Drugs online research references
Int J Obes Relat Metab Disord. 1994 Sep;18(9):648-9.
Effects of weight reduction programs on close family members.
Franson K, Rossner S.
Obesity Unit, Karolinska Hospital, Stockholm.
Ninety-two patients in long-term treatment for obesity completed a questionnaire on the weight development of their close family members. Of 47 such relatives, 37 had lost a mean of 6.1 kg and 10 increased a mean of 5.1 kg. Treatment of obesity will affect many more than those taking part in the actual program and generally result in weight loss. This effect on family members was mostly considered beneficial.
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=7812420&dopt=Abstract
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Biochim Biophys Acta. 1995 Feb 9;1254(3):311-8.
Characterization of a partially purified diacylglycerol lipase from bovine aorta.
Lee MW, Kraemer FB, Severson DL.
MRC Signal Transduction Group, Faculty of Medicine, University of Calgary, Alberta, Canada.
A partially-purified diacylglycerol (DG) lipase from bovine aorta has been characterized with respect to the effects of lipid metabolites and two lipase inhibitors, phenylboronic acid and tetrahydrolipstatin (THL). DG lipase activity was determined by the hydrolysis of the sn-1 position of 1-[1-14C]palmitoyl-2-oleoyl-sn-glycerol. The products of the lipase reaction, 2-monoacylglycerol (2-monoolein) and non-esterified fatty acids (oleate, archidonate) produced a concentration-dependent (20-200 microM) inhibition of DG lipase activity. Oleoyl-CoA and dioleoylphosphatidic acid also inhibited aortic DG lipase activity, but lysophosphatidylcholine had little or no effect. The inhibition of aortic DG lipase by phenylboronic acid was competitive, with a Ki of approx. 4 mM. THL was a very potent inhibitor of aortic DG lipase; the concentration required for inhibition to 50% of control was 2-6 nM. THL inhibition was reduced when the concentration of substrate in the assay was increased. Attempts to identify the aortic DG lipase by covalent-labelling with [14C]THL were unsuccessful. Immunoblotting experiments revealed that hormone-sensitive triacylglycerol lipase (HSL) could not be detected in bovine aorta.
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=7857971&dopt=Abstract
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Eur J Biochem. 1994 Jun 1;222(2):395-403.
Interactions of lipoprotein lipase with the active-site inhibitor tetrahydrolipstatin (Orlistat).
Lookene A, Skottova N, Olivecrona G.
Department of Medical Biochemistry and Biophysics, University of Umea, Sweden.
Lipoprotein lipase (LPL) was rapidly inactivated by low concentrations of the active-site inhibitor tetrahydrolipstatin (THL). The presence of amphiphils (e.g. long-chain fatty acids) or of lipid/water interfaces (lipid emulsions) was required for inhibition to occur. Apolipoprotein CII increased the maximal inactivation rate constant by 1.8-fold in the presence of an emulsion of long-chain triacylglycerols, but had no effect in the presence of an emulsion of tributyrylglycerol. The fully inhibited enzyme had a ratio of THL/LPL of nearly 2, indicating that both subunits of the LPL homo-dimer bound THL. The THL-LPL complex was stable below pH 7.5. At higher pH reactivation occurred indicating that THL was slowly turned over by the enzyme. The apparent reactivation rate constant was increased about threefold by the presence of lipid/water interfaces. Sucrose density gradient centrifugation revealed that THL induces tetramerisation of LPL. This aggregation was reversible on reactivation of the inhibited enzyme. Binding to heparin was not affected by THL. In contrast, binding to lipid droplets and to lipoproteins was increased, indicating exposure of hydrophobic regions in the inhibited LPL. It is suggested that THL induces local conformational changes in LPL, which may involve opening of the putative surface lid structure which covers the active-site.
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=8020477&dopt=Abstract
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