In vitro Gastrointestinal Models for Prebiotic Carbohydrates: A Critical Review

2019 ◽  
Vol 25 (32) ◽  
pp. 3478-3483 ◽  
Author(s):  
Oswaldo Hernandez-Hernandez
Keyword(s):  
Small Intestine ◽  
Gastrointestinal Tract ◽  
Brush Border ◽  
Critical Review ◽  
In Vitro Digestibility ◽  
Human Gastrointestinal Tract ◽  
Intestinal Brush Border ◽  
Small Intestinal ◽  
Existing Data

Background: In the last decade, various consortia and companies have created standardized digestion protocols and gastrointestinal simulators, such as the protocol proposed by the INFOGEST Consortium, the simulator SHIME, the simulator simgi®, the TIM, etc. Most of them claim to simulate the entire human gastrointestinal tract. However, few results have been reported on the use of these systems with potential prebiotic carbohydrates. Methods: This critical review addresses the existing data on the analysis of prebiotic carbohydrates by different in vitro gastrointestinal simulators, the lack of parameters that could affect the results, and recommendations for their enhancement. Results: According to the reviewed data, there is a lack of a realistic approximation of the small intestinal conditions, mainly because of the absence of hydrolytic conditions, such as the presence of small intestinal brush border carbohydrases that can affect the digestibility of different carbohydrates, including prebiotics. Conclusion: There is a necessity to standardize and enhance the small intestine simulators to study the in vitro digestibility of carbohydrates.

Characterization and modulation of rat small intestinal brush-border membrane transbilayer fluidity

1991 ◽  
Vol 260 (4) ◽  
pp. G586-G594
Author(s):  
P. K. Dudeja ◽  
R. K. Wali ◽  
J. M. Harig ◽  
T. A. Brasitus
Keyword(s):  
Brush Border ◽  
Brush Border Membrane ◽  
Leucine Aminopeptidase ◽  
Aminopeptidase Activity ◽  
Intestinal Brush Border Membrane ◽  
Intestinal Brush Border ◽  
Leucine Transport ◽  
Small Intestinal

In the present experiments, selective quenching by trinitrophenyl groups as well as steady-state fluorescence polarization and differential polarized phase fluorescence techniques, using three different lipid soluble fluorophores, were used to directly examine the fluidity of the exofacial and cytofacial leaflets of rat small intestinal brush-border membranes. These studies revealed that the fluidity of the exofacial hemileaflet was greater than the cytofacial hemileaflet. Differences in the distribution of phosphatidylcholine and phosphatidylethanