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Related Experiment Videos

Characterization of microsomal ATPases from developing human placenta.

M Mukherjea, A S Chakraborti, S Misra

    Biochemical Medicine and Metabolic Biology
    |April 1, 1986
    PubMed
    Summary

    Human placental ATPase enzyme activity increases with gestational age until mid-pregnancy, then declines. Enzyme properties like substrate affinity and Vmax vary during development and at term.

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    Area of Science:

    • Biochemistry
    • Human Physiology
    • Developmental Biology

    Background:

    • Microsomal ATPases play crucial roles in cellular energy metabolism and transport.
    • Understanding ATPase activity in the human placenta is vital for comprehending feto-maternal exchange and placental development.

    Purpose of the Study:

    • To investigate the ontogenic changes and kinetic properties of various ATPases in the developing human placenta.
    • To characterize the influence of gestational age on enzyme activity, substrate affinity (Km), and maximal velocity (Vmax).

    Main Methods:

    • Enzyme activity assays were performed on human placental microsomes at different gestational ages.
    • Kinetic parameters (Km and Vmax) for ATP hydrolysis were determined for different ATPase types.
    • The effects of specific amino acids and deoxycholate on enzyme activity were assessed.

    Main Results:

    • Placental ATPase activities (Na+ + K+ + Mg2+-dependent, Mg2+-dependent, and Ca2+-dependent) increased until 18-21 weeks of gestation, followed by a decrease in late pregnancy.
    • Mg2+-dependent and Na+ + K+ + Mg2+-dependent ATPases exhibited similar Km values, distinct from the Ca2+-dependent enzyme.
    • Mg2+-dependent ATPase showed higher substrate affinity but lower Vmax compared to Ca2+-dependent ATPase. Vmax declined at term.
    • Enzymes were heat-labile and unaffected by tested amino acids; deoxycholate caused ~50% inhibition.

    Conclusions:

    • Human placental ATPase activities undergo significant developmental regulation throughout gestation.
    • Kinetic properties of placental ATPases vary, suggesting distinct roles and regulatory mechanisms.
    • These findings provide insights into placental function and its changes during pregnancy, with potential implications for fetal development.

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