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Your search keyword '"Triacylglycerol Hydrolase"' showing total 6 results
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6 results on '"Triacylglycerol Hydrolase"'

1. The fatty-acid amide hydrolase inhibitor URB597 does not affect triacylglycerol hydrolysis in rat tissues

Author

Clapper, Jason R, Duranti, Andrea, Tontini, Andrea, Mor, Marco, Tarzia, Giorgio, and Piomelli, Daniele

Subjects
Pharmacology and Pharmaceutical Sciences, Biomedical and Clinical Sciences, Substance Misuse, Development of treatments and therapeutic interventions, 5.1 Pharmaceuticals, Adipose Tissue, White, Amidohydrolases, Animals, Benzamides, Brain, Carbamates, Enzyme Inhibitors, Hydrolysis, Liver, Male, Myocardium, Rats, Rats, Wistar, Triglycerides, Triolein, URB597, anandamide, fatty-acid amide hydrolase, triacylglycerol hydrolase, Pharmacology & Pharmacy, Pharmacology and pharmaceutical sciences
Abstract

The O-arylcarbamate URB597 (cyclohexylcarbamic acid 3'-carbamoylbiphenyl-3-yl ester; also referred to as KDS-4103) is a potent inhibitor of fatty-acid amide hydrolase (FAAH), an intracellular serine hydrolase responsible for the inactivation of the endogenous cannabinoid anandamide. URB597 demonstrates a remarkable degree of selectivity for FAAH over other serine hydrolases (e.g. cholinesterases) or other components of the endocannabinoid system (e.g. cannabinoid receptors). However, in a proteomic-based selectivity screen based on the displacement of fluorophosphonate-rhodamine (FPR) from mouse brain proteins, it was recently shown that URB597 prevents FPR binding to triacylglycerol hydrolase (TGH) with a median inhibitory concentration of 192nM. To determine whether this effect correlates with inhibition of TGH activity, we investigated the ability of URB597 to inhibit triolein hydrolysis in rat liver and heart tissues, which are rich in TGH, as well as white adipose tissue (WAT), which is rich in adipose triacylglycerol lipase (TGL) and hormone-sensitive lipase. The results show that URB597 does not affect triolein hydrolysis in any of these tissues at concentrations as high as 10microM, whereas it inhibits FAAH activity at low nanomolar concentrations. Moreover, intraperitoneal (i.p.) administration of URB597 at doses that maximally inhibit FAAH in vivo (0.3-3mgkg(-1)) exerts no effect on triolein hydrolysis and tissue triacylglycerol (TAG) levels in rat liver, heart or WAT. The results indicate that URB597, while potent at inhibiting FAAH, does not affect TGH and TGL activities in rat tissues.

Published
2006

2. Study on the Characteristics of Tissue Expression of Hormone Sensitive Lipase and Triacylglycerol Hydrolase in Pigs

Author

Qi Wang, Li-Hong Zhang, Li-Jie Zhang, and Gongshe Yang

Subjects
Male, Kidney, medicine.medical_specialty, Lung, medicine.diagnostic_test, Swine, food and beverages, Spleen, Hormone-sensitive lipase, Triacylglycerol Hydrolase, Lipase, Sterol Esterase, Biology, medicine.anatomical_structure, Endocrinology, Gene Expression Regulation, Tissue expression, Western blot, Internal medicine, medicine, Animals, General Earth and Planetary Sciences, Tissue Distribution, Gene, General Environmental Science
Abstract

In this study, the specific expression of TGH and HSL genes in different tissues of Bamei pig was investigated by RT-PCR and Western blot. The result of RT-PCR showed that the expression of HSL could be detected in all these seven tissues examined, which was higher expressed in fat, lower in heart, liver, lung, spleen and kidney. Expression of TGH gene could also be detected in seven tissues, and higher in liver and fat, lower in heart and kidney and lowest in spleen and lung. The result of Western blot showed that, HSL gene was highest expressed in epiploica fat and subcutaneous fat, higher in other tissues, but could not be detected in kidney. Expression of TGH was detected in epiploica fat, subcutaneous fat, liver, lung and spleen, and highest in fat and liver, but it had not been found in heart and kidney. These results suggested that both HSL and TGH could be regulated by post-transcriptional, and their function was involved in different tissues.

Published
2007
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3. The physiological role of triacylglycerol hydrolase in lipid metabolism

Author

Richard Lehner and Dean Gilham

Subjects
medicine.medical_specialty, Very low-density lipoprotein, Apolipoprotein B, Arteriosclerosis, Endocrinology, Diabetes and Metabolism, Lipolysis, Lipoproteins, Lipoproteins, VLDL, Gene Expression Regulation, Enzymologic, Endocrinology, Internal medicine, Diabetes mellitus, medicine, Animals, Humans, Triglycerides, biology, Chemistry, Triacylglycerol Hydrolase, Lipid metabolism, Lipase, medicine.disease, Lipid Metabolism, Adipose Tissue, Liver, biology.protein, Cholesterol Esters
Published
2004

5. The relationship between cholesterol ester hydrolase and triacyglycerol hydrolase from bovine adrenal cortex

Author

Fook-Thean Lee, Stephen J. Yeaman, and Kenneth G. Cook

Subjects
Chemistry, Biophysics, Triacylglycerol Hydrolase, Cell Biology, Lipase, Cholesterol ester hydrolase, Sterol Esterase, Biochemistry, Phenylmethylsulfonyl Fluoride, Kinetics, medicine.anatomical_structure, Structural Biology, Cortex (anatomy), Genetics, medicine, Adrenal Cortex, Chromatography, Gel, Animals, Bovine adrenal, Cattle, Molecular Biology, Carboxylic Ester Hydrolases
Published
1980

6. Differential release of hepatic lipolytic activities

Author

M.C. Oerlemans, W.C. Hülsmann, and Hans Jansen

Subjects
Male, Biophysics, Biochemistry, Phospholipase A1, Hydrolase, Animals, Hepatectomy, Molecular Biology, Triglycerides, chemistry.chemical_classification, Antiserum, Immunoassay, Heparin, Lipid Mobilization, Triacylglycerol Hydrolase, Cell Biology, Lipase, Molecular biology, Monoacylglycerol Lipases, Rats, Monoacylglycerol lipase, Perfusion, Kinetics, Liver lipase, Enzyme, chemistry, Liver, Phospholipases, Rat liver, lipids (amino acids, peptides, and proteins), Carboxylic Ester Hydrolases
Abstract

Summary Perfusion of rat liver with a heparin-containing medium results in a release of upto 95% of the total neutral (or alkaline) triacylglycerol hydrolase activity (EC 3.1.1.3). Of the monoacylglycerol hydrolase (EC 3.1.1.23), phospholipase A1 (EC 3..1.1.32) and palmitoyl-CoA hydrolase (EC 3.1.2.2) activities only 17 to 4% were found to be heparin-releasable. Antiserum raised against heparin-releasable liver lipase inhibits triacylglycerol hydrolase, monoacylglycerol hydrolase, palmitoyl-CoA hydrolase and phospholipase A1 activities in perfusates of isolated livers completely. Non-heparin-releasable monoacylglycerol hydrolase, palmitoyl-CoA hydrolase and phospholipase A1 activities are not inhibited by the antiserum and are therefore catalyzed by different enzyme(s). The difference in substrate specificities of releasable and nonreleasable liver enzymes is discussed in relation to their possible function in lipoprotein metabolism.

Published
1977

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