Title : CRABPs Alter all-trans-Retinoic Acid Metabolism by CYP26A1 via Protein-Protein Interactions.

Pub. Date : 2022 Apr 24

PMID : 35565751






6 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Cellular retinoic acid binding proteins (CRABP1 and CRABP2) bind all-trans-retinoic acid (atRA), the active metabolite of vitamin A, with high affinity. Tretinoin cellular retinoic acid binding protein 1 Homo sapiens
2 Cellular retinoic acid binding proteins (CRABP1 and CRABP2) bind all-trans-retinoic acid (atRA), the active metabolite of vitamin A, with high affinity. Tretinoin cellular retinoic acid binding protein 1 Homo sapiens
3 Cellular retinoic acid binding proteins (CRABP1 and CRABP2) bind all-trans-retinoic acid (atRA), the active metabolite of vitamin A, with high affinity. Tretinoin cellular retinoic acid binding protein 1 Homo sapiens
4 CRABP1 and CRABP2 have been shown to interact with the atRA-clearing cytochrome P450 enzymes CYP26B1 and CYP26C1 and with nuclear retinoic acid receptors (RARs). Tretinoin cellular retinoic acid binding protein 1 Homo sapiens
5 We hypothesized that CRABP1 and CRABP2 also alter atRA metabolism and clearance by CYP26A1, the third key atRA-metabolizing enzyme in the CYP26 family. Tretinoin cellular retinoic acid binding protein 1 Homo sapiens
6 In comparison, the apparent kcat value was about 30% lower (0.71 +- 0.07 min-1 for holo-CRABP1 and 0.75 +- 0.09 min-1 for holo-CRABP2) in the presence of CRABPs than with free atRA (1.07 +- 0.08 min-1). Tretinoin cellular retinoic acid binding protein 1 Homo sapiens