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Mi Kyeong Lee - One of the best experts on this subject based on the ideXlab platform.
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Pancreatic Lipase Inhibitory Phthalide Derivatives from the Rhizome of Cnidium officinale
Records of Natural Products, 2016Co-Authors: Ji Yeon Jeong, Seon Beom Kim, Qing Liu, Bang Yeon Hwang, Mi Kyeong LeeAbstract:Pancreatic Lipase plays an important role in the digestion and absorption of fats; it has become a target of interest in the treatment of obesity. Investigations of Pancreatic Lipase inhibitory compounds from Cnidium officinale rhizomes have resulted in the isolation of a new phthalide derivative (1) together with ten known phthalides (2-11). Phthalide derivatives from C. officinale showed mild inhibition against Pancreatic Lipase with 13 56% inhibition at 100 μM. Structure activity relationship suggested that the double bond in the side chain of phthalide increased its inhibitory activity, whereas the addition of hydroxyl moiety to side chain reduced activity. Lineweaver-Burk plot analysis also demonstrated that compound 2 was a noncompetitive inhibitor with an IC50 of 86.4 μM. Taken together, C. officinale and its phthalide constituents might be beneficial for the regulation of obesity through Pancreatic Lipase inhibition.
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Pancreatic Lipase inhibitory constituents from morus alba leaves and optimization for extraction conditions
Bioorganic & Medicinal Chemistry Letters, 2015Co-Authors: Ji Yeon Jeong, Seon Beom Kim, Qing Liu, Bang Yeon Hwang, Jin Woo Lee, Ki Yong Lee, Mi Kyeong LeeAbstract:The leaves of Morus alba (Moraceae) have been traditionally used for the treatment of metabolic diseases including diabetes and hyperlipidemia. Thus, inhibitory effect of M. alba leaves on Pancreatic Lipase and their active constituents were investigated in this study. Twenty phenolic compounds including ten flavonoids, eight benzofurans, one stilbene and one chalcones were isolated from the leaves of M. alba. Among the isolated compounds, morachalcone A (20) exerted strong Pancreatic Lipase inhibition with IC50 value of 6.2 μM. Other phenolic compounds containing a prenyl group showed moderate Pancreatic Lipase inhibition with IC50 value of <50 μM. Next, extraction conditions with maximum Pancreatic Lipase inhibition and phenolic content were optimized using response surface methodology with three-level-three-factor Box-Behnken design. Our results suggested the optimized extraction condition for maximum Pancreatic Lipase inhibition and phenolic content as ethanol concentration of 74.9%; temperature 57.4 °C and sample/solvent ratio, 1/10. The Pancreatic Lipase inhibition and total phenolic content under optimized condition were found to be 58.5% and 26.2 μg GAE (gallic acid equivalent)/mg extract, respectively, which were well matched with the predicted value.
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Pancreatic Lipase inhibitory constituents from Morus alba leaves and optimization for extraction conditions.
Bioorganic & medicinal chemistry letters, 2015Co-Authors: Ji Yeon Jeong, Seon Beom Kim, Qing Liu, Bang Yeon Hwang, Jin Woo Lee, Ki Yong Lee, Mi Kyeong LeeAbstract:The leaves of Morus alba (Moraceae) have been traditionally used for the treatment of metabolic diseases including diabetes and hyperlipidemia. Thus, inhibitory effect of M. alba leaves on Pancreatic Lipase and their active constituents were investigated in this study. Twenty phenolic compounds including ten flavonoids, eight benzofurans, one stilbene and one chalcones were isolated from the leaves of M. alba. Among the isolated compounds, morachalcone A (20) exerted strong Pancreatic Lipase inhibition with IC50 value of 6.2 μM. Other phenolic compounds containing a prenyl group showed moderate Pancreatic Lipase inhibition with IC50 value of
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optimization of Pancreatic Lipase inhibition by cudrania tricuspidata fruits using response surface methodology
Bioorganic & Medicinal Chemistry Letters, 2014Co-Authors: Ji Yeon Jeong, Bang Yeon Hwang, Ki Yong Lee, Mi Kyeong LeeAbstract:Abstract The fruits of Cudrania tricuspidata (Carr.) Bur. (Moraceae) significantly inhibited Pancreatic Lipase, which plays a key role in fat absorption. Optimization of extraction conditions with minimum Pancreatic Lipase activity and maximum yield was determined using response surface methodology with three-level-three-factor Box–Behnken design (BBD). Regression analysis showed a good fit of the experimental data and the optimal condition was obtained as ethanol concentration, 74.5%; temperature 61.9 °C and extraction time, 13.5 h. The Pancreatic Lipase activity and extraction yield under optimal conditions were found to be 65.5% and 54.0%, respectively, which were well matched with the predicted value of 65.8% and 47.1%. Further fractionation of C. tricuspidata extract resulted in the isolation of compound 1 , which was identified as 5,7,4′-trihydroxy-6,8-diprenylisoflavone. It inhibited Pancreatic Lipase activity with IC 50 value of 65.0 μM. HPLC analysis suggested positive correlation between Pancreatic Lipase inhibition and 5,7,4′-trihydroxy-6,8-diprenylisoflavone of C. tricuspidata fruits.
