Regulation of adipose-tissue lipolysis by phosphorylation of hormone-sensitive lipase.
Hormone-sensitive lipase has been purified from rat adipose tissue to almost 50 per cent protein purity and partially characterized. The isolated enzyme can be phosphorylated by ATP-Mg2+ in the presence of the catalytic subunit of cyclic AMP-dependent protein kinase from the same tissue. Its activity towards emulsified triglyceride is thereby increased two-fold. The enzyme is phosphorylated also in the intact adipocyte, verifying the physiological relevance of the findings with the isolated enzyme. Noradrenaline causes a rapid increase in phosphorylation of the enzyme in intact adipocytes, immediately followed by a marked increase of its activity. Addition of dibutyryl-cyclic AMP to the adipocytes causes the same effects. The extent of phosphorylation of the enzyme after maximal noradrenaline stimulation of the adipocytes is rapidly decreased by insulin addition in close association with inhibition of the lipase activity. The results demonstrate that these hormones regulate the activity of the hormone-sensitive lipase, ie the rate of lipolysis in the adipocytes, by changes of the degree of phosphorylation of the enzyme.
D000255:Adenosine Triphosphate / Q000502:physiology*; D000273:Adipose Tissue / Q000187:drug effects / Q000378:metabolism*; D000818:Animals; D003994:Bucladesine / Q000494:pharmacology; D066298:In Vitro Techniques; D007328:Insulin / Q000494:pharmacology; D008066:Lipolysis / Q000187:drug effects*; D009638:Norepinephrine / Q000494:pharmacology; D010766:Phosphorylation; D011494:Protein Kinases / Q000502:physiology; D051381:Rats; D002787:Sterol Esterase / Q000378:metabolism*
D007328:Insulin; D003994:Bucladesine; D000255:Adenosine Triphosphate; D011494:Protein Kinases; D002787:Sterol Esterase; D009638:Norepinephrine