Base de dados : MEDLINE
Pesquisa : D12.776.200 [Categoria DeCS]
Referências encontradas : 470 [refinar]
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[PMID]:27449720
[Au] Autor:Kehoe K; Van Elzen R; Verkerk R; Sim Y; Van der Veken P; Lambeir AM; De Meester I
[Ad] Endereço:Laboratory of Medical Biochemistry, Department of Pharmaceutical Sciences, University of Antwerp, Antwerp, Belgium. Electronic address: kaat.kehoe@uantwerpen.be.
[Ti] Título:Prolyl carboxypeptidase purified from human placenta: its characterization and identification as an apelin-cleaving enzyme.
[So] Source:Biochim Biophys Acta;1864(11):1481-8, 2016 11.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Mh] Termos MeSH primário: Carboxipeptidases/química
Peptídeos e Proteínas de Sinalização Intercelular/química
Placenta/química
alfa-MSH/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Apelina
Carboxipeptidases/genética
Carboxipeptidases/isolamento & purificação
Carboxipeptidases/metabolismo
Colipases/química
Colipases/genética
Colipases/metabolismo
Metabolismo Energético/genética
Precursores Enzimáticos/química
Precursores Enzimáticos/genética
Precursores Enzimáticos/metabolismo
Feminino
Expressão Gênica
Grelina/química
Grelina/genética
Grelina/metabolismo
Células Endoteliais da Veia Umbilical Humana
Seres Humanos
Peptídeos e Proteínas de Sinalização Intercelular/genética
Peptídeos e Proteínas de Sinalização Intercelular/metabolismo
Cinética
Placenta/enzimologia
Gravidez
Proteólise
Especificidade por Substrato
alfa-MSH/genética
alfa-MSH/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (APLN protein, human); 0 (Apelin); 0 (Colipases); 0 (Enzyme Precursors); 0 (Ghrelin); 0 (Intercellular Signaling Peptides and Proteins); 0 (obestatin, human); 581-05-5 (alpha-MSH); 72994-53-7 (procolipase); EC 3.4.- (Carboxypeptidases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160725
[St] Status:MEDLINE


  2 / 470 MEDLINE  
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[PMID]:27155582
[Au] Autor:Haque N; Prabhu NP
[Ad] Endereço:Department of Biotechnology & Bioinformatics, School of Life Sciences, University of Hyderabad, Hyderabad 500 046, India.
[Ti] Título:Lid closure dynamics of porcine pancreatic lipase in aqueous solution.
[So] Source:Biochim Biophys Acta;1860(10):2313-25, 2016 10.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Pancreatic lipases hydrolyze fatty acids in dietary pathway. The activity of porcine pancreatic lipase (PPL) is controlled by lid domain along with a coenzyme, colipase. The active open-state conformation of the protein could be induced by detergents or bile salts which would be further stabilized by binding of colipase. In the absence of these interactions, the lid preferably attains a closed conformation in water. METHODS: Molecular dynamic simulation was used to monitor the lid movement of PPL in open and closed conformations in water. Free energy surface was constructed from the simulation. Energy barriers and major structural changes during lid opening were evaluated. RESULTS: The lid closure of PPL in water from its open conformation might be initiated by columbic interactions which initially move the lid away from domain 1. This is followed by major dihedral changes on the lid residues which alter the trajectory of motion. The lid then swirls back towards domain 1 to attain closed conformation. This is accompanied with conformational changes around ß5- and ß9-loops as well. However, PPL in closed conformation shows only the domain movements and the lid remains in its closed conformation. CONCLUSIONS: PPL in closed conformation is stable in water and the open conformation is driven towards closed state. The lid follows a swirling trajectory during the closure. GENERAL SIGNIFICANCE: Conformational state of the lid regulates the activity and substrate specificity of PPL. Hence, it is essential to understand the lid dynamics and the role of specific amino acid residues involved.
[Mh] Termos MeSH primário: Colipases/química
Lipase/química
Pâncreas/enzimologia
Água/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos/genética
Animais
Sítios de Ligação
Colipases/genética
Colipases/metabolismo
Hidrólise
Lipase/genética
Lipase/metabolismo
Simulação de Dinâmica Molecular
Mutagênese Sítio-Dirigida
Conformação Proteica
Especificidade por Substrato
Suínos/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Colipases); 059QF0KO0R (Water); EC 3.1.1.3 (Lipase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160508
[St] Status:MEDLINE


  3 / 470 MEDLINE  
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[PMID]:27155580
[Au] Autor:Haque N; Prabhu NP
[Ad] Endereço:Department of Biotechnology & Bioinformatics, School of Life Sciences, University of Hyderabad, Hyderabad 500 046, India.
