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The functional status of lipoprotein lipase in rat liver.

ABSTRACT: 1. Acetone-dried powders of liver and heart tissues from rats given a high-carbohydrate diet or a fat meal were assayed for lipoprotein lipase activity. Heart tissue showed typical lipoprotein lipase activity, whereas none was detected in liver by the usual assay procedures. 2. When mixed acetone-dried powders were prepared from heart plus liver, there was a marked suppression of the expected activity, indicating that an inhibitor was present in the liver. This inhibition was partially overcome in the presence of relatively large amounts of heparin. 3. Lipoprotein lipase was also detected in liver alone when large quantities of heparin were added to the assay system. 4. No increase in lipoprotein lipase activity in either liver or heart was detected when rats were given a fat meal. 5. It is concluded that the liver of the rat contains lipoprotein lipase that is normally present in an inactive state. The results imply that a heparinase is the agent responsible for the inactivation. 6. The significance of the non-functional status of lipoprotein lipase in the liver is discussed. The results support the view that direct hydrolysis of plasma triglycerides by the liver is not a significant physiological process.

SUBMITTER: Mayes PA

PROVIDER: S-EPMC1198834 | biostudies-other | 1968 Jul

REPOSITORIES: biostudies-other

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Project description:Lipoprotein lipase (LPL) is responsible for the intravascular catabolism of triglyceride-rich lipoproteins and plays a central role in whole-body energy balance and lipid homeostasis. As such, LPL is subject to tissue-specific regulation in different physiological conditions, but the mechanisms of this regulation remain incompletely characterized. Previous work revealed that LPL comprises a set of proteoforms with different isoelectric points, but their regulation and functional significance have not been studied thus far. Here we studied the distribution of LPL proteoforms in different rat tissues and their regulation under physiological conditions. First, analysis by two-dimensional electrophoresis and Western blot showed different patterns of LPL proteoforms (i.e., different pI or relative abundance of LPL proteoforms) in different rat tissues under basal conditions, which could be related to the tissue-specific regulation of the enzyme. Next, the comparison of LPL proteoforms from heart and brown adipose tissue between adults and 15-day-old rat pups, two conditions with minimal regulation of LPL in these tissues, yielded virtually the same tissue-specific patterns of LPL proteoforms. In contrast, the pronounced down-regulation of LPL activity observed in white adipose tissue during fasting is accompanied by a prominent reconfiguration of the LPL proteoform pattern. Furthermore, refeeding reverts this down-regulation of LPL activity and restores the pattern of LPL proteoforms in this tissue. Importantly, this reversible proteoform-specific regulation during fasting and refeeding indicates that LPL proteoforms are functionally diverse. Further investigation of potential differences in the functional properties of LPL proteoforms showed that all proteoforms exhibit lipolytic activity and have similar heparin-binding affinity, although other functional aspects remain to be investigated. Overall, this study demonstrates the ubiquity, differential distribution and specific regulation of LPL proteoforms in rat tissues and underscores the need to consider the existence of LPL proteoforms for a complete understanding of LPL regulation under physiological conditions.

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The functional status of lipoprotein lipase in rat liver.

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