Co-ordinated induction of beta-carotene cleavage enzyme and retinal reductase in the duodenum of the developing chicks.
The developmental patterns of expression of beta-carotene cleavage enzyme activity were compared with those of retinal reductase and NAD-dependent retinol dehydrogenase activities in chick duodenum during the perinatal period. The beta-carotene cleavage enzyme activity was not detected in the duodenum before hatching, but it increased rapidly during 24 h after hatching. On the other hand, a considerable level of beta-carotene cleavage enzyme activity was observed in the liver of embryonic stages and its activity gradually rose during the perinatal period. Comparison of kinetic constants for the beta-carotene cleavage enzyme activities in the duodenum and the liver indicated that the enzyme in the duodenum possessed a lower affinity for beta-carotene than that in the liver. The retinal reductase activity was detected in the microsomes of the duodenum at the earliest time examined, i.e. day 16 of embryogenesis and its activity began to rise on the last day of embryogenesis, which was followed by a gradual increase until 1 day of age. The NAD-dependent retinol dehydrogenase activity was also seen in the microsomes of the duodenum in embryonic stages and its activity increased in parallel with the retinal reductase activity around the hatching period. These developmental inductions of beta-carotene cleavage enzyme and retinal reductase activities in the duodenum coincided with those of cellular retinol-binding protein, type II (CRBPII) and lecithin: retinol acyltransferase (LRAT). These results suggest that a co-ordinated induction mechanism should be operative for beta-carotene cleavage enzyme and retinal reductase, both of which are inevitable in the process of beta-carotene absorption and metabolism.
Tajima
S
S
School of Food and Nutritional Sciences, University of Shizuoka, 52-1 Yada, Shizuoka 422-8526, Japan.
Goda
T
T
Takase
S
S
D000217:Acyltransferases / Q000378:metabolism; D000429:Alcohol Oxidoreductases / Q000096:biosynthesis* / Q000378:metabolism; D000818:Animals; D002642:Chick Embryo / Q000201:enzymology*; D002645:Chickens / Q000254:growth & development / Q000378:metabolism; D004386:Duodenum / Q000196:embryology / Q000201:enzymology*; D004790:Enzyme Induction; D008099:Liver / Q000196:embryology / Q000201:enzymology*; D010105:Oxygenases / Q000096:biosynthesis*; D012177:Retinol-Binding Proteins / Q000378:metabolism; D054840:Retinol-Binding Proteins, Cellular; D019207:beta Carotene / Q000378:metabolism; D050559:beta-Carotene 15,15'-Monooxygenase
D012177:Retinol-Binding Proteins; D054840:Retinol-Binding Proteins, Cellular; D019207:beta Carotene; D000429:Alcohol Oxidoreductases; C022520:retinol dehydrogenase; C084155:alcohol dehydrogenase (NAD(P)+); D010105:Oxygenases; D050559:beta-Carotene 15,15'-Monooxygenase; D000217:Acyltransferases; C056942:lecithin-retinol acyltransferase