[Ti] Título:Lid dynamics of porcine pancreatic lipase in non-aqueous solvents.
[So] Source:Biochim Biophys Acta;1860(10):2326-34, 2016 10.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Understanding the dynamics of enzymes in organic solvents has wider implications on their industrial applications. Pancreatic lipases, which show activity in their lid open-state, demonstrate enhanced activity in organic solvents at higher temperatures. However, the lid dynamics of pancreatic lipases in non-aqueous environment is yet to be clearly understood. METHODS: Dynamics of porcine pancreatic lipase (PPL) in open and closed conformations was followed in ethanol, toluene, and octanol using molecular simulation methods. In silico double mutant D250V and E254L of PPL (PPLmut-Cl) was created and its lid opening dynamics in water and in octanol was analyzed. RESULTS: PPL showed increase in solvent accessible surface area and decrease in packing density as the polarity of the surrounded solvent decreased. Breaking the interactions between D250-Y115, and D250-E254 in PPLmut-Cl directed the lid to attain open-state conformation. Major energy barriers during the lid movement in water and in octanol were identified. Also, the trajectories of lid movement were found to be different in these solvents. CONCLUSIONS: Only the double mutant at higher temperature showed lid opening movement suggesting the essential role of the three residues in holding the lid in closed conformation. The lid opening dynamics was faster in octanol than water suggesting that non-polar solvents favor open conformation of the lid. GENERAL SIGNIFICANCE: This study identifies important interactions between the lid and the residues in domain 1 which possibly keeps the lid in closed conformation. Also, it explains the rearrangements of residue-residue interactions during lid opening movement in water and in octanol.
[Mh] Termos MeSH primário: Colipases/química
Lipase/química
Conformação Proteica
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Sítios de Ligação
Colipases/genética
Colipases/metabolismo
Etanol/química
Hidrólise
Lipase/genética
Lipase/metabolismo
Simulação de Dinâmica Molecular
Octanóis/química
Pâncreas/química
Pâncreas/enzimologia
Especificidade por Substrato
Suínos/genética
Tolueno/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Colipases); 0 (Octanols); 3FPU23BG52 (Toluene); 3K9958V90M (Ethanol); EC 3.1.1.3 (Lipase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160508
[St] Status:MEDLINE


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[PMID]:25502231
[Au] Autor:Jaczó Z; Pál E; Dénes R; Somogyi A; Sasvári-Székely M; Guttman A; Rónai Z
[Ad] Endereço:Department of Medical Chemistry, Molecular Biology and Pathobiochemistry, Semmelweis University, Budapest, Hungary.
[Ti] Título:Rapid analysis of colipase gene variants by multicapillary electrophoresis.
[So] Source:Electrophoresis;36(11-12):1237-43, 2015 Jun.
[Is] ISSN:1522-2683
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Despite of the fact that the Human Genome Project was completed more than a decade ago, identification of the genetic background of polygenic diseases is still challenging. Several somewhat different approaches are available to investigate inheritable factors of complex phenotypes, all require, however efficient, high-throughput techniques for SNP genotyping. In this paper, we report a robust and reliable multiplex PCR-RFLP for genotype and haplotype analysis of six SNPs (rs41270082, rs3748051, rs142027015, rs3748048, rs73404011, and rs72925892) of the colipase (CLPS) gene. A multicapillary (12 capillaries) electrophoresis unit was used for high throughput and sensitive analysis of the digestion fragments. A Microsoft Excel-based spreadsheet was designed for the flexible visualization and evaluation of the electrophoretic separations, which is readily adaptable for any kind of electrophoresis application. Haplotype analysis of the two loci localized in close proximity of each other was carried out by molecular method, extended haplotypes including all five SNPs in the 5' upstream region were calculated. The techniques were applied in a case-control association study of type 2 diabetes mellitus. Although, single marker analysis did not reveal any significant association, it was observed that the rare GGCCG haplotype of the five 5' upstream region SNPs was about three times more frequent among patients compared to healthy control population. Our results demonstrated the applicability of multicapillary CGE in large-scale, high-throughput SNP analysis, and suggested that the CLPS gene polymorphisms might be considered as genetic risk factor for type 2 diabetes mellitus.