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Inhibitory activity of benzophenones from Anemarrhena asphodeloides on Pancreatic Lipase.
Natural product communications, 2013Co-Authors: Seon Beom Kim, Jong Hoon Ahn, Qing Liu, Bang Yeon Hwang, Mi Kyeong LeeAbstract:Pancreatic Lipase is a key enzyme for lipid absorption by hydrolysis of total dietary fats. Therefore, inhibition of Pancreatic Lipase is suggested to be an effective therapy in the regulation of obesity. The EtOAc-soluble fraction of Anemarrhena asphodeloides rhizomes significantly inhibited Pancreatic Lipase activity as assessed using porcine Pancreatic Lipase as an in vitro assay system. Further fractionation of the EtOAc-soluble fraction of A. asphodeloides led to the isolation of a new benzophenone glycoside, zimoside A (1), together with the eleven known compounds iriflophenone (2), 2,4',6-trihydroxy-4-methoxybenzophenone (3), foliamangiferoside A (4), (2,3-dihydroxy-4-methoxyphenyl)(4-hydroxyphenyl)-methanone (5), 1,4,5,6,-tetrahydroxyxanthone (6), isosakuranetin (7), 4-hydroxybenzoic acid (8), 4-hydroxyacetophenone (9), vanillic acid (10), tyrosol (11) and 5-hydroxymethyl-2-furaldehyde (12). Among the isolated compounds, 3, 5 and 10 showed significant inhibition of Pancreatic Lipase activity.
Robert Verger - One of the best experts on this subject based on the ideXlab platform.
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human Pancreatic Lipase related protein 2 is a galactoLipase
Biochemistry, 2004Co-Authors: Barbara Sias, Robert Verger, Francine Ferrato, Philippe Grandval, Dominique Lafont, Paul Boullanger, Alain De Caro, B Leboeuf, Frédéric CarrièreAbstract:Human Pancreatic Lipase-related protein 2 (HPLRP2) was found to be expressed in the pancreas, but its biochemical properties were not investigated in detail. A recombinant HPLRP2 was produced in insect cells and the yeast Pichia pastoris and purified by cation exchange chromatography. Its substrate specificity was investigated using pH-stat and monomolecular film techniques and various lipid substrates (triglycerides, diglycerides, phospholipids, and galactolipids). Lipase activity of HPLRP2 on trioctanoin was inhibited by bile salts and poorly restored by adding coLipase. In vivo, HPLRP2 therefore seems unlikely to show any Lipase activity on dietary fat. In human Pancreatic Lipase (HPL), residues R256, D257, Y267, and K268 are involved in the stabilization of the open conformation of the lid domain, which interacts with coLipase. These residues are not conserved in HPLRP2. When the corresponding mutations (R256G, D257G, Y267F, and K268E) are introduced into HPL, the effects of coLipase are drastically reduced in the presence of bile salts. This may explain why coLipase has such weak effects on HPLRP2. HPLRP2 displayed a very low level of activity on phospholipid micelles and monomolecular films. Its activity on monogalactosyldiglyceride monomolecular film, which was much higher, was similar to the activity of guinea pig Pancreatic Lipase related-protein 2, which shows the highest galactoLipase activity ever measured. The physiological role of HPLRP2 suggested by the present results is the digestion of galactolipids, the most abundant lipids occurring in plant cells, and therefore, in the vegetables that are part of the human diet.
