Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.1.79 (hormone-sensitive lipase)
 2,163 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

To determine whether the estrogen-induced hyperlipidemia is affected by fasting, male growing chicks were administered subcutaneously a single dose of 17 beta-estradiol (25 mg/kg body wt), and the hormone treatment lasted for 2 days with or without feed (Experiment 1). In the second experiment, chicks were initially fasted for 1 or 3 days, and then treated with the same dosage of 17 beta-estradiol as in Experiment 1 for 2 days without feed. Plasma and liver lipids, and the activities of hepatic malic enzyme, glucose-6-phosphate dehydrogenase, and hormone-sensitive lipase in the adipose tissue were determined. Compared with fed control chicks, estrogen treatment in fed birds resulted in a marked elevation of plasma lipids, especially triglyceride during the 2-day period (137 vs 2263 mg/dl). In fasted chicks, the present finding that estrogen also induced a marked hyperlipidemia is noteworthy. Upon estrogen treatment (Experiment 1), the level of plasma triglyceride in fasted birds increased about 16 times over that of the fasted control group (133 vs 2093 mg/dl). Even in chicks fasted for 5 days (Experiment 2), estrogen treatment resulted in a persistent hypertriglyceridemia (75 vs 1369 mg/dl). In fed chicks, estrogen treatment also induced a fatty liver with massive accumulation of triglyceride, but the liver of estrogen-treated/fasted chicks appeared to be normal. In both fed and fasted chicks, malic enzyme was found to be the major NADPH producing enzyme in the liver. Upon fasting, both malic enzyme and glucose-6-phosphate dehydrogenase activities decreased significantly (P less than 0.05). In fed chicks, the total activities of both enzymes increased with estrogen treatment, whereas the effect of hormone on these enzymes was less obvious in fasted chicks. The hormone-sensitive lipase activity in the adipose tissue was much lower in fed chicks compared with that of fasted birds (0.15 vs 0.33 nmol of oleic acid released/min/mg protein). Estrogen treatment in fed chicks had no effect on the hormone-sensitive lipase activity, but its activity was enhanced by the hormone treatment in fasted chicks. The present finding that hyperlipidemia persisted in estrogenized chicks during the fasting seems to indicate the complex nature of this hormonal influence on lipid metabolism.
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PMID:Estrogen induces hyperlipidemia in fasted chicks. 230 May 91

We have previously produced and tested a liposome preparation based on hydrogenated soy lecithin (HSL-L) for the purpose of designing blood replacement in the form of liposome encapsulated hemoglobin (LEH). While these liposomes had acceptable physicochemical properties which addressed many of the desirable characteristics of "artificial blood," they produced hypotension, hemoconcentration, and thrombocytopenia when administered to rats. The following studies present improved synthetic distearoyl phosphatidylcholine-based liposomes (sDSPC-L) which were compared to the HSL-L for their biological effects in the conscious normovolemic rat (n = 6 - 11). HSL-L induced hypotension (-25 +/- 3 mmHg, P less than 0.01), tachycardia (+88 +/- 11 beats/min, P less than 0.01), decrease in cardiac index (-33 +/- 4%, P less than 0.01), and elevation of the total peripheral resistance index (+0.450 +/- 0.003 mmHg/ml/min/kg, P less than 0.01). The hematologic responses to HSL-L were: leukocytosis (+6,070 +/- 1,064/microliters, P less than 0.01), hemoconcentration (+4.0 +/- 0.1%, P less than 0.01), 0.01), and thrombocytopenia (-160 +/- 18 X 10(3)/microliters, P less than 0.01). Plasma thromboxane B2 (TXB2) was elevated to 30.4 +/- 5.6 pg/100 microliters (P less than 0.01). In contrast, the only effects induced by sDSPC-L were slight tachycardia (+37 +/- 9 beats/min, P less than 0.05) and a marginal increase in plasma TXB2 to 9.7 +/- 3.3 pg/100 microliters (P less than 0.05). All effects, except for those related to cardiac output and peripheral resistance, were transient. These data underscore the importance of pure synthetic DSPC in improving the biological effects of liposomes and suggest sDSPC-L as a promising vehicle for encapsulating hemoglobin.
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PMID:Improved biological properties of synthetic distearoyl phosphatidyl choline-based liposome in the conscious rat. 231 Dec 5

