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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1970 Sep;67(1):290–295. doi: 10.1073/pnas.67.1.290

ATP-Dependent and Cyclic AMP-Dependent Activation of Rat Adipose Tissue Lipase by Protein Kinase from Rabbit Skeletal Muscle*

Jussi K Huttunen 1,, Daniel Steinberg 1, Steven E Mayer 1
PMCID: PMC283201  PMID: 4318780

Abstract

Brief incubation of partially purified preparations of hormone-sensitive lipase from rat epididymal fat pads with ATP, Mg++, cyclic adenosine 3′:5′-monophosphate and rabbit muscle protein kinase (phosphorylase b kinase kinase) resulted in enhancement of lipolytic activity (44-93%). Little or no activation was observed when either the cofactor mixture or the protein kinase was omitted. When the fat pads were incubated with epinephrine prior to homogenization, addition of kinase and cofactors to the soluble supernatant fraction caused no activation whereas good activation was obtained in preparations from paired fat pads not exposed to epinephrine. The results indicate that the cyclic AMP-mediated activation of hormone-sensitive lipase in adipose tissue involves a protein phosphorylation step. Whether the lipase itself is phosphorylated and thus activated or whether the protein kinase is activating a mediating enzyme, in analogy with its action in the glycogen phosphorylase system, remains to be determined.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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