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Human Pancreatic Lipase: CoLipase Dependence and Interfacial Binding of Lid Domain Mutants†
Biochemistry, 1999Co-Authors: Sofiane Bezzine, Robert Verger, Francine Ferrato, Margarita G. Ivanova, Véronique Lopez, Frédéric CarrièreAbstract:Five key amino acid residues from human Pancreatic Lipase (HPL) are mutated in some Pancreatic Lipase-related proteins 2 (PLRP2) that are not reactivated by coLipase in the presence of bile salts. ...
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Molecular evolution of the Pancreatic Lipase and two related enzymes towards different substrate selectivities
Journal of Molecular Catalysis B: Enzymatic, 1997Co-Authors: Frédéric Carrière, Sofiane Bezzine, Robert VergerAbstract:Abstract The Pancreatic Lipase gene family includes lipoprotein Lipases, hepatic Lipases, Pancreatic upases, phosphoLipases A1 from vespid venoms, and non-enzymatic proteins from Drosophila . Among the previous enzymes, the classical human Pancreatic Lipase (HPL), the guinea pig Pancreatic Lipase-related protein 2 (GPLRP2) and the phosphoLipase A1 from hornet venom (DolmI) illustrate three steps in the molecular evolution of the Pancreatic Lipase gene family towards different substrate selectivities for triglycerides and phospholipids. Based on the known 3D structure of HPL, sequence alignments and kinetic properties, we compared these three enzymes for a better understanding of their structure-function relationships. Three surface loops surrounding the active site (β5 loop, β9 loop, lid domain) are believed to play an important role in substrate selectivity.
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Pancreatic Lipase-related protein 2 but not classical Pancreatic Lipase hydrolyzes galactolipids
Biochimica et biophysica acta, 1996Co-Authors: Lena Andersson, Mark E. Lowe, Frédéric Carrière, Åke Nilsson, Robert VergerAbstract:Abstract The Pancreatic Lipase family contains three subfamilies, the ‘classical’ Lipases and the Pancreatic Lipase-related proteins 1 (PLRP1) and 2 (PLRP2). Galactolipids are present in membranes of leaves and vegetables and consist of digalactosyldiacylglycerol (DGalDG) monogalactosyldiacylglycerol (MGalDG) and sulfoquinovosyldiacylglycerol (SQDG). These lipids were incubated with PLRP2 from guinea-pig (GPLRP2) and rat (RPLRP2). In the presence of bile salts (DGalDG) was efficiently hydrolyzed by GPLRP2 and, although less efficiently, by RPLRP2 to digalactosylmonoacylglycerol (DGalMG), free fatty acids and water-soluble galactose-containing compounds. Also, MGalDG and SQDG were hydrolyzed by GPLRP2 and RPLRP2. These data suggest a possible role of PLRP2 in the digestion of dietary galactolipids.
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kinetic behaviour of Pancreatic Lipase in five species using emulsions and monomolecular films of synthetic glycerides
Biochimica et Biophysica Acta, 1995Co-Authors: Youssef Gargouri, Abderraouf Bensalah, Isabelle Douchet, Robert VergerAbstract:Abstract In the absence of coLipase and bile salts, using tributyrin emulsions or monomolecular films of dicaprin at low surface pressure, we observed that no significant Lipase activity can be measured with Human Pancreatic Lipase (HuPL), Horse Pancreatic Lipase (HoPL) or Dog Pancreatic Lipase (DPL). Only Porcine Pancreatic Lipase (PPL) and recombinant Guinea Pig Pancreatic Lipase Related Protein of type 2 (r-GPL) hydrolyse pure tributyrin in the absence of any additive, as well as dicaprin films at low surface pressures. The former Lipases may lack enzyme activity because of irreversible interfacial denaturation due to the high energy existing at the tributyrin/water interface and at the dicaprin film surface at low surface pressures. The enzyme denaturation cannot be reflected in the number of disulfide bridges, since all the Pancreatic Lipases tested here contain six disulfide bridges, but behaved very differently at interfaces. We propose to use the surface pressure threshold, as determined using the monomolecular technique, as a criterion for classifying Lipases in terms of their sensitivity to interfacial denaturation.
