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PMID: 4337238 Published · ppublish English Journal Article

Glucagon-stimulated phosphorylation of mitochondrial and lysosomal membranes of rat liver in vivo.

Zahlten RN, Hochberg AA, Stratman FW, Lardy HA

Abstract

The pancreatic hormone, glucagon, stimulates the net uptake of inorganic (32)P 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 (32)P incorporation into the alcohol-ether soluble lipids of mitochondria but did not alter the relative distribution of (32)P in various phospholipid species.

MeSH Terms
Amino Acids/analysis Animals Butyrates/pharmacology Chromatography, Paper Cyclic AMP/pharmacology Fasting Glucagon/pharmacology Lipids/analysis Liver/cytology Lysosomes/analysis,metabolism Male Membranes/drug effects,metabolism Mitochondria, Liver/analysis,metabolism Oxidative Phosphorylation/drug effects Phosphates/analysis Phosphorus Isotopes Protein Binding/drug effects Rats Time Factors
Chemicals
Amino Acids Butyrates Lipids Phosphates Phosphorus Isotopes Glucagon Cyclic AMP
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Zahlten R N
Hochberg A A
Stratman F W
Lardy H A
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25 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1972-04-00
Pages
800-4
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC426567
Subset
IM
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