavní autoři:	Mein, Jonathan R., Dolnikowski, Gregory G., Ernst, Hansgeorg, Russell, Robert M., Wang, Xiang-Dong
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	United States Elsevier Inc 01.02.2011
Témata:	Animals Apo-carotenoid beta-cryptoxanthin beta-ionone Carotenoids - biosynthesis Carotenoids - chemistry Cell Line Chromatography, High Pressure Liquid CMO1 CMO2 Cryptoxanthins enzyme kinetics Fatty Acid Desaturases - genetics Fatty Acid Desaturases - metabolism ferrets Ferrets - genetics Ferrets - metabolism Gas Chromatography-Mass Spectrometry high performance liquid chromatography in vitro studies In Vitro Techniques Kinetics Liver - metabolism lutein Lutein - metabolism Metabolism Oxidation-Reduction Recombinant Proteins - genetics Recombinant Proteins - metabolism Spodoptera Substrate Specificity vitamin A Xanthophyll Xanthophylls - metabolism zeaxanthin Zeaxanthins CMO2 CMO1 Metabolism Xanthophyll Apo-carotenoid
ISSN:	0003-9861, 1096-0384, 1096-0384
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Shrnutí:	[Display omitted] ▸ Vertebrate CMO2 enzymatically cleaves xanthophylls at the 9,10 and 9′,10′ double bond. ▸ Lutein and zeaxanthin are preferentially cleaved over β-cryptoxanthin. ▸ 3-OH-β-apo-10′-carotenal is oxidized to 3-OH-β-apo-10′-carotenoic acid. Xanthophyll carotenoids, such as lutein, zeaxanthin and β-cryptoxanthin, may provide potential health benefits against chronic and degenerative diseases. Investigating pathways of xanthophyll metabolism are important to understanding their biological functions. Carotene-15,15′-monooxygenase (CMO1) has been shown to be involved in vitamin A formation, while recent studies suggest that carotene-9′,10′-monooxygenase (CMO2) may have a broader substrate specificity than previously recognized. In this in vitro study, we investigated baculovirus-generated recombinant ferret CMO2 cleavage activity towards the carotenoid substrates zeaxanthin, lutein and β-cryptoxanthin. Utilizing HPLC, LC–MS and GC–MS, we identified both volatile and non-volatile apo-carotenoid products including 3-OH-β-ionone, 3-OH-α-ionone, β-ionone, 3-OH-α-apo-10′-carotenal, 3-OH-β-apo-10′-carotenal, and β-apo-10′-carotenal, indicating cleavage at both the 9,10 and 9′,10′ carbon–carbon double bond. Enzyme kinetic analysis indicated the xanthophylls zeaxanthin and lutein are preferentially cleaved over β-cryptoxanthin, indicating a key role of CMO2 in non-provitamin A carotenoid metabolism. Furthermore, incubation of 3-OH-β-apo-10′-carotenal with CMO2 lysate resulted in the formation of 3-OH-β-ionone. In the presence of NAD+, in vitro incubation of 3-OH-β-apo-10′-carotenal with ferret hepatic homogenates formed 3-OH-β-apo-10′-carotenoic acid. Since apo-carotenoids serve as important signaling molecules in a variety of biological processes, enzymatic cleavage of xanthophylls by mammalian CMO2 represents a new avenue of research regarding vertebrate carotenoid metabolism and biological function.
Bibliografie:	http://dx.doi.org/10.1016/j.abb.2010.11.005 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0003-9861 1096-0384 1096-0384
DOI:	10.1016/j.abb.2010.11.005