Post-translational regulation of lipoprotein lipase activity in adipose tissue.
Changes in adipose-tissue lipoprotein lipase activity that are independent of protein synthesis were investigated in an incubation system in vitro. Under appropriate conditions at 25 degrees C a progressive increase in the enzyme activity occurs that is energy-dependent. Part of the enzyme is rapidly inactivated when the tissue is incubated with adrenaline or adrenaline plus theophylline. The mechanism of this inactivation appears to be distinct from, and to follow, the activation of the enzyme. A hypothesis is presented to account for the results in terms of an activation of the enzyme during obligatory post-translational processing and a catecholamine-regulated inactivation of the enzyme as an alternative to secretion from the adipocyte.
D000273:Adipose Tissue / Q000166:cytology / Q000187:drug effects / Q000201:enzymology*; D000818:Animals; D003513:Cycloheximide / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D004837:Epinephrine / Q000494:pharmacology; D066298:In Vitro Techniques; D007700:Kinetics; D008071:Lipoprotein Lipase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D008297:Male; D051381:Rats; D013806:Theophylline / Q000494:pharmacology; D014475:Uncoupling Agents / Q000494:pharmacology
D014475:Uncoupling Agents; D003513:Cycloheximide; D013806:Theophylline; D008071:Lipoprotein Lipase; D004837:Epinephrine