[Recent knowledge about intestinal absorption and cleavage of carotenoids].
Our knowledge about intestinal absorption and cleavage of carotenoids has rapidly grown during the last years. New facts about carotenoid absorption have emerged while some controversies about cleavage are close to end. The knowledge of the absorption and conversion processes is indispensable to understand and interpret the perturbations that can occur in the metabolism of carotenoids and vitamin A. Recently, it has been shown that the absorption of certain carotenoids is not passive - as believed for a long time - but is a facilitated process that requires, at least for lutein, the class B-type 1 scavenger receptor (SR-B1). Various epidemiological and clinical studies have shown wide variations in carotenoid absorption from one subject to another, such differences are now explained by the structure of the concerned carotenoid, by the nature of the food that is absorbed with the carotenoid, by diverse exogenous factors like the intake of medicines or interfering components, by diet factors, by genetic factors, and by the nutritional status of the subject. Recently, the precise mechanism of beta-carotene cleavage by betabeta-carotene 15,15' monooxygenase (EC 1.14.99.36) - formerly called beta-carotene 15,15' dioxygenase (ex EC 1.13.11.21) - has been discovered, and a second enzyme which cleaves asymmetrically the beta-carotene molecule has been found. beta-carotene 15,15' monooxygenase only acts on the 15,15' bond, thus forming two molecules of retinal from one molecule of beta-carotene by central cleavage. Even though the betabeta-carotene 15,15' monooxygenase is much more active on the beta-carotene molecule, a study has shown that it can act on all carotenoids. Searchers now agree that other enzymes that can catalyse an eccentric cleavage of carotenoids probably exist, but under physiological conditions the betabeta-carotene 15,15' monooxygenase is by far the most active, and it is mainly effective in the small bowel mucosa and in the liver. However the conversion of provitamin A carotenoids into vitamin A is only partial, and requires a satisfactory protein status.
Borel
P
P
UMR 476 Inserm/1260 Inra Marseille, France.
Drai
J
J
Faure
H
H
Fayol
V
V
Galabert
C
C
Laromiguière
M
M
Le Moël
G
G
D000818:Animals; D001682:Biological Availability; D002338:Carotenoids / Q000097:blood / Q000378:metabolism*; D002415:Cats; D002648:Child; D004043:Dietary Fiber; D006801:Humans; D007231:Infant, Newborn; D007408:Intestinal Absorption; D007413:Intestinal Mucosa / Q000201:enzymology; D007421:Intestine, Small / Q000201:enzymology; D008099:Liver / Q000201:enzymology; D000077276:Lycopene; D006899:Mixed Function Oxygenases / Q000378:metabolism; D009752:Nutritional Status; D010599:Pharmacokinetics; D051381:Rats; D013997:Time Factors; D014801:Vitamin A / Q000378:metabolism*; D014802:Vitamin A Deficiency / Q000378:metabolism; D024341:Xanthophylls / Q000378:metabolism
D004043:Dietary Fiber; D024341:Xanthophylls; D014801:Vitamin A; D002338:Carotenoids; D006899:Mixed Function Oxygenases; C079232:beta-carotene hydroxylase; D000077276:Lycopene