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

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.

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.

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

scholarly journals Prognostic value of canine pancreatic lipase immunoreactivity and lipase activity in dogs with gastric dilatation-volvulus

PLoS ONE ◽  
2018 ◽  
Vol 13 (9) ◽  
pp. e0204216 ◽  
Author(s):  
Giuseppe Spinella ◽  
Francesco Dondi ◽  
Lisa Grassato ◽  
Luca Magna ◽  
Veronica Cola ◽  
...  
Keyword(s):  
Pancreatic Lipase ◽  
Lipase Activity ◽  
Prognostic Value ◽  
Gastric Dilatation

1558: METFORMIN AMELIORATES HEMODYNAMIC RESPONSE IN AGING MALE MICE AFTER HEMORRHAGIC SHOCK

2018 ◽  
Vol 46 (1) ◽  
pp. 763-763
Author(s):  
Dzmitry Matsiukevich ◽  
Giovanna Piraino ◽  
Patrick Lahni ◽  
Vivian Wolfe ◽  
Paul Hake ◽  
...  
Keyword(s):  
Hemorrhagic Shock ◽  
Hemodynamic Response ◽  
Aging Male ◽  
Male Mice

Evaluation of lipase activity in serum by radial enzyme diffusion.

1976 ◽  
Vol 22 (5) ◽  
pp. 633-637 ◽  
Author(s):  
J M Goldberg ◽  
P Pagast
Keyword(s):  
Pancreatic Lipase ◽  
Lipase Activity ◽  
Reference Method ◽  
Pancreatic Disease ◽  
Serum Lipase ◽  
Normal Limits ◽  
Diffusion Assay

Abstract Results of determination of serum lipase by radial enzyme diffusion correlate well with those by a titrimetric reference method in the abnormal range. The specificity of the diffusion assay allows the differentiation of patients with pancreatic disease, even when the lipase activity of the serum is within the normal limits of the tritrimetric assay. Pancreatic lipase is not detectable by the diffusion assay in the serum of individuals who are free from pancreatic disease.

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