scholarly journals Physiological parameters governing the action of pancreatic lipase

2010 ◽  
Vol 23 (1) ◽  
pp. 146-154 ◽  
Author(s):  
Iain A. Brownlee ◽  
Deborah J. Forster ◽  
Matthew D. Wilcox ◽  
Peter W. Dettmar ◽  
Chris J. Seal ◽  
...  
Keyword(s):  
Weight Management ◽  
Pancreatic Lipase ◽  
Lipase Activity ◽  
Dietary Lipid ◽  
Ion Concentration ◽  
Lipid Absorption ◽  
Energy Yield ◽  
Body Of Knowledge ◽  
Lipid Ester ◽  
Duodenal Lumen

The most widely used pharmacological therapies for obesity and weight management are based on inhibition of gastrointestinal lipases, resulting in a reduced energy yield of ingested foods by reducing dietary lipid absorption. Colipase-dependent pancreatic lipase is believed to be the major gastrointestinal enzyme involved in catalysis of lipid ester bonds. There is scant literature on the action of pancreatic lipase under the range of physiological conditions that occur within the human small intestine, and the literature that does exist is often contradictory. Due to the importance of pancreatic lipase activity to nutrition and weight management, the present review aims to assess the current body of knowledge with regards to the physiology behind the action of this unique gastrointestinal enzyme system. Existing data would suggest that pancreatic lipase activity is affected by intestinal pH, the presence of colipase and bile salts, but not by the physiological range of Ca ion concentration (as is commonly assumed). The control of secretion of pancreatic lipase and its associated factors appears to be driven by gastrointestinal luminal content, particularly the presence of acid or digested proteins and fats in the duodenal lumen. Secretion of colipase, bile acids and pancreatic lipase is driven by cholecystokinin and secretin release.

scholarly journals Inhibitory Activity of Benzophenones from Anemarrhena asphodeloides on Pancreatic Lipase

2013 ◽  
Vol 8 (4) ◽  
pp. 1934578X1300800 ◽  
Author(s):  
Yang Hee Jo ◽  
Seon Beom Kim ◽  
Jong Hoon Ahn ◽  
Qing Liu ◽  
Bang Yeon Hwang ◽  
...  
Keyword(s):  
Pancreatic Lipase ◽  
Lipase Activity ◽  
Soluble Fraction ◽  
Significant Inhibition ◽  
Dietary Fats ◽  
Lipid Absorption ◽  
Vitro Assay ◽  
Key Enzyme ◽  
Anemarrhena Asphodeloides

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.

Decreased lipid absorption due to reduced pancreatic lipase activity in aging male mice

2014 ◽  
Vol 15 (5) ◽  
pp. 463-473 ◽  
Author(s):  
Kazushi Yamamoto ◽  
Yasuna Kitano ◽  
Shuang E ◽  
Yu Hatakeyama ◽  
Yu Sakamoto ◽  
...  
Keyword(s):  
Pancreatic Lipase ◽  
Lipase Activity ◽  
Lipid Absorption ◽  
Aging Male ◽  
Male Mice

Effect of dietary cellulose on site of lipid absorption

1985 ◽  
Vol 249 (2) ◽  
pp. G184-G191
Author(s):  
D. Gallaher ◽  
B. O. Schneeman
Keyword(s):  
Small Intestine ◽  
Cellular Uptake ◽  
Pancreatic Lipase ◽  
Lipase Activity ◽  
Lipid Absorption ◽  
Distal Intestine ◽  
Intestinal Contents ◽  
Microvillus Membrane ◽  
Stomach Emptying

The effect of dietary cellulose on the localization within the small intestine of isotopically labeled triglyceride (TG) and cholesterol (CH) from a test meal was investigated. Feeding a 20% cellulose meal resulted in greater quantities of 14C-TG present in both the contents and mucosa of the distal intestine compared with a fiber-free control meal. In contrast, cellulose had no effect on the localization of CH within either the intestinal contents or the mucosa. Accumulation of TG within the intestine was not due to differences in stomach emptying, as the emptying rate was similar for both TG and CH. Within the bulk phase TG must be hydrolyzed by pancreatic lipase before it is available for cellular uptake at the microvillus membrane, whereas CH requires no hydrolysis. The greater amount of TG, but not of CH, within the intestine suggests that cellulose can interfere with lipase activity in vivo. Consequently, cellulose can delay TG hydrolysis and increase the amount of lipid absorbed in the ileum.

Do the Natural Chemical Compounds Interact with the Same Targets of Current Pharmacotherapy for Weight Management?-A Review

2019 ◽  
Vol 20 (4) ◽  
pp. 399-411 ◽  
Author(s):  
Shiqi Luo ◽  
George Binh Lenon ◽  
Harsharn Gill ◽  
Heidi Yuen ◽  
Angela Wei Hong Yang ◽  
...  
Keyword(s):  
Weight Loss ◽  
Weight Management ◽  
Pancreatic Lipase ◽  
Weight Reduction ◽  
Chemical Compounds ◽  
Alpha Amylase ◽  
Melanocortin Receptor ◽  
Health Concern ◽  
European Medicines Agency ◽  
Ppar Γ

Background: Obesity has become a worldwide health concern. Pharmacotherapies are now being introduced because lifestyle modifications alone are insufficient for weight management. The treatment outcomes of current approved anti-obesity agents are not satisfying due to drug-related intolerances. And so natural therapies including herbal medicines are popular alternatives for weight reduction; however, there are limited studies about their mechanism of actions. Methods: Five databases (PubMed, Scopus, Google Scholar, Science Direct, Proquest) were searched to investigate the targets and safety profiles of the current and past anti-obesity drugs that have been approved by the Food and Drug Administration (FDA) or the European Medicines Agency (EMA) as well as the commonly used off-label agents. The targets for weight-loss natural products and their principle bioactive components have also been searched. Only articles in English were included. Results: The targets for current anti-obesity single agents include pancreatic lipase, Glucagon Like Peptide-1(GLP-1) receptor, and serotonin 2C (5-HT2C) receptor. Potential targets such as amylin, pancreatic alpha amylase, leptin receptor, melanocortin receptor 4 receptor (MC4R), Peroxisome Proliferator- Activated Receptors gamma (PPAR γ), endocannabinoid 1 (CB1) receptor and Adenosine Monophosphate (AMP)-Activated Protein Kinase (AMPK) were discussed in various studies. Natural compounds have been found to interact with targets like pancreatic lipase, pancreatic alpha amylase, AMPK and PPAR γ to achieve weight reduction. Conclusion: Current pharmacotherapies and natural chemical compounds do act on same targets. Further investigations on the interactions between herbal compounds and the above targets are essential for the development of novel weight-loss therapies.

scholarly journals Clock regulation of dietary lipid absorption

2012 ◽  
Vol 15 (4) ◽  
pp. 336-341 ◽  
Author(s):  
M. Mahmood Hussain ◽  
Xiaoyue Pan
Keyword(s):  
Dietary Lipid ◽  
Lipid Absorption

scholarly journals Modification of a phospholipid stabilized emulsion interface by bile salt: effect on pancreatic lipase activity

1998 ◽  
Vol 39 (3) ◽  
pp. 623-632 ◽  
Author(s):  
Martin Wickham ◽  
Martin Garrood ◽  
John Leney ◽  
Peter D.G. Wilson ◽  
Annette Fillery-Travis
Keyword(s):  
Bile Salt ◽  
Pancreatic Lipase ◽  
Lipase Activity ◽  
Salt Effect

scholarly journals Studies on the detergent inhibition of pancreatic lipase activity.

1983 ◽  
Vol 24 (10) ◽  
pp. 1336-1342
Author(s):  
Y Gargouri ◽  
R Julien ◽  
A G Bois ◽  
R Verger ◽  
L Sarda
Keyword(s):  
Pancreatic Lipase ◽  
Lipase Activity

scholarly journals Kinetic studies on pancreatic lipase activity in micellar systems. II. Effect of fatty acid chain length of substrates.

1983 ◽  
Vol 31 (12) ◽  
pp. 4213-4219 ◽  
Author(s):  
HIROSHI NAKAHARA ◽  
SATOSHI OKADA ◽  
KENSHU MOCHIDA ◽  
HIDENOBU OHMORI ◽  
MASAICHIRO MASU
Keyword(s):  
Fatty Acid ◽  
Chain Length ◽  
Pancreatic Lipase ◽  
Lipase Activity ◽  
Kinetic Studies ◽  
Fatty Acid Chain Length ◽  
Fatty Acid Chain ◽  
Micellar Systems

Regulation of apo A-IV transcription by lipid in newborn swine is associated with a promoter DNA-binding protein

2003 ◽  
Vol 284 (2) ◽  
pp. G248-G254 ◽  
Author(s):  
Song Lu ◽  
Ying Yao ◽  
Heng Wang ◽  
Songmei Meng ◽  
Xiangying Cheng ◽  
...  
Keyword(s):  
Transcriptional Activation ◽  
Promoter Sequence ◽  
Dietary Lipid ◽  
Lipid Absorption ◽  
Proximal Promoter ◽  
Significant Shift ◽  
Human Sequence ◽  
Nuclear Extracts ◽  
Promoter Dna ◽  
Isocaloric Diets

Dietary lipid acutely upregulates apolipoprotein (apo) A-IV expression by sevenfold at the pretranslational level in neonatal swine jejunum. To determine the mechanism of this regulation, two-day-old female swine received intraduodenal infusions of low- and high-triacylglycerol (TG) isocaloric diets for 24 h. Nuclear runoff assay confirmed apo A-IV gene transcriptional regulation by the high-TG diet. Footprinting analysis using the swine apo A-IV proximal promoter sequence (+14 to −246 bp) demonstrated three regions protected by the low-TG extracts. Of these three motifs, only ACCTTC showed 100% homology to the human sequence and was further studied. EMSA was performed using probes containing wild-type (WT) and mutant (M) motifs. A shift was noted with the low-TG nuclear extracts with the WT probe but not with the M probe. Excess unlabeled free WT probe competed out the shift, whereas the M probe did not. No significant shift occurred with either probe using high-TG extracts. These results suggest that a repressor protein binds to the ACCTTC motif and becomes unbound during lipid absorption, allowing transcriptional activation of the apo A-IV gene in newborn swine small intestine.

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