Frédéric Carrière - One of the best experts on this subject based on the ideXlab platform.
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human Pancreatic Lipase related protein 2 is a galactoLipase
Biochemistry, 2004Co-Authors: Barbara Sias, Robert Verger, Francine Ferrato, Philippe Grandval, Dominique Lafont, Paul Boullanger, Alain De Caro, B Leboeuf, Frédéric CarrièreAbstract:Human Pancreatic Lipase-related protein 2 (HPLRP2) was found to be expressed in the pancreas, but its biochemical properties were not investigated in detail. A recombinant HPLRP2 was produced in insect cells and the yeast Pichia pastoris and purified by cation exchange chromatography. Its substrate specificity was investigated using pH-stat and monomolecular film techniques and various lipid substrates (triglycerides, diglycerides, phospholipids, and galactolipids). Lipase activity of HPLRP2 on trioctanoin was inhibited by bile salts and poorly restored by adding coLipase. In vivo, HPLRP2 therefore seems unlikely to show any Lipase activity on dietary fat. In human Pancreatic Lipase (HPL), residues R256, D257, Y267, and K268 are involved in the stabilization of the open conformation of the lid domain, which interacts with coLipase. These residues are not conserved in HPLRP2. When the corresponding mutations (R256G, D257G, Y267F, and K268E) are introduced into HPL, the effects of coLipase are drastically reduced in the presence of bile salts. This may explain why coLipase has such weak effects on HPLRP2. HPLRP2 displayed a very low level of activity on phospholipid micelles and monomolecular films. Its activity on monogalactosyldiglyceride monomolecular film, which was much higher, was similar to the activity of guinea pig Pancreatic Lipase related-protein 2, which shows the highest galactoLipase activity ever measured. The physiological role of HPLRP2 suggested by the present results is the digestion of galactolipids, the most abundant lipids occurring in plant cells, and therefore, in the vegetables that are part of the human diet.
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Human Pancreatic Lipase: CoLipase Dependence and Interfacial Binding of Lid Domain Mutants†
Biochemistry, 1999Co-Authors: Sofiane Bezzine, Robert Verger, Francine Ferrato, Margarita G. Ivanova, Véronique Lopez, Frédéric CarrièreAbstract:Five key amino acid residues from human Pancreatic Lipase (HPL) are mutated in some Pancreatic Lipase-related proteins 2 (PLRP2) that are not reactivated by coLipase in the presence of bile salts. ...
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Molecular evolution of the Pancreatic Lipase and two related enzymes towards different substrate selectivities
Journal of Molecular Catalysis B: Enzymatic, 1997Co-Authors: Frédéric Carrière, Sofiane Bezzine, Robert VergerAbstract:Abstract The Pancreatic Lipase gene family includes lipoprotein Lipases, hepatic Lipases, Pancreatic upases, phosphoLipases A1 from vespid venoms, and non-enzymatic proteins from Drosophila . Among the previous enzymes, the classical human Pancreatic Lipase (HPL), the guinea pig Pancreatic Lipase-related protein 2 (GPLRP2) and the phosphoLipase A1 from hornet venom (DolmI) illustrate three steps in the molecular evolution of the Pancreatic Lipase gene family towards different substrate selectivities for triglycerides and phospholipids. Based on the known 3D structure of HPL, sequence alignments and kinetic properties, we compared these three enzymes for a better understanding of their structure-function relationships. Three surface loops surrounding the active site (β5 loop, β9 loop, lid domain) are believed to play an important role in substrate selectivity.