Subcutaneous adipose tissue cell size and density and hormone-sensitive lipase activity were determined during late pregnancy and first lactation in Holstein heifers. Animals were daughters of bulls with either +791 (high line) or +390 (low line) kg Predicted Difference (1974 base) for milk. Each line consumed either a 71%: 29% (high energy) or a 36%:63% (low energy) barley concentrate and alfalfa hay diet from 0 to 140 d lactation. Heifers fed the low energy ration ate 33% less NE1 and produced 20% less milk with 52.7% greater milk fat percentage during 28 to 140 d of lactation than heifers fed the high energy ration. Prepartum, animals of the high line had similar adipocyte volume and density to low line animals. However, during early lactation, high line animals had a greater decrease in volume and a larger increase in density than low line animals. There was a delayed recovery of volume in high line, compared with low line animals in late lactation. Adipocyte volume also was decreased by dietary energy restriction. Hormone-sensitive lipase activity was similar in both genetic lines prepartum and increased in all groups at 60 d postpartum. Animals of high line or fed low energy rations had increased activity per gram during early, but not later, lactation. Activity per cell and per milligram cytoplasm protein increased in all groups in early lactation and were highest in high line animals fed the low energy ration.
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PMID:Regulation of bovine adipose tissue metabolism during lactation. 6. Cellularity and hormone-sensitive lipase activity as affected by genetic merit and energy intake. 234 50

Mammary gland lipase activity of the mouse increased 45-fold compared to that in unmated gland at the 15th day of pregnancy and was 65-fold at the 20th day of pregnancy. After parturition, the activity abruptly decreased during 3 days to 38% of that at the 20th day of pregnancy. On the other hand, only a very small lipoprotein lipase activity was observed in the pregnant gland, the activity increased to 15-fold that of 20 day pregnancy at the 3rd day of lactation. These facts suggest that the mammary epithelial cells (mammary gland lipase activity was detected only in epithelial cells) utilize the fat reserved in the gland during pregnancy, but the lactating mammary epithelial cells utilize the fat supplied from the blood circulation. Mammary gland lipase activity was decreased by treatment with epinephrine which increased the fat mobilization in other adipose tissues. Hydrocortisone and prolactin decreased the mammary gland lipase activity in the glands of pregnancy and lactation. In addition, no hormone-sensitive lipase activity was observed in the mammary gland. Thus, the control of fat mobilization in the mammary gland must be different from that in other adipose tissues.
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PMID:[Changes in lipase activity during pregnancy and lactation in the mouse mammary gland]. 234 21

Transient exposure of cultured 3T3-L1 preadipocytes to hypolipidemic fibrate drugs results in extensive adipocyte conversion. Adipocyte conversion in culture was characterized by an increase in neutral lipids content and in adipocyte marker enzymes like hormone-sensitive lipase and glycerol-3-phosphate dehydrogenase. Adipocyte conversion in culture was also accompanied by induction of cyanide-insensitive peroxisomal palmitoyl-CoA oxidation. The conversion pattern exerted by fibrate drugs in 3T3-L1 cells was similar to that reported previously for primary cultured epididymal preadipocytes (R. Brandes, R. Arad and J. Bar-Tana, Biochim. Biophys. Acta, 877, 314-321 (1986)), and seems to refute clonal selection in the conversion sequel initiated by fibrate drugs in primary cultured preadipocytes.
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PMID:Adipocyte conversion of cultured 3T3-L1 preadipocytes by bezafibrate. 243 18

The present work was aimed at investigation of lipid peroxidation during fasting and its effects upon metabolism of adipose tissue, especially lipolytic activity. An increase in the lipid peroxidation was demonstrated in an animal model (male rats) through accumulation of lipofuscin-like pigments (LFP), the end product of lipid peroxidation. The increased LFP levels correlated with a decrease in the activity of hormone-sensitive lipase. LFP content increased in the plasma, liver and adipose tissue. The time-course of the changes depended on the initial body mass of the animals. Correlations were found between lipolytic activity and LFP content in adipose tissue and in plasma. In the course of the repeated cycles of fasting--feeding, the changes of LFP and lipolysis were antiparallel to each other. During four cycles, there was a net increase in LFP and a net decrease in lipolysis. The lipolytic activity depended on many factors, among which we identified the initial body mass of animals, their age, and the way of feeding. The results obtained in this animal model enable application of the methods used in the investigation of fasting in obese patients.
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PMID:Lipid peroxidation and lipolysis during fasting. 249 Oct 7

