| First Author | Fierce Y | Year | 2008 |
| Journal | Arch Biochem Biophys | Volume | 472 |
| Issue | 2 | Pages | 126-38 |
| PubMed ID | 18295589 | Mgi Jnum | J:135646 |
| Mgi Id | MGI:3794225 | Doi | 10.1016/j.abb.2008.02.010 |
| Citation | Fierce Y, et al. (2008) In vitro and in vivo characterization of retinoid synthesis from beta-carotene. Arch Biochem Biophys 472(2):126-38 |
| abstractText | Retinoids are indispensable for the health of mammals, which cannot synthesize retinoids de novo. Retinoids are derived from dietary provitamin A carotenoids, like beta-carotene, through the actions of beta-carotene-15,15'-monooxygenase (BCMO1). As the substrates for retinoid-metabolizing enzymes are water insoluble, they must be transported intracellularly bound to cellular retinol-binding proteins. Our studies suggest that cellular retinol-binding protein, type I (RBP1) acts as an intracellular sensor of retinoid status that, when present as apo-RBP1, stimulates BCMO1 activity and the conversion of carotenoids to retinoids. Cellular retinol-binding protein, type II (RBP2), which is 56% identical to RBP1 does not influence BCMO1 activity. Studies of mice lacking BCMO1 demonstrate that BCMO1 is responsible for metabolically limiting the amount of intact beta-carotene that can be absorbed by mice from their diet. Our studies provide new insights into the regulation of BCMO1 activity and the physiological role of BCMO1 in living organisms. |