[Mh] Termos MeSH primário: Colipases/genética
Eletroforese Capilar/métodos
Polimorfismo de Nucleotídeo Único
[Mh] Termos MeSH secundário: Estudos de Casos e Controles
Diabetes Mellitus Tipo 2/genética
Genótipo
Haplótipos
Sequenciamento de Nucleotídeos em Larga Escala
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Colipases)
[Em] Mês de entrada:1603
[Cu] Atualização por classe:150611
[Lr] Data última revisão:
150611
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141216
[St] Status:MEDLINE
[do] DOI:10.1002/elps.201400551


  5 / 470 MEDLINE  
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[PMID]:25008989
[Au] Autor:Parker R; Rigby NM; Ridout MJ; Gunning AP; Wilde PJ
[Ad] Endereço:Institute of Food Research, Norwich Research Park, Colney, Norwich, NR4 7UA, UK. roger.parker@ifr.ac.uk peter.wilde@ifr.ac.uk.
[Ti] Título:The adsorption-desorption behaviour and structure function relationships of bile salts.
[So] Source:Soft Matter;10(34):6457-66, 2014 Sep 14.
[Is] ISSN:1744-6848
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The digestion of dietary components in the human gastrointestinal (GI) tract is a complex, dynamic, inherently heterogeneous process. A key aspect of the digestion of lipid in the GI tract is the combined action of bile salts, lipase and colipase in hydrolysing and solubilising dispersed lipid. The bile salts are a mixture of steroid acid conjugates with surfactant properties. In order to examine whether the different bile salts have different interfacial properties their dynamic interfacial behaviour was characterised. Differences in the adsorption behaviour to solid hydrophobic surfaces of bile salt species were studied using dual polarisation interferometry and atomic force microscopy (AFM) under physiological conditions. Specifically, the cholates adsorbed more slowly and a significant proportion were irreversibly adsorbed following buffer rinsing; whereas the deoxycholates and chenodeoxycholates adsorbed more rapidly and desorbed to a greater extent following buffer rinsing. The conjugating groups (taurine, glycine) did not influence the behaviour. AFM showed that the interfacial structures that remained following buffer rinsing were also different between these two groups. In addition, the adsorption-desorption behaviour affected the adsorption of colipase to a solid surface. This supports the idea that cooperative adsorption occurs between certain bile salts and colipase to facilitate the adsorption and activity of pancreatic lipase in order to restore lipolytic activity in the presence of bile salts. This study provides insights into how differences in bile salt structure could affect lipase activity and solubilisation of lipolysis products and other lipid-soluble bioactive molecules.
[Mh] Termos MeSH primário: Ácidos e Sais Biliares/química
Colipases/química
[Mh] Termos MeSH secundário: Adsorção
Microscopia de Força Atômica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bile Acids and Salts); 0 (Colipases)
[Em] Mês de entrada:1510
[Cu] Atualização por classe:140807
[Lr] Data última revisão:
140807
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140711
[St] Status:MEDLINE
[do] DOI:10.1039/c4sm01093k


  6 / 470 MEDLINE  
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[PMID]:24816161
[Au] Autor:Birk RZ; Rubio-Aliaga I; Boekschoten MV; Danino H; Müller M; Daniel H
[Ad] Endereço:Department of Nutrition,Faculty of Health Sciences, Ariel University,Ariel40700,Israel.
[Ti] Título:Differential regulation of pancreatic digestive enzymes during chronic high-fat diet-induced obesity in C57BL/6J mice.
[So] Source:Br J Nutr;112(2):154-61, 2014 Jul 28.
