Tg. Tietjen et al., EXPRESSION OF THE CLASS-I ALCOHOL-DEHYDROGENASE GENE IN DEVELOPING RAT FETUSES, The Journal of histochemistry and cytochemistry, 42(6), 1994, pp. 745-753
Class I alcohol dehydrogenase (ADH) is the principal enzyme responsibl
e for ethanol oxidation in mammals. Although primarily regarded as an
enzyme that functions in the adult, Class I ADH has been reported to b
e present in fetal tissues. By in situ hybridization, we demonstrated
the tissue localization of the Class I ADH transcript in developing ra
t fetuses between Days 15 (E 15) and 18 (E18) of gestation. Abundant t
ranscripts were present in epidermis, lung, and urinary bladder. In th
ese tissues, the messages were localized primarily to the superficial
layer of the epithelium and increased with development. The liver exhi
bited significant signals only in the E18 fetus, when parenchymal hepa
tocytes first appeared. The E15 and E16 small intestines, with their e
pithelium arranged in a stratified fashion, displayed signals in the s
ubmucosal mesenchymal layer. By E17, a rearrangement of the intestinal
epithelium into an almost monolayer configuration was observed. This
change was associated with a redistribution of the ADH transcript to t
he surface of the epithelium. further relocation of the messages was n
oted in the adult small intestine, in which they became concentrated i
n the base of the crypt. These findings indicate that expression of th
e rat class I ADH gene follows a dynamic course in specific epithelial
tissues during fetal development. In addition, the apparent superfici
al localization of the ADH message in most of these tissues suggests t
hat ADH functions in metabolizing either endogenously or exogenously d
erived alcohol substrates present in the fetal environment.