scholarly journals Possible role of lipoprotein lipase in the regulation of endogenous triacylglycerols in the rat heart

1981 ◽  
Vol 198 (1) ◽  
pp. 159-166 ◽  
Author(s):  
W K Palmer ◽  
R A Caruso ◽  
L B Oscai

1. Adrenaline has a biphasic effect on intracellular lipoprotein lipase activity and on endogenous triacylglycerol content in heparin-perfused heart. 2. A high concentration of adrenaline (1 microM in the perfusion buffer) activated endogenous lipoprotein lipase activity and, at the same time, decreased intracellular triacylglycerol stores. 3. In contrast, a low concentration (0.005 microM-adrenaline) inhibited intracellular lipoprotein lipase activity. Under these conditions, cardiac triacylglycerol content was elevated above control values. 4. Perfusing the heart with high and low concentrations of 3-isobutyl-1-methylxanthine elicited a biphasic effect on endogenous lipoprotein lipase activity and triacylglycerol content similar to that seen with adrenaline treatment. 5. The effect of adrenaline on intracellular lipoprotein lipase activity appears to be mediated by cyclic AMP through protein kinase. 6. A possible role for intracellular lipoprotein lipase in the regulation of endogenous triacylglycerol in rat heart is proposed.

1988 ◽  
Vol 255 (3) ◽  
pp. E247-E254 ◽  
Author(s):  
T. Chajek-Shaul ◽  
G. Bengtsson-Olivecrona ◽  
J. Peterson ◽  
T. Olivecrona

When isolated rat hearts were perfused with medium containing 125I-labeled bovine lipoprotein lipase (LPL), they bound both lipase activity and radioactivity. More than 80% of the bound lipase could be rapidly released by heparin. Low concentrations of bovine LPL displaced 50-60% of the endogeneous, endothelial-bound LPL. Higher concentrations caused additional binding. Both binding and exchange were rapid processes. The hearts continuously released endogenous LPL into the medium. An antiserum that inhibited bovine but not rat LPL was used to differentiate endogeneous and exogeneous LPL activity. When the pool of endothelial LPL was labeled with bovine 125I-labeled LPL and then chased with unlabeled bovine LPL, approximately 50% of the labeled lipase was rapidly displaced. During chase perfusion with medium only, catalytically active bovine LPL appeared in the perfusate. The rate of release was similar to that observed for endogeneous LPL activity and amounted to 10-13% of the heparin-releasable fraction in the first 5 min of perfusion. There was little or no degradation of bovine 125I-labeled LPL to fragments or acid-soluble products. These results indicate that endothelial LPL is accessible for exchange with exogeneous LPL and that detachment rather than degradation may be the pathway for catabolism of endothelial LPL.


Life Sciences ◽  
1977 ◽  
Vol 21 (3) ◽  
pp. 467-473 ◽  
Author(s):  
Gregory J. Bagby ◽  
Maw-Shung Liu ◽  
Judy A. Spitzer

1975 ◽  
Vol 7 (02) ◽  
pp. 152-157 ◽  
Author(s):  
P. de Gasquet ◽  
E. Pequignot-Planche ◽  
N. Tonnu ◽  
F. Diaby

1991 ◽  
Vol 41 (12) ◽  
pp. 2005-2009 ◽  
Author(s):  
Elisabeth Sévilla ◽  
Annick Valette ◽  
Marguerite Gastaldi ◽  
Jean Boyer ◽  
Alain Vérine

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