Hormone-sensitive lipase is phosphorylated at a single site (site 2) in vitro by the AMP-activated protein kinase, without any direct effect on the activity of the enzyme. The amino acid sequence around this site has been determined. Ca2+/calmodulin-dependent protein kinase II also phosphorylates hormone-sensitive lipase predominantly at this site, whilst cyclic-GMP-dependent protein kinase phosphorylates exclusively the regulatory site (site 1) which is also phosphorylated by cyclic-AMP-dependent protein kinase. Phosphorylation of site 2 has been found to inhibit subsequent phosphorylation and activation of hormone-sensitive lipase by the cyclic-AMP-dependent and cyclic-GMP-dependent protein kinases, indicating that site-2 phosphorylation may have an antilipolytic role in vivo.
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PMID:Phosphorylation of bovine hormone-sensitive lipase by the AMP-activated protein kinase. A possible antilipolytic mechanism. 253

Anti-hormone-sensitive lipase (HSL) immunoglobulin selectively immunoprecipitates a single 84 kDa 32P-phosphoprotein from macrophage homogenates previously phosphorylated by cyclic AMP-dependent protein kinase in the presence of [gamma-32P]ATP-Mg. This immunoglobulin also completely removes the neutral cholesterol ester hydrolase activity from macrophage homogenates. These data demonstrate that HSL is responsible for the neutral cholesterol ester hydrolase activity in macrophages and hence plays a key role in cholesterol metabolism in these cells.
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PMID:Hormone-sensitive lipase is responsible for the neutral cholesterol ester hydrolase activity in macrophages. 254 Oct 13

The mRNA for human hormone-sensitive lipase (HSL) was identified using Northern blot analysis and a cDNA-probe for rat HSL. As in the rat, human adipose tissue expresses a single mRNA species of 3.3 kb. Using Western blotting with a polyclonal rabbit antibody towards rat adipose tissue HSL, the corresponding enzyme in human adipose tissue was identified with an apparent 88 kDa polypeptide, thus slightly larger than the rat and bovine 84 kDa, and the mouse and guinea-pig 82 kDa species. Additional evidence for the identification was provided by the inhibition of HSL diacylglycerol lipase activity by the anti-rat HSL antibody, and by NaF, DFP and Hg2+, known inhibitors of HSL. The concentration of the enzyme, as reflected by its activity per g tissue and the specific activity was about two thirds of that in the rat adipose tissue (200 g rats). The identification of the human enzyme protein made it possible to directly demonstrate its phosphorylation by cAMP-dependent protein kinase, thus extending the previous report regarding activation of the lipase with this kinase and ATP-Mg2+ in human adipose tissue extracts (Khoo, J.C., Aquino, A.A. and Steinberg, D. (1974) J. Clin. Invest. 53, 1124-1131).
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PMID:Human adipose tissue hormone-sensitive lipase: identification and comparison with other species. 255 74

In addition to acetyl-CoA carboxylase and HMG-CoA reductase, the AMP-activated protein kinase phosphorylates glycogen synthase, phosphorylase kinase, hormone-sensitive lipase and casein. A number of other substrates for the cyclic AMP-dependent protein kinase, e.g., L-pyruvate kinase and 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, are not phosphorylated at significant rates. Examination of the sites phosphorylated on acetyl-CoA carboxylase, hormone-sensitive lipase, glycogen synthase and phosphorylase kinase suggests a consensus recognition sequence in which the serine residue phosphorylated by the AMP-activated protein kinase has a hydrophobic residue on the N-terminal side (i.e., at -1) and at least one arginine residue at -2, -3 or -4. Substrates for cyclic AMP-dependent protein kinase which lack the hydrophobic residue at -1 are not substrates for the AMP-activated protein kinase.
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PMID:The substrate and sequence specificity of the AMP-activated protein kinase. Phosphorylation of glycogen synthase and phosphorylase kinase. 256 85


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