Abstract
ABSTRACT The study was carried out to evaluate the effect of AAT-deletion mutation at codon 248 of the BCO2 gene on the content of lutein, β-carotene, retinol, and α-tocopherol in the liver and fat of crossbred rabbits. The experimental animals comprised 90 rabbits, produced by reciprocal crossing between ins/del heterozygous parents of Flemish Giant, New Zealand Red, and Termond White breeds. All rabbits in the litter were genotyped, given the same diet, and finally slaughtered at 140 d of age. [...]
Highlights
Carotenoids can be divided into hydrocarbon carotenoids, i.e., carotenes (e.g., β-carotene and lycopene) and oxygenated carotenoids, i.e., xanthophylls
We reported for the first time the presence of a homozygous AAT in-frame deletion at codon 248 of the BCO2 gene in three yellow-fat rabbits (Strychalski et al, 2015)
The carcasses of rabbits were visually inspected, and it was found that all animals with the del/del genotype at codon 248 in BCO2 gene had yellow fat, whereas rabbits with ins/ins and ins/del genotypes had white fat (Figure 2)
Summary
Carotenoids can be divided into hydrocarbon carotenoids, i.e., carotenes (e.g., β-carotene and lycopene) and oxygenated carotenoids, i.e., xanthophylls (e.g., lutein and zeaxanthin). Carotenoids are cleaved by homologous enzymes BCO1 (β-carotene 15,15'-monooxygenase 1) and BCO2 (β-carotene 9',10'-oxygenase). BCO2 is characterized by broader substrate specificity than BCO1. BCO1 is a cytoplasmic protein, and BCO2 is found in the mitochondria (Amengual et al, 2011). Provitamin A carotenoids, such as β-carotene, α-carotene, and β-cryptoxanthin, may be cleaved by either BCO1 or BCO2. The activity of BCO2 is higher towards non-provitamin A carotenoids such as lycopene, lutein, and zeaxanthin (Mein et al, 2011). BCO2 cleaves carotenoids, yielding apo-10’-carotenals and ionones, whose functions have not been fully elucidated to date (Lietz et al, 2012)
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