Role of Pancreatic Cholesterol Esterase in the Uptake and Esterification of Cholesterol by Isolated Intestinal Cells

Gallo, Linda L.; Newbill, T.; Hyun, Jin Hai; Vahouny, George V.; Treadwell, C. R.

doi:10.3181/00379727-156-39921

Cited by 77 publications

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“…Similar distribution was observed for another pancreatic enzyme, cholesterol esterase. Gallo et al (29,30) demonstrated that "intestinal" cholesterol esterase was of pancreatic origin and was localized within the absorptive cells. They proposed two roles for pancreatic cholesterol esterase in the process of adsorption of dietary cholesterol in the intestine; catalysis of the hydrolysis of dietary cholesterol ester and maybe the catalysis of cholesterol ester re-esterification after being taken up by the villus cell.…”

Section: Discussionmentioning

confidence: 99%

Coenzyme A-independent Monoacylglycerol Acyltransferase from Rat Intestinal Mucosa

Tsujita¹,

Miyazaki

Tabei

et al. 1996

Journal of Biological Chemistry

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Rat intestinal mucosa contains high diacylglycerolsynthesizing activity (monoacylglycerol acyltransferase (MGAT) activity) due to monoacylglycerol and fatty acid, independently of coenzyme A and ATP. MGAT activity was purified from rat intestinal mucosa by successive chromatography separations on DEAEcellulose, CM-Sephadex, and anti-IgG-Sepharose against rat pancreatic lipase. The enzyme was electrophoretically homogeneous, and its molecular weight was 49,000, which is identical with that of rat pancreatic lipase. Immunoblotting analysis with antibody against rat pancreatic lipase showed one immunoreactive protein with an estimated molecular weight of 49,000. The activity of the purified enzyme was completely inhibited by addition of the antibody. Using immunocytochemical techniques, it was found that immunoreactive protein against rat pancreatic lipase was uniformly distributed within the absorptive cells of the intestine but was absent from the microvillar membrane. The MGAT activity of intestinal mucosal homogenate was inhibited by about 65% by addition of antibody against rat pancreatic lipase. Trioleoylglycerol-and dioleoylglycerol-hydrolyzing activities of the purified enzyme and pancreatic lipase were inhibited by addition of intestinal mucosa extract.These results suggest that pancreatic lipase is present in intestinal absorptive cells and that it may contribute to resynthesis of diacylglycerol from monoacylglycerol and fatty acids in these cells.Dietary fat (triacylglycerol) is digested by pancreatic lipase to 2-monoacylglycerols and free fatty acids prior to its absorption in the intestinal lumen (1). Unlike esterases, pancreatic lipase develops its full activity only with emulsified substrates; i.e. it is activated at lipid-water interfaces (2). The adsorbed 2-monoacylglycerols and free fatty acids are resynthesized to triacylglycerol by enterocytes. Triacylglycerols are synthesized by two pathways, the glycerol 3-phosphate pathway and the monoacylglycerol pathway (3). During fat absorption in monogastric animals, the monoacylglycerol pathway is the major route of triacylglycerol synthesis (4). This pathway involves the stepwise acylation of 2-monoacylglycerols absorbed from the intestinal lumen. Monoacylglycerol acyltransferase (MGAT) 1 is a microsomal enzyme that catalyzes the synthesis of 1,2-diacylglycerols from 2-monoacylglycerols and long chain fatty acyl coenzyme A (5, 6). Fatty acyl coenzyme A is synthesized from free fatty acid and coenzyme A by fatty acyl-CoA synthetase, a reaction which requires energy (ATP). Because the main purpose of eating fat diets is to gain energy, it is comprehensible that ATP is required in the fat adsorption process. Therefore, we examined a newly discovered pathway which does not require energy.Previously, we reported that, under physiological conditions, lipases/esterases catalyze the synthesis of acyl-alcohol ester from free fatty acids and alcohols (7-9). These reactions do not require ATP or coenzyme A. Pancreatic cholesterol esterase, which is known to hyd...