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Pancreatic Lipase-related protein 2 but not classical Pancreatic Lipase hydrolyzes galactolipids
Biochimica et biophysica acta, 1996Co-Authors: Lena Andersson, Mark E. Lowe, Frédéric Carrière, Åke Nilsson, Robert VergerAbstract:Abstract The Pancreatic Lipase family contains three subfamilies, the ‘classical’ Lipases and the Pancreatic Lipase-related proteins 1 (PLRP1) and 2 (PLRP2). Galactolipids are present in membranes of leaves and vegetables and consist of digalactosyldiacylglycerol (DGalDG) monogalactosyldiacylglycerol (MGalDG) and sulfoquinovosyldiacylglycerol (SQDG). These lipids were incubated with PLRP2 from guinea-pig (GPLRP2) and rat (RPLRP2). In the presence of bile salts (DGalDG) was efficiently hydrolyzed by GPLRP2 and, although less efficiently, by RPLRP2 to digalactosylmonoacylglycerol (DGalMG), free fatty acids and water-soluble galactose-containing compounds. Also, MGalDG and SQDG were hydrolyzed by GPLRP2 and RPLRP2. These data suggest a possible role of PLRP2 in the digestion of dietary galactolipids.
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Cloning of the classical guinea pig Pancreatic Lipase and comparison with the Lipase related protein 2.
FEBS letters, 1994Co-Authors: Frédéric Carrière, Kenneth Thirstrup, Siv A. Hjorth, Esper BoelAbstract:Starting from total Pancreatic mRNAs, the classical guinea pig Pancreatic Lipase was cloned using rapid amplification of 3' and 5' cDNA ends. Internal oligonucleotide primers were designed from a partial cDNA clone including the region coding for the lid domain. Using this strategy, we did not amplify the cDNA corresponding to the Pancreatic Lipase related protein 2 in which the lid domain is deleted. Amino acid sequences of the classical guinea pig Pancreatic Lipase and the related protein 2 were compared based on the primary and tertiary structures of the classical human Pancreatic Lipase. Their distinct physiological roles are discussed in the light of functional amino acid differences.
Mark E. Lowe - One of the best experts on this subject based on the ideXlab platform.
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Properties and function of Pancreatic Lipase related protein 2.
Biochimie, 2000Co-Authors: Mark E. LoweAbstract:The Lipase gene family includes Pancreatic triglyceride Lipase and two Pancreatic proteins, Pancreatic Lipase related proteins 1 and 2, with strong nucleotide and amino acid sequence homology to Pancreatic triglyceride Lipase. All three proteins have virtually identical three-dimensional structures. Of the Pancreatic triglyceride Lipase homologues, only Pancreatic Lipase related protein 2 has Lipase activity. Like Pancreatic triglyceride Lipase, related protein 2 cleaves triglycerides, but it has broader substrate specificity. Pancreatic Lipase related protein 2 also hydrolyzes phospholipids and galactolipids, two fats that are not substrates for Pancreatic triglyceride Lipase. The rat-related protein 2 also differs from Pancreatic triglyceride Lipase in sensitivity to bile salts and in response to coLipase. Although the pancreas expresses both Lipases, their temporal pattern of expression differs. Pancreatic Lipase-related protein 2 mRNA appears before birth and persists into adulthood, whereas PTL mRNA first appears at the suckling-weanling transition. Additionally, intestinal enterocytes, paneth cells and cultured cytotoxic T-cells express mRNA encoding Pancreatic Lipase related protein 2. A physiological function for Pancreatic Lipase related protein 2 was demonstrated in mice that did not express this protein. Pancreatic Lipase related protein 2 deficient mice malabsorbed fat in the suckling period, but not after weaning. They also had a defect in T-cell mediated cytotoxicity. Thus, Pancreatic Lipase related protein 2 is a Lipase that participates in the cytotoxic activity of T-cells and plays a critical role in the digestion of breast milk fats.
