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Regulation of hepatic L-serine dehydratase and L-serine-pyruvate aminotransferase in the developing neonatal rat.
Biochem J. 1974 Dec; 144(3):519-31.BJ

Abstract

1. The activities of l-serine dehydratase and l-serine-pyruvate aminotransferase were determined in rat liver during foetal and neonatal development. 2. l-Serine-pyruvate aminotransferase activity begins to develop in late-foetal liver, increases rapidly at birth to a peak during suckling and then decreases at weaning to the adult value. 3. l-Serine dehydratase activity is very low prenatally, but increases rapidly after birth to a transient peak. After a second transient peak around the time weaning begins, activity gradually rises to the adult value. Both of these peaks have similar isoenzyme compositions. 4. In foetal liver both l-serine dehydratase and l-serine-pyruvate aminotransferase activities are increased after injection in utero of glucagon or dibutyryl cyclic AMP. Cycloheximide or actinomycin D inhibited the prenatal induction of both enzymes and actinomycin D blocked the natural increase of l-serine dehydratase immediately after birth. Glucose or insulin administration also blocked the perinatal increase of l-serine dehydratase. 5. After the first perinatal peak of l-serine dehydratase, activity is increased by cortisol and this is inhibited by actinomycin D. After the second postnatal peak, activity is increased by amino acids or cortisol and this is insensitive to actinomycin D inhibition. Glucose administration blocks the cortisol-stimulated increase in l-serine dehydratase and also partially lowers the second postnatal peak of activity. 6. The developmental patterns of the enzymes are discussed in relation to the pathways of gluconeogenesis from l-serine. The regulation of enzyme activity by hormonal and dietary factors is discussed with reference to the changes in stimuli that occur during neonatal development and to their possible mechanisms of action.

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Authors

Snell K
No affiliation info available
Walker DG
No affiliation info available

MeSH

AnimalsAnimals, NewbornBucladesineCycloheximideDactinomycinEnzyme InductionGlucagonGlucoseInsulinKineticsL-Serine DehydrataseLiverPyruvatesRatsSerineTransaminasesWeaning

Pub Type(s)

Journal Article

Language

eng

PubMed ID

4377655

Citation

Snell, K, and D G. Walker. "Regulation of Hepatic L-serine Dehydratase and L-serine-pyruvate Aminotransferase in the Developing Neonatal Rat." The Biochemical Journal, vol. 144, no. 3, 1974, pp. 519-31.
Snell K, Walker DG. Regulation of hepatic L-serine dehydratase and L-serine-pyruvate aminotransferase in the developing neonatal rat. Biochem J. 1974;144(3):519-31.
Snell, K., & Walker, D. G. (1974). Regulation of hepatic L-serine dehydratase and L-serine-pyruvate aminotransferase in the developing neonatal rat. The Biochemical Journal, 144(3), 519-31.
Snell K, Walker DG. Regulation of Hepatic L-serine Dehydratase and L-serine-pyruvate Aminotransferase in the Developing Neonatal Rat. Biochem J. 1974;144(3):519-31. PubMed PMID: 4377655.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Regulation of hepatic L-serine dehydratase and L-serine-pyruvate aminotransferase in the developing neonatal rat. AU - Snell,K, AU - Walker,D G, PY - 1974/12/1/pubmed PY - 1974/12/1/medline PY - 1974/12/1/entrez SP - 519 EP - 31 JF - The Biochemical journal JO - Biochem J VL - 144 IS - 3 N2 - 1. The activities of l-serine dehydratase and l-serine-pyruvate aminotransferase were determined in rat liver during foetal and neonatal development. 2. l-Serine-pyruvate aminotransferase activity begins to develop in late-foetal liver, increases rapidly at birth to a peak during suckling and then decreases at weaning to the adult value. 3. l-Serine dehydratase activity is very low prenatally, but increases rapidly after birth to a transient peak. After a second transient peak around the time weaning begins, activity gradually rises to the adult value. Both of these peaks have similar isoenzyme compositions. 4. In foetal liver both l-serine dehydratase and l-serine-pyruvate aminotransferase activities are increased after injection in utero of glucagon or dibutyryl cyclic AMP. Cycloheximide or actinomycin D inhibited the prenatal induction of both enzymes and actinomycin D blocked the natural increase of l-serine dehydratase immediately after birth. Glucose or insulin administration also blocked the perinatal increase of l-serine dehydratase. 5. After the first perinatal peak of l-serine dehydratase, activity is increased by cortisol and this is inhibited by actinomycin D. After the second postnatal peak, activity is increased by amino acids or cortisol and this is insensitive to actinomycin D inhibition. Glucose administration blocks the cortisol-stimulated increase in l-serine dehydratase and also partially lowers the second postnatal peak of activity. 6. The developmental patterns of the enzymes are discussed in relation to the pathways of gluconeogenesis from l-serine. The regulation of enzyme activity by hormonal and dietary factors is discussed with reference to the changes in stimuli that occur during neonatal development and to their possible mechanisms of action. SN - 0264-6021 UR - https://www.unboundmedicine.com/medline/citation/4377655/Regulation_of_hepatic_L_serine_dehydratase_and_L_serine_pyruvate_aminotransferase_in_the_developing_neonatal_rat_ DB - PRIME DP - Unbound Medicine ER -