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The initial synthesis of proteins during development. Phosphoenolpyruvate carboxylase in rat liver at birth

H Philippidis, R W Hanson, L Reshef

    The Biochemical Journal
    |March 1, 1972
    PubMed

    Insights

    Phosphoenolpyruvate carboxylase rapidly appears in rat liver at birth due to a 20-fold increase in synthesis and minimal degradation. This enzyme induction pattern resembles bacterial substrate-induced enzyme regulation.

    Area of Science:

    • Biochemistry
    • Developmental Biology
    • Enzymology

    Background:

    • Phosphoenolpyruvate carboxylase (PEPC) is a key gluconeogenic enzyme.
    • Its role in developing rat liver requires elucidation.

    Purpose of the Study:

    • To investigate the developmental changes in hepatic phosphoenolpyruvate carboxylase levels in rats.
    • To determine the synthesis and degradation rates of this enzyme during early development.

    Main Methods:

    • Utilized a specific antibody against rat liver phosphoenolpyruvate carboxylase.
    • Quantified enzyme levels, synthesis rates, and degradation rates in fetal and neonatal rat livers.

    Main Results:

    • PEPC levels significantly increase at birth, with a 20-fold rise in synthesis rate from fetus to 1-day-old rat.
    • No significant degradation was observed in the first day post-birth, leading to a 12-fold increase in hepatic enzyme content.
    • Post-neonatal development showed a degradation half-time of approximately 13 hours.

    Conclusions:

    • The rapid appearance of PEPC at birth is primarily driven by a substantial increase in its synthesis rate.
    • The observed pattern of PEPC induction in neonatal rat liver shares similarities with bacterial substrate-induced enzyme systems.

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