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Pancreatic Lipase-related protein 2 but not classical Pancreatic Lipase hydrolyzes galactolipids
Biochimica et biophysica acta, 1996Co-Authors: Lena Andersson, Mark E. Lowe, Frédéric Carrière, Åke Nilsson, Robert VergerAbstract:Abstract The Pancreatic Lipase family contains three subfamilies, the ‘classical’ Lipases and the Pancreatic Lipase-related proteins 1 (PLRP1) and 2 (PLRP2). Galactolipids are present in membranes of leaves and vegetables and consist of digalactosyldiacylglycerol (DGalDG) monogalactosyldiacylglycerol (MGalDG) and sulfoquinovosyldiacylglycerol (SQDG). These lipids were incubated with PLRP2 from guinea-pig (GPLRP2) and rat (RPLRP2). In the presence of bile salts (DGalDG) was efficiently hydrolyzed by GPLRP2 and, although less efficiently, by RPLRP2 to digalactosylmonoacylglycerol (DGalMG), free fatty acids and water-soluble galactose-containing compounds. Also, MGalDG and SQDG were hydrolyzed by GPLRP2 and RPLRP2. These data suggest a possible role of PLRP2 in the digestion of dietary galactolipids.
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RAT GP-3 IS A Pancreatic Lipase WITH KINETIC PROPERTIES THAT DIFFER FROM COLipase-DEPENDENT Pancreatic Lipase
Journal of lipid research, 1995Co-Authors: M L Jennens, Mark E. LoweAbstract:The pancreas contains three homologous pro- teins, coLipase-dependent Pancreatic Lipase (PL) and two re- cently described Pancreatic Lipase-related proteins, PLRPl and PLRP2. Rat (r) PLRP2 was first identified as a zymogen granule membrane protein, GP-3. Subsequently, we showed that rPLRP2 could cleave fatty acids from triglycerides, but the kinetic properties of rPLRP2 have not been further inves- tigated. To further characterize rPLRP2, we expressed the recombinant enzyme in a baculovirus system, purified the secreted protein, and measured its kinetic properties. rPLRP2 had a broad pH optimum and the curve was similar to that of rPL. At pH 7.5, rPLRP2 cleaved short, medium, and long chain triglycerides by a kinetic mechanism that did not include interfacial activation. The activity against these sub- strates was not affected by bile salts. In particular, rPLRP2 did not show the bile salt inhibition typical of PL. Although coLipase increased rPLRP2 activity in the presence of bile salts, the increase was only 2- to 5-fold compared to the absolute requirement for coLipase that rPL had under these conditions. Finally, rPLRP2 could hydrolyze phospholipids, a substrate poorly hydrolyzed by PL. p~ Our characterization of rPLRP2 demonstrates clear differences among the kinetic properties of rPLRP2 and rPL, rPLRP2, and PLRP2 homo- logues isolated from guinea pig and coypu pancreas. These findings have important implications for the physiological function of rPLRPB.-Jennens, M. L., and M. E. Lowe. Rat GP-3 is a Pancreatic Lipase with kinetic properties that differ from coLipasedependent Pancreatic 1ipase.J. Lipid Res. 1995. 36: 2374-2382.
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The catalytic site residues and interfacial binding of human Pancreatic Lipase.
The Journal of biological chemistry, 1992Co-Authors: Mark E. LoweAbstract:In this study, the essential serine residue and 2 other amino acids in human Pancreatic triglyceride Lipase (triacylglycerol acylhydrolase, EC 3.1.1.3) were tested for their contribution to the enzyme's catalytic site or interfacial binding site. By site-specific mutagenesis of the cDNA for human Pancreatic Lipase, amino acid substitutions were made at Ser153, His264, and Asp177. The mutant cDNAs were expressed in transfected COS-1 cells. Both the medium and the cells were examined for the presence of Pancreatic Lipase by Western blot analysis. The activity of the expressed proteins against triolein and the interfacial binding was measured. Proteins with mutations in Ser153 were secreted by the cells and bound to interfaces but had no detectable activity. Changing His264 to a leucine or Asp177 to an asparagine also produced inactive Lipase. Substituting glutamic acid for Asp177 produced an active protein. These results demonstrate that Ser153 is involved in the catalytic site of Pancreatic Lipase and is not crucial for interfacial binding. Moreover, the essential roles of His264 and Asp177 in catalysis were demonstrated. A Ser-His-Asp catalytic triad similar to that present in serine proteases is present in human Pancreatic Lipase.