[Is] ISSN:1475-2662
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Exocrine pancreatic digestive enzymes are essential for the digestion of dietary components and are regulated by them. Chronic excess dietary high fat (HF) consumption is a contributing factor of diet-induced obesity (DIO) and associated chronic diseases and requires adaptation by the pancreas. The aim of the present study was to investigate the effects of chronic HF diet feeding on exocrine pancreatic digestive enzyme transcript levels in DIO C57BL/6J mice. C57BL/6J mice were fed diets containing either 10 or 45% energy (E%) derived from fat for 12 weeks (n 10 mice per diet group). Pancreatic tissue and blood samples were collected at 0, 4 and 12 weeks. The expression of a panel of exocrine pancreatic digestive enzymes was analysed using quantitative RT-PCR and Western blot analysis. The HF (45 E%) diet-fed C57BL/6J mice developed obesity, hyperleptinaemia, hyperglycaemia and hyperinsulinaemia. The transcript levels of pancreatic lipase (PL), pancreatic lipase-related protein 2 (PLRP2) and pancreatic phospholipase A2 (PLA2) were initially elevated; however, they were down-regulated to basal control levels at week 12. The transcript levels of colipase were significantly affected by diet and time. The protein levels of PL and PLRP2 responded to HF diet feeding. The transcript levels of amylase and proteases were not significantly affected by diet and time. The transcript levels of specific lipases in hyperinsulinaemic, hyperleptinaemic and hyperglycaemic DIO C57BL/6J mice are down-regulated. However, these mice compensate for this by the post-transcriptional regulation of the levels of proteins that respond to dietary fat. This suggests a complex regulatory mechanism involved in the modulation of fat digestion.
[Mh] Termos MeSH primário: Dieta Hiperlipídica/efeitos adversos
Regulação Enzimológica da Expressão Gênica
Obesidade/enzimologia
Pâncreas Exócrino/enzimologia
Processamento de Proteína Pós-Traducional
Processamento Pós-Transcricional do RNA
[Mh] Termos MeSH secundário: Animais
Colipases/genética
Colipases/metabolismo
Hiperglicemia/etiologia
Hiperinsulinismo/etiologia
Resistência à Insulina
Leptina/sangue
Lipase/genética
Lipase/metabolismo
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Obesidade/etiologia
Obesidade/metabolismo
Obesidade/fisiopatologia
Pâncreas Exócrino/metabolismo
Pâncreas Exócrino/fisiopatologia
Fosfolipases A2 Secretórias/genética
Fosfolipases A2 Secretórias/metabolismo
RNA Mensageiro/metabolismo
Distribuição Aleatória
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Colipases); 0 (Leptin); 0 (RNA, Messenger); EC 3.1.1.3 (Lipase); EC 3.1.1.3 (pancreatic lipase related protein 2); EC 3.1.1.4 (Phospholipases A2, Secretory)
[Em] Mês de entrada:1409
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140513
[St] Status:MEDLINE
[do] DOI:10.1017/S0007114514000816


  7 / 470 MEDLINE  
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[PMID]:23977086
[Au] Autor:Bou Ali M; Karray A; Gargouri Y; Ben Ali Y
[Ad] Endereço:Laboratory of Biochemistry, National Engineering School of Sfax (ENIS), University of Sfax, Sfax, Tunisia.
[Ti] Título:N-terminal domain of turkey pancreatic lipase is active on long chain triacylglycerols and stabilized by colipase.
[So] Source:PLoS One;8(8):e71605, 2013.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The gene encoding the TPL N-terminal domain (N-TPL), fused with a His6-tag, was cloned and expressed in Pichia pastoris, under the control of the glyceraldehyde-3-phosphate dehydrogenase (GAP) constitutive promoter. The recombinant protein was successfully expressed and secreted with an expression level of 5 mg/l of culture medium after 2 days of culture. The N-TPL was purified through a one-step Ni-NTA affinity column with a purification factor of approximately 23-fold. The purified N-TPL, with a molecular mass of 35 kDa, had a specific activity of 70 U/mg on tributyrin. Surprisingly, this domain was able to hydrolyse long chain TG with a specific activity of 11 U/mg using olive oil as substrate. This result was confirmed by TLC analysis showing that the N-TPL was able to hydrolyse insoluble substrates as olive oil. N-TPL was unstable at temperatures over 37°C and lost 70% of its activity at acid pH, after 5 min of incubation. The N-TPL exhibited non linear kinetics, indicating its rapid denaturation at the tributyrin-water interface. Colipase increased the N-TPL stability at the lipid-water interface, so the TPL N-terminal domain probably formed functional interactions with colipase despite the absence of the C-terminal domain.
