Nutritional regulation of lipoprotein lipase in guinea pig tissues.
Glucose transport in guinea pig adipocytes has been shown to be markedly resistant to stimulation by insulin. Lipoprotein lipase is another transport catalyst in adipose tissue which is believed to be regulated by insulin. We have therefore studied how feeding-fasting affects lipoprotein lipase activity in guinea pig tissues. There was an even more marked decrease in adipose tissue lipoprotein lipase activity on fasting in guinea pigs (10-20 fold) than in rats or mice (4-5 fold). In adipocytes, the activity decreased only 2.5-4.5 fold; most of the change was in extracellular lipoprotein lipase. On glucose refeeding, the activity was rapidly restored. In the first 4 hours after glucose administration extracellular lipoprotein lipase activity increased to more than 10 times the amount present in adipocytes. After cycloheximide, lipoprotein lipase activity decreased with a half-life of 22 min. It is concluded that lipoprotein lipase is rapidly produced and turned over in guinea pig adipose tissue, and that the system is quite sensitive to feeding-fasting. In contrast to adipose tissue, there was no significant change in lipoprotein lipase activity in any other tissue on fasting. There was a strong correlation between the activities in heart and diaphragm muscle, but this correlation was independent of feeding-fasting.
D000273:Adipose Tissue / Q000201:enzymology*; D000818:Animals; D002021:Buffers; D003513:Cycloheximide / Q000494:pharmacology; D003902:Detergents / Q000494:pharmacology; D004435:Eating; D005215:Fasting; D006168:Guinea Pigs; D007700:Kinetics; D008071:Lipoprotein Lipase / Q000378:metabolism*; D008099:Liver / Q000201:enzymology; D008168:Lung / Q000201:enzymology; D008297:Male; D051379:Mice; D009132:Muscles / Q000201:enzymology; D009206:Myocardium / Q000201:enzymology; D009928:Organ Specificity; D051381:Rats; D011919:Rats, Inbred Strains; D013045:Species Specificity
D002021:Buffers; D003902:Detergents; D003513:Cycloheximide; D008071:Lipoprotein Lipase