Jungin Kim - One of the best experts on this subject based on the ideXlab platform.
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Pancreatic Lipase inhibitory activity of taraxacum officinale in vitro and in vivo
Nutrition research and practice, 2008Co-Authors: Jian Zhang, Minjung Kang, Myung Jin Kim, Mi Eun Kim, Ji Hyun Song, Young Min Lee, Jungin KimAbstract:Obesity has become a worldwide health problem. Orlistat, an inhibitor of Pancreatic Lipase, is currently approved as an anti-obesity drug. However, gastrointestinal side effects caused by Orlistat may limit its use. In this study the inhibitory activities of dandelion (Taraxacum officinale) against Pancreatic Lipase in vitro and in vivo were measured to determine its possible use as a natural anti-obesity agent. The inhibitory activities of the 95% ethanol extract of T. officinale and Orlistat were measured using 4-methylumbelliferyl oleate (4-MU oleate) as a substrate at concentrations of 250, 125, 100, 25, 12.5 and 4 microg/ml. To determine Pancreatic Lipase inhibitory activity in vivo, mice (n=16) were orally administered with corn oil emulsion (5 ml/kg) alone or with the 95% ethanol extract of T. officinale (400 mg/kg) following an overnight fast. Plasma triglyceride levels were measured at 0, 90, 180, and 240 min after treatment and incremental areas under the response curves (AUC) were calculated. The 95% ethanol extract of T. officinale and Orlistat, inhibited, porcine Pancreatic Lipase activity by 86.3% and 95.7% at a concentration of 250 microg/ml, respectively. T. officinale extract showed dose-dependent inhibition with the IC(50) of 78.2 microg/ml. A single oral dose of the extract significantly inhibited increases in plasma triglyceride levels at 90 and 180 min and reduced AUC of plasma triglyceride response curve (p
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Pancreatic Lipase inhibitory activity of taraxacum officinale in vitro and in vivo
Nutrition Research and Practice, 2008Co-Authors: Jian Zhang, Minjung Kang, Myung Jin Kim, Mi Eun Kim, Ji Hyun Song, Young Min Lee, Jungin KimAbstract:Obesity has become a worldwide health problem. Orlistat, an inhibitor of Pancreatic Lipase, is currently approved as an anti-obesity drug. However, gastrointestinal side effects caused by Orlistat may limit its use. In this study the inhibitory activities of dandelion (Taraxacum officinale) against Pancreatic Lipase in vitro and in vivo were measured to determine its possible use as a natural anti-obesity agent. The inhibitory activities of the 95% ethanol extract of T. officinale and Orlistat were measured using 4-methylumbelliferyl oleate (4-MU oleate) as a substrate at concentrations of 250, 125, 100, 25, 12.5 and 4 microg/ml. To determine Pancreatic Lipase inhibitory activity in vivo, mice (n=16) were orally administered with corn oil emulsion (5 ml/kg) alone or with the 95% ethanol extract of T. officinale (400 mg/kg) following an overnight fast. Plasma triglyceride levels were measured at 0, 90, 180, and 240 min after treatment and incremental areas under the response curves (AUC) were calculated. The 95% ethanol extract of T. officinale and Orlistat, inhibited, porcine Pancreatic Lipase activity by 86.3% and 95.7% at a concentration of 250 microg/ml, respectively. T. officinale extract showed dose-dependent inhibition with the IC(50) of 78.2 microg/ml. A single oral dose of the extract significantly inhibited increases in plasma triglyceride levels at 90 and 180 min and reduced AUC of plasma triglyceride response curve (p<0.05). The results indicate that T. officinale exhibits inhibitory activities against Pancreatic Lipase in vitro and in vivo. Further studies to elucidate anti-obesity effects of chronic consumption of T. officinale and to identify the active components responsible for inhibitory activity against Pancreatic Lipase are necessary.