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Section: Discussionmentioning

confidence: 99%

Coenzyme A-independent Monoacylglycerol Acyltransferase from Rat Intestinal Mucosa

Tsujita¹,

Miyazaki

Tabei

et al. 1996

Journal of Biological Chemistry

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“…Gallo et al reported that depletion of cholesterol esterase in the intestinal lumen following antibody administration led to a reduction of lymphatic cholesterol absorption in rats 28 . Furthermore, they observed that the addition of cholesterol esterase to culture medium increased cholesterol esterification of isolated intestinal cells 27 . Subsequently, these authors showed that pancreatic cholesterol esterase is localized inside rat intestinal mucosal cells 29 .…”

Section: Mechanisms Responsible For the Acceleration Of Cholesterol Amentioning

confidence: 99%

“…It was suggested that cholesterol esterase accelerates intestinal absorption and esterification of unesterified cholesterol 26,27 . Gallo et al reported that depletion of cholesterol esterase in the intestinal lumen following antibody administration led to a reduction of lymphatic cholesterol absorption in rats 28 .…”

Section: Mechanisms Responsible For the Acceleration Of Cholesterol Amentioning

confidence: 99%

Factors Affecting Intestinal Absorption of Cholesterol and Plant Sterols and Stanols

Ikeda

2015

J. Oleo Sci.

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“…Culture broth was centrifuged for 15 min at 8650g and supernatant was collected and examined for CHE activity based on Gallo's method 1 . Bacterial isolates producing CHE were identified by using PCR amplification of 16 S rDNA gene employing bacterial universal primers Bac8F (5 -AGAGTTTGATCCTGGCTCAG-3 ) and Bac1492R (5 -ACGGTTACCTTGTTACGACTT-3 ) 26 .…”

Section: Bacterial Screening and Genetic Identificationmentioning

confidence: 99%

“…Cholesterol esterase (CHE; EC 3.1.1.13) is a glycoprotein that belongs to the lipase/esterase family [1][2][3] . Triacylglycerols, cholesteryl esters, phosphoglycerides, esters of vitamins A and D, and monoacylglycerols are also among the physiological substrates of the enzyme 4 .…”

Section: Introductionmentioning

confidence: 99%

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Khuchareontaworn¹,

Pakpitchareon²,

Areekit³

et al. 2010

ScienceAsia

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Cholesterol esterase (CHE; EC 3.1.1.13) plays an important role in the hydrolysis of cholesterol ester to cholesterol and free fatty acids. It is used for clinical detection of cholesterol. Herein, the CHE producing microorganisms were isolated from oil contaminated soil samples at 45°C by spreading the sample on nutritive agar. Pseudomonas aeruginosa strain RE 24.3 was selected since it produced the highest CHE activity. The purified enzyme, namely CHEPaRE24.3, had high activity between 30 and 45°C at the optimum pH of 7.0. The substrate specificity test revealed that CHEPaRE24.3 hydrolysed a variety of cholesterol esters. Inhibitor examination found that Hg 2+ , β-mercaptoethanol, and DTT could inhibit the enzyme activity at 99.38%, 100%, and 43.2%, respectively. It is remarkable that PMSF showed no effect on enzyme activity. The stability test indicated that the CHEPaRE24.3 enzyme remained at 70% activity after 28 days storage at 4°C, 29°C, or 37°C. The long-term storage stability and thermotolerance of CHEPaRE24.3 as well as its resistance to PMSF suggests that it could be applicable for use in a cholesterol biosensor.

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Role of Pancreatic Cholesterol Esterase in the Uptake and Esterification of Cholesterol by Isolated Intestinal Cells

Cited by 77 publications

References 0 publications

Coenzyme A-independent Monoacylglycerol Acyltransferase from Rat Intestinal Mucosa

Coenzyme A-independent Monoacylglycerol Acyltransferase from Rat Intestinal Mucosa

Factors Affecting Intestinal Absorption of Cholesterol and Plant Sterols and Stanols

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