[Mh] Termos MeSH primário: Colipases/metabolismo
Lipase/química
Lipase/metabolismo
Pâncreas/enzimologia
Triglicerídeos/metabolismo
Perus/metabolismo
[Mh] Termos MeSH secundário: Animais
Células Clonais
DNA Complementar/genética
Eletroforese em Gel de Poliacrilamida
Ativação Enzimática
Vetores Genéticos/genética
Histidina/metabolismo
Concentração de Íons de Hidrogênio
Hidrólise
Cinética
Lipase/isolamento & purificação
Oligopeptídeos/metabolismo
Pichia/metabolismo
Ligação Proteica
Estabilidade Proteica
Estrutura Terciária de Proteína
Proteínas Recombinantes de Fusão/isolamento & purificação
Proteínas Recombinantes de Fusão/metabolismo
Especificidade por Substrato
Temperatura Ambiente
Fatores de Tempo
Transformação Genética
Trioleína/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Colipases); 0 (DNA, Complementary); 0 (His-His-His-His-His-His); 0 (Oligopeptides); 0 (Recombinant Fusion Proteins); 0 (Triglycerides); 122-32-7 (Triolein); 4QD397987E (Histidine); EC 3.1.1.3 (Lipase); S05LZ624MF (tributyrin)
[Em] Mês de entrada:1404
[Cu] Atualização por classe:150423
[Lr] Data última revisão:
150423
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130827
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0071605


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[PMID]:23770034
[Au] Autor:Xiao X; Ross LE; Sevilla WA; Wang Y; Lowe ME
[Ad] Endereço:Department of Pediatrics, Children's Hospital of Pittsburgh of the University of Pittsburgh Medical Center, Pittsburgh, PA 15224, USA.
[Ti] Título:Porcine pancreatic lipase related protein 2 has high triglyceride lipase activity in the absence of colipase.
[So] Source:Biochim Biophys Acta;1831(9):1435-41, 2013 Sep.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Efficient dietary fat digestion is essential for newborns who consume more dietary fat per body weight than at any other time of life. In many mammalian newborns, pancreatic lipase related protein 2 (PLRP2) is the predominant duodenal lipase. Pigs may be an exception since PLRP2 expression has been documented in the intestine but not in the pancreas. Because of the differences in tissue-specific expression, we hypothesized that the kinetic properties of porcine PLRP2 would differ from those of other mammals. To characterize its properties, recombinant porcine PLRP2 was expressed in HEK293T cells and purified to homogeneity. Porcine PLRP2 had activity against tributyrin, trioctanoin and triolein. The activity was not inhibited by bile salts and colipase, which is required for the activity of pancreatic triglyceride lipase (PTL), minimally stimulated PLRP2 activity. Similar to PLRP2 from other species, PLRP2 from pigs had activity against galactolipids and phospholipids. Importantly, porcine PLRP2 hydrolyzed a variety of dietary substrates including pasteurized human mother's milk and infant formula and its activity was comparable to that of PTL. In conclusion, porcine PLRP2 has broad substrate specificity and has high triglyceride lipase activity even in the absence of colipase. The data suggest that porcine PLRP2 would be a suitable lipase for inclusion in recombinant preparations for pancreatic enzyme replacement therapy.
[Mh] Termos MeSH primário: Colipases/metabolismo
Galactolipídeos/metabolismo
Intestinos/metabolismo
Lipase/metabolismo
Pâncreas/metabolismo
Fosfolipídeos/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Western Blotting
Caprilatos/metabolismo
Bovinos
Gorduras na Dieta/metabolismo
Seres Humanos
Hidrólise
Lipase/genética
Dados de Sequência Molecular
RNA Mensageiro/genética
Reação em Cadeia da Polimerase em Tempo Real
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
Suínos
Triglicerídeos/metabolismo
Trioleína/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Caprylates); 0 (Colipases); 0 (Dietary Fats); 0 (Galactolipids); 0 (Phospholipids); 0 (RNA, Messenger); 0 (Recombinant Proteins); 0 (Triglycerides); 122-32-7 (Triolein); 6P92858988 (tricaprylin); EC 3.1.1.3 (Lipase); EC 3.1.1.3 (pancreatic lipase related protein 2); S05LZ624MF (tributyrin)
[Em] Mês de entrada:1310
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130618
[St] Status:MEDLINE


  9 / 470 MEDLINE  
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[PMID]:23732775
[Au] Autor:Johnson K; Ross L; Miller R; Xiao X; Lowe ME
[Ad] Endereço:Department of Pediatrics, Children's Hospital of Pittsburgh at University of Pittsburgh Medical Center, Pittsburgh, Pennsylvania, USA.
[Ti] Título:Pancreatic lipase-related protein 2 digests fats in human milk and formula in concert with gastric lipase and carboxyl ester lipase.
[So] Source:Pediatr Res;74(2):127-32, 2013 Aug.
[Is] ISSN:1530-0447
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Dietary fats must be digested into fatty acids and monoacylglycerols prior to absorption. In adults, colipase-dependent pancreatic triglyceride lipase (PTL) contributes significantly to fat digestion. In newborn rodents and humans, the pancreas expresses low levels of PTL. In rodents, a homologue of PTL, pancreatic lipase-related protein 2 (PLRP2), and carboxyl ester lipase (CEL) compensate for the lack of PTL. In human newborns, the role of PLRP2 in dietary fat digestion is unclear. To clarify the potential of human PLRP2 to influence dietary fat digestion in newborns, we determined PLRP2 activity against human milk and infant formula. METHODS: The activity of purified recombinant PLRP2, gastric lipase (GL), and CEL against fats in human milk and formula was measured with each lipase alone and in combination with a standard pH-stat assay. RESULTS: Colipase added to human milk stimulated fat digestion. PLRP2 and CEL had activity against human milk and formula. Predigestion with GL increased PLRP2 activity against both substrates. Together, CEL and PLRP2 activity was additive with formula and synergistic with human milk. CONCLUSION: PLRP2 can digest fats in human milk and formula. PLRP2 acts in concert with CEL and GL to digest fats in human milk in vitro.
[Mh] Termos MeSH primário: Fórmulas Infantis/metabolismo
Lipase/metabolismo
Leite Humano/metabolismo
[Mh] Termos MeSH secundário: Análise de Variância
Colipases/isolamento & purificação
Colipases/metabolismo
Eletroforese em Gel de Poliacrilamida
Seres Humanos
Concentração de Íons de Hidrogênio
Recém-Nascido
Lipase/isolamento & purificação
Pichia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Colipases); EC 3.1.1.3 (CEL protein, human); EC 3.1.1.3 (Lipase); EC 3.1.1.3 (gastric lipase, human); EC 3.1.1.3 (pancreatic lipase related protein 2)
[Em] Mês de entrada:1402
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130605
[St] Status:MEDLINE
[do] DOI:10.1038/pr.2013.90


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[PMID]:23547942
[Au] Autor:Periago MJ; Bravo S; García-Alonso FJ; Rincón F
[Ad] Endereço:Departamento de Tecnología de los Alimento, Nutrición y Bromatología, Facultad de Veterinaria, University of Murcia , Campus de Espinardo, Campus Regional de Excelencia Internacional "Campus Mare Nostrum", 30071-Espinardo, Murcia, Spain.
[Ti] Título:Detection of key factors affecting lycopene in vitro accessibility.
[So] Source:J Agric Food Chem;61(16):3859-67, 2013 Apr 24.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:On the basis of a Plackett-Burman experimental design for a resolution IV level obtained via a foldover strategy, the effect of 11 factors on lycopene in vitro accessibility was investigated. The selected factors were thermal treatment (X1), olive oil addition (X2), gastric pH (X3), gastric digestion time (X4), pepsin concentration (X5), intestinal pH (X6), pancreatin concentration (X7), bile salts concentration (X8), colipase addition (X9), intestinal digestion time (X10), and intestinal digestion speed (X11). Tomato passata was used as a natural source of lycopene. Samples were collected after gastric and intestinal digestion, and from the micellar phase, to quantify the (all-E)-lycopene and its (Z)-isomers by HPLC. Except for X3, X6, X7, and X11, the other factors studied explained lycopene in vitro accessibility, mainly regarding intestinal digestion, with R(2) values ≥ 0.60. Our results showed that the accessibility of lycopene is influenced by the conditions applied during in vitro intestinal digestion.
[Mh] Termos MeSH primário: Carotenoides/farmacocinética
[Mh] Termos MeSH secundário: Ácidos e Sais Biliares
Carotenoides/química
Carotenoides/metabolismo
Colipases/metabolismo
Digestão
Temperatura Alta
Concentração de Íons de Hidrogênio
Técnicas In Vitro
Intestinos/metabolismo
Isomerismo
Lycopersicon esculentum/química
Azeite de Oliva
Pancreatina/metabolismo
Óleos Vegetais/química
Estômago/metabolismo
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bile Acids and Salts); 0 (Colipases); 0 (Olive Oil); 0 (Plant Oils); 36-88-4 (Carotenoids); 8049-47-6 (Pancreatin); SB0N2N0WV6 (lycopene)
[Em] Mês de entrada:1406
[Cu] Atualização por classe:151119
[Lr] Data última revisão:
151119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130404
[St] Status:MEDLINE
[do] DOI:10.1021/jf3052994



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