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. 1972 Apr;69(4):800–804. doi: 10.1073/pnas.69.4.800

Glucagon-Stimulated Phosphorylation of Mitochondrial and Lysosomal Membranes of Rat Liver In Vivo

Rainer N Zahlten 1,2, Abraham A Hochberg 1,2, F W Stratman 1,2, Henry A Lardy 1,2
PMCID: PMC426567  PMID: 4337238

Abstract

The pancreatic hormone, glucagon, stimulates the net uptake of inorganic 32P in vivo into rat liver and its incorporation into proteins of microsomes, mitochondrial membranes, and lysosomes. Incorporation into cytosolic proteins was enhanced only slightly by glucagon. More than 95% of the protein-bound phosphate is present as phosphoserine. Both the radioactivity and the total amount of protein-bound phosphate are increased after injection of glucagon. Glucagon treatment enhanced 32P incorporation into the alcohol-ether soluble lipids of mitochondria but did not alter the relative distribution of 32P in various phospholipid species.

Keywords: hormone, inorganic phosphate, phospholipids

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Selected References

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