期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1970
卷号：67
期号：1
页码：290-295
DOI：10.1073/pnas.67.1.290
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.
