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Glycogen metabolism in neonatal liver of the rat.

Authors
Type
Published Article
Journal
Archives of Biochemistry and Biophysics
0003-9861
Publisher
Elsevier
Publication Date
Volume
249
Issue
2
Pages
605–610
Identifiers
PMID: 3092743
Source
Medline

Abstract

Prior to birth the fetus of the rat accumulates large quantities of hepatic glycogen, with these stores mobilized as glucose in the early postnatal period to sustain the newborn until the onset of suckling and gluconeogenesis. The liver acts to mobilize glycogen in the early neonatal period and gradually adjusts to the alternating supply of nutrients that results from the onset of a feeding cycle. Early postnatal glycogen mobilization is reflected in the decreased active form of glycogen synthase (GS), the rate-limiting enzyme of glycogenesis, and increased activation of glycogen phosphorylase (GP), the rate-limiting enzyme of glycogenolysis. Levels of smooth endoplasmic reticulum (SER)-associated synthase phosphatase and phosphorylase phosphatase activities are diminished from high prenatal levels, contributing to these changes in activation of GS and GP. With the onset of suckling at 1-4 h after birth the liver again accumulates small quantities of glycogen. The period of 6 to 12 h after birth is characterized by large scale glycogenolysis. Glycogen levels are again increased at 24 h after birth, reflecting hepatic adaptation to the onset of meal feeding.

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