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Functional activation by glucagon of glucose 6‐phosphatase and gluconeogenesis in the perfused liver of the fetal guinea pig
Author(s) -
Band Geoffrey C.,
Jones Colin T.
Publication year - 1980
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(80)81028-3
Subject(s) - glucagon , citation , gluconeogenesis , chemistry , philosophy , library science , medicine , computer science , biochemistry , enzyme , insulin
The fetal livers of several species have the enzymic capacity for gluconeogenesis [l-4]. Despite this, de novo glucose synthesis has not been demonstrated, and glucose output from the perfused fetal liver [5-71 is probably the result of glycogenolysis rather than gluconeogenesis. Studies with the perfused fetal guinea pig liver have indicated that at 50 days gestational age no gluconeogenesis occurs in the presence of a range of gluconeogenic substrates, even though the liver has moderate activities of the gluconeogenic enzymes. The reasons for this are unclear. Glucagon is a potent activator of gluconeogenesis in adult livers [8] and stimulated the incorporation of [14C]alanine into glucose by the perfused liver of the near-term (63 day) guinea pig fetus [9]. Thus the effects of glucagon on the perfused fetal guinea pig liver at 50 days have been investigated. The results indicate that glucagon stimulates gluconeogenesis and causes functional activation of glucose 6-phosphatase.