These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: ATP-dependent and cyclic AMP-dependent activation of rat adipose tissue lipase by protein kinase from rabbit skeletal muscle.
    Author: Huttunen JK, Steinberg D, Mayer SE.
    Journal: Proc Natl Acad Sci U S A; 1970 Sep; 67(1):290-5. PubMed ID: 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.
    [Abstract] [Full Text] [Related] [New Search]