Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.1.34 (lipoprotein lipase)
 7,025 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Previous studies have demonstrated that in vitro treatment of adipocytes with catecholamines results in a decrease in the activity of the enzyme lipoprotein lipase (LPL). To examine the mechanism of this effect, primary cultures of rat adipocytes were cultured in the presence of various concentrations of epinephrine (10(-9)-10(-5) M). Epinephrine yielded a dose-dependent decrease in LPL activity; heparin-releasable LPL activity was reduced to 66% of control values after exposure to 10(-5) M epinephrine for 2 h. However, there was no effect of epinephrine on LPL immunoreactive mass, as measured by enzyme-linked immunosorbent assay. When cells were pulse labeled with [35S]methionine, there was a rapid and dose-dependent decrease in immunoprecipitable LPL. In spite of the decrease in LPL translation, neither epinephrine nor other catecholamines altered the level of LPL mRNA or the rate of LPL transcription. To further examine LPL posttranslational processing, cells were pulse labeled with [35S]methionine in the absence of epinephrine and then chased with unlabeled methionine in the presence of epinephrine. Cells exposed to epinephrine during the chase demonstrated a decrease in LPL secretion into the medium as well as a decrease in LPL degradation. The addition of epinephrine during LPL posttranslational processing did not alter the sensitivity of the newly synthesized LPL protein to endo-beta-N-acetylglucosaminidase-H. Thus, epinephrine had multiple effects on adipocyte LPL. Although there was a rapid decrease in LPL synthesis that was not due to changes in LPL mRNA, the level of LPL protein was unchanged under these conditions due to a decrease in LPL degradation and secretion.(ABSTRACT TRUNCATED AT 250 WORDS)
 ...
PMID:Epinephrine inhibits lipoprotein lipase gene expression in rat adipocytes through multiple steps in posttranscriptional processing. 173 72

Vanadate increased lipoprotein lipase (LPL) activity in the isolated fat pads in a time- and dose-dependent manner. The increasing effect of vanadate was inhibited by amiloride, similar to that of insulin, and it also was not additive to that of insulin. Although the increasing effects of vanadate and insulin were preserved in K(+)-free medium, appreciable decreases in both effects were observed by replacement of Na+ with choline ion or omission of Ca2+ in the medium. Vanadate showed the full effect in the presence of cycloheximide at concentrations that inhibited protein synthesis of the fat pads, suggesting that the action of vanadate is not due to the increase in protein synthesis. Tetrakis (acetoxymethyl) ester of quin 2 at 50 microM concentration never inhibited the action of vanadate though it showed a little inhibition at a concentration of 300 microM. No inhibition of the action of vanadate was observed with ruthenium red. These results suggest that vanadate increases the LPL activity via a process less sensitive to the intracellular Ca2+ concentration. Adrenaline, dibutyryl cyclic AMP, and 3-isobutyl-1-methylxanthine all inhibited the action of vanadate, suggesting that the action is inhibited with increase in the intracellular concentration of cyclic AMP. Monensin and carbonyl cyanide m-chlorophenylhydrazone inhibited the action of vanadate. In contrast, the action of insulin was never inhibited by monensin. Tunicamycin and 2-deoxyglucose, at rather high concentrations, inhibited both actions. These findings suggest that vanadate increases the LPL activity through mechanisms of action involving amiloride- and monensin-sensitive pathways dependent on energy.
 ...
PMID:Increasing effect of vanadate on lipoprotein lipase activity in isolated rat fat pads. 216 42

Epinephrine was used to activate the heparin non-releasable lipoprotein lipase (LPL) in the 3 skeletal muscle fiber types of the perfused rat hindlimb. Following a 9 min washout of the capillary-bound lipoprotein lipase, the hindquarter of the rat was perfused with a buffer containing 10 nM of epinephrine. Activity of the residual LPL in soleus, red vastus lateralis, and white vastus lateralis muscles increased 75%, 96%, and 102% respectively, following epinephrine perfusion. These results suggest that skeletal muscle LPL is under hormonal control possibly through protein phosphorylation by cyclic AMP dependent protein kinase.
 ...
PMID:Epinephrine-activation of heparin-nonreleasable lipoprotein lipase in 3 skeletal muscle fiber types of the rat. 281 80

3T3-L1 adipocytes were used to test the hypothesis that hormone-sensitive lipolysis and lipoprotein lipase activity might be regulated in a reciprocal manner. Intracellular lipolysis was stimulated by catecholamine, dibutyryl cAMP, and ACTH, but not by glucagon. The effects of epinephrine on lipolysis were blocked by the beta-antagonist propanolol but not by the alpha-antagonist phentolamine. Hormone-stimulated lipolysis was not changed by acute (45 min) or chronic (2 days) treatment of the cells with insulin whereas the latter treatment augmented lipoprotein lipase activity about fivefold. Epinephrine did not affect the lipoprotein lipase activity of insulin-stimulated cells. Withdrawal of glucose from the medium decreased lipoprotein lipase activity and the effect of epinephrine on lipolysis. Effects of lipolytic agents on activity of lipoprotein lipase were variable and concentration-dependent. Lipoprotein lipase activity was decreased only by concentrations of epinephrine greater than those inducing maximal intracellular lipolysis, and the decrease in activity occurred about 30 min after the increase in glycerol release. There seems to be no relationship between the level of activity of lipoprotein lipase and the maximal rate of hormone-stimulated lipolysis in 3T3-L1 cells. Unlike in adipose tissue and adipocytes of rats, hormone-stimulated lipolysis and lipoprotein lipase activity in murine 3T3-L1 adipocytes appear to be regulated independently.
 ...
PMID:Effect of epinephrine and other lipolytic agents on intracellular lipolysis and lipoprotein lipase activity in 3T3-L1 adipocytes. 301 31

Immunoprecipitations of hepatic lipase from pulse-labeled rat liver have demonstrated that hepatic lipase is synthesized in two distinct molecular weight forms, HL-I (Mr = 51,000) and HL-II (Mr = 53,000). Both forms are immunologically related to purified hepatic lipase, but not to lipoprotein lipase. HL-I and HL-II are also kinetically related and represent different stages of intracellular processing. Glycosidase experiments suggest that HL-I is the high mannose microsomal form of the mature, sialylated HL-II enzyme. Hepatic lipase activity was detected in liver and adrenal gland but was absent in brain, heart, kidney, testes, small intestine, lung, and spleen. The adrenal and liver lipase activities were inhibited in a similar dose-dependent manner by hepatic lipase antiserum. Immunoblot analysis of partially purified adrenal lipase showed an immunoreactive band co-migrating with HL-II at 53,000 daltons which was absent in a control blot treated with preimmune serum. Adrenal lipase and authentic hepatic lipase yielded similar peptide maps, confirming the presence of the lipase in adrenal gland. However, incorporation of L-[35S]methionine into immunoprecipitable hepatic lipase was not detected in this tissue. In addition, Northern blot analysis showed the presence of hepatic lipase mRNA in liver but not adrenal gland. The presence of hepatic lipase in adrenal gland in the absence of detectable synthesis or messenger suggests that hepatic lipase originates in liver and is transported to this extrahepatic site.
 ...
PMID:Synthesis of hepatic lipase in liver and extrahepatic tissues. 332 89

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.
 ...
PMID:Possible role of lipoprotein lipase in the regulation of endogenous triacylglycerols in the rat heart. 617 39

The lipoprotein lipase activity of epididymal fat-bodies from starved rats was measured during incubations at 37 degrees C in vitro. Protein synthesis independent activation of the enzyme, previously observed during incubations at 25 decrease C, also occurs at 37 degrees C. Protein-synthesis-dependent increases in the activity of the enzyme occur in the presence of insulin and are markedly potentiated by glucocorticoids. The effects on the activity of the enzyme of insulin alone, or in the presence of glucocorticoids, are correlated with its effects on total protein synthesis in the tissue. Adrenaline antagonizes the increase in activity of the enzyme brought about by insulin and abolishes the potentiation of insulin action by glucocorticoids. These changes may be due, at least in part, to its stimulation of inactivation of the enzyme in the tissue. It is suggested that changes in adipose-tissue lipoprotein lipase activity that occur with changes in nutritional status in vivo result from the combined effects of changes in plasma insulin and glucocorticoid concentrations.
 ...
PMID:Effects of insulin, glucocorticoids and adrenaline on the activity of rat adipose-tissue lipoprotein lipids. 699 75

After a 5 week period of feeding a cholesterol-rich diet to rabbits, hyperresponders with high plasma cholesterol levels and hyporesponders with low plasma cholesterol levels could be distinguished from normal responders. The response was found to be correlated with the esterase genotype at the Est-2 locus. The increase in total body cholesterol was higher in hyper-than in hyporesponders. In both groups most of the accumulated dietary cholesterol was found in plasma and liver. Adrenal weight and plasma corticosterone levels were more increased in hyper- than in hyporesponders. The cholesterol-rich diet resulted in an augmentation of liver lipase and lipoprotein lipase activities. These lipolytic activities were more increased in hyper- than in the hyporesponders.
 ...
PMID:Genetic and physiological aspects of cholesterol accumulation in hyperresponding and hyporesponding rabbits. 726 98

Epinephrine has effects on both blood flow and metabolism in adipose tissue. To investigate how these effects might interact in vivo, epinephrine was infused into six healthy volunteers at a rate of 25 ng.kg-1.min-1. The rates of action of lipoprotein lipase and hormone-sensitive lipase in adipose tissue were calculated by measurement of arteriovenous differences across subcutaneous abdominal adipose tissue, and adipose tissue blood flow was measured. Epinephrine caused a significant rise in adipose tissue blood flow (P < 0.001), and the net efflux of nonesterified fatty acids (NEFA) from adipose tissue increased significantly (P < 0.05). Most of this efflux could be accounted for by hormone-sensitive lipase-derived NEFA efflux from cells (P < 0.05), but there was also a significant rise in the contribution of lipoprotein lipase-derived NEFA (P < 0.05). We conclude that adipose tissue blood flow plays an important role in the regulation of lipid metabolism, controlling substrate presentation for lipoprotein lipase and also preventing the local accumulation of fatty acids derived from both hormone-sensitive lipase and lipoprotein lipase.
 ...
PMID:Effects of epinephrine infusion on adipose tissue: interactions between blood flow and lipid metabolism. 894 69

Subcutaneous (subc) abdominal and femoral adipose tissue metabolism was studied in sedentary and endurance-trained premenopausal women. Both fat cell weight and lipoprotein lipase (LPL) activity were lower in the subc abdominal depot of trained women compared with controls. Epinephrine- and isoproterenol-stimulated lipolytic responses, as well as the beta-adrenergic sensitivity of subc abdominal adipocytes, were higher in trained than in sedentary women, whereas both the antilipolytic effect of brimonidine (UK-14304) and the alpha 2-adrenoceptor sensitivity were lower in endurance-trained than in sedentary subjects. Maximal lipolysis in the presence of postadrenoceptor agents was also enhanced in subc abdominal adipose cells of trained women compared with sedentary controls. Negative relationships were found between maximal lipolytic responses of subc abdominal fat cells to catecholamines or to postreceptor agents and body fatness as well as abdominal fat distribution indexes. It is concluded that 1) endurance-trained women are characterized by a preferential lipid mobilization from the subc abdominal fat depot, and 2) differences in the metabolic characteristics of subc abdominal adipocytes between trained and sedentary women may involve changes in both LPL activity and the lipolytic cascade that include modifications at receptor and postreceptor levels. However, these alterations appear to be largely resulting from the reduced adipose cell size rather than from exercise training per se.
 ...
PMID:Regional differences in adipose tissue metabolism between sedentary and endurance-trained women. 931 38


1 2 Next >>