Hepatic glucose-6-phosphatase development in preterm and full-term guinea-pigs: comparison with rat and human

H Lyall1, H M Scott, A Burchell

  • 1Department of Obstetrics and Gynaecology, Ninewells Hospital and Medical School, University of Dundee, United Kingdom.

Insights

Prematurity does not permanently alter liver glucose-6-phosphatase activity in guinea pigs. Postnatal development of this enzyme is not significantly impacted by being born early.

Area of Science:

  • Biochemistry
  • Developmental Biology
  • Neonatal Physiology

Background:

  • Hepatic glucose-6-phosphatase (G6Pase) activity is crucial for glucose homeostasis after birth.
  • Term infants exhibit a significant postnatal rise in G6Pase activity.
  • Preterm infants often show persistently low G6Pase activity, suggesting potential developmental impairment.

Purpose of the Study:

  • To investigate if prematurity causes long-term changes in hepatic glucose-6-phosphatase activity in mammals.
  • To examine the ontogeny of G6Pase in term and preterm guinea pigs.

Main Methods:

  • Studied hepatic glucose-6-phosphatase activity in term guinea pigs.
  • Analyzed G6Pase activity in guinea pigs delivered prematurely via Caesarean section.
  • Compared G6Pase activity levels at birth and during the postnatal period.

Main Results:

  • Hepatic G6Pase activity was approximately 5-fold lower in preterm guinea pigs at birth compared to term neonates.
  • Preterm guinea pigs demonstrated a rapid increase in G6Pase activity postnatally, reaching levels similar to term-born counterparts.
  • The postnatal changes in hepatic G6Pase activity in term guinea pigs were less pronounced than those observed in rats or human infants.

Conclusions:

  • Prematurity alone does not lead to abnormal long-term development of hepatic glucose-6-phosphatase activity in guinea pigs.
  • The guinea pig model suggests that the observed low G6Pase activity in preterm infants may not be solely due to prematurity itself.
  • Further research is needed to understand the mechanisms behind altered G6Pase activity in preterm human infants.

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