Levels of mRNAs coding for lipogenic enzymes in rat lung upon fasting and refeeding and during perinatal development.
The relative amounts of mRNAs coding for fatty-acid synthase (EC 2.3.1.85), acetyl-CoA carboxylase (EC 6.4.1.2), ATP citrate lyase (EC 4.1.3.8) and malic enzyme (EC 1.1.1.40) were determined in lungs and livers of adult rats that were normally fed, starved for 48 h or starved for 48 h and subsequently refed for 72 h with a carbohydrate-rich, fat-free diet. In the liver, starvation caused a small decrease in the relative abundance of the mRNAs which was not statistically significant. Subsequent refeeding caused a statistically significant increase in mRNAs for all of the enzymes studied. In the lung, no significant changes were found, indicating that the regulation of the abundance of mRNAs encoding the lipogenic enzymes in the lung differs from that in the liver. In the developing rat lung, mRNA for fatty-acid synthase increased 3-fold in abundance between fetal days 18 and 20 and decreased directly after birth (at day 22 of gestation). A similar pattern was observed for ATP citrate lyase mRNA. The level of acetyl-CoA carboxylase mRNA decreased significantly after birth. These observations indicate that in perinatal rat lungs, pretranslational regulation is involved in the control of the synthesis of these enzymes. The abundance of acetyl-CoA carboxylase mRNA did not change in the prenatal period, a time during which the specific activity of this enzyme increases. This lack of correlation between the specific activity of acetyl-CoA carboxylase and the abundance of its mRNA may indicate that translational regulation of the synthesis of the enzyme or post-synthetic regulatory effects on enzyme molecules are involved in the control of this enzyme in the prenatal period. No changes in the abundance of lung malic enzyme mRNAs were observed throughout the perinatal period.
Batenburg
J J
JJ
Laboratory of Veterinary Biochemistry, Utrecht University, The Netherlands.
Whitsett
J A
JA
D001275:ATP Citrate (pro-S)-Lyase / Q000235:genetics; D000103:Acetyl-CoA Carboxylase / Q000235:genetics; D000818:Animals; D000831:Animals, Newborn / Q000378:metabolism*; D005215:Fasting; D064429:Fatty Acid Synthases / Q000235:genetics; D005502:Food; D005786:Gene Expression Regulation; D005865:Gestational Age; D008055:Lipids / Q000096:biosynthesis*; D008099:Liver / Q000201:enzymology; D008168:Lung / Q000196:embryology / Q000201:enzymology* / Q000254:growth & development; D008291:Malate Dehydrogenase / Q000235:genetics; D008297:Male; D009693:Nucleic Acid Hybridization; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains
D008055:Lipids; D012333:RNA, Messenger; D008291:Malate Dehydrogenase; D064429:Fatty Acid Synthases; D001275:ATP Citrate (pro-S)-Lyase; D000103:Acetyl-CoA Carboxylase