Retinoid glucuronides do not interact with retinoid binding proteins.
Retinoid glucuronides have recently been described as water soluble, biologically active retinoids. In mouse mammary gland organ cultures retinoyl glucuronide, a retinoic acid counterpart, inhibited hormone induced differentiation. In this report we examined whether the effects of retinoyl and retinyl glucuronides are mediated by specific retinoid binding protein in mammary glands in organ culture. Results indicated that neither retinoyl nor retinyl glucuronide competed for cytosolic retinoic acid or retinol binding proteins respectively. These results indicate that either the effects of retinoid glucuronides are independent of retinoid binding proteins or they have to be metabolized to an active component which may in turn bind to retinoid binding protein for the glucuronide action.
Mehta
R G
RG
Laboratory of Pathophysiology, IIT Research Institute, Chicago, IL 60616.
Barua
A B
AB
Olson
J A
JA
Moon
R C
RC
D000818:Animals; D005260:Female; D005965:Glucuronates / Q000378:metabolism*; D008321:Mammary Glands, Animal / Q000378:metabolism; D051379:Mice; D008807:Mice, Inbred BALB C; D009924:Organ Culture Techniques; D012176:Retinoids / Q000378:metabolism*; D012177:Retinol-Binding Proteins / Q000378:metabolism*
D005965:Glucuronates; D012176:Retinoids; D012177:Retinol-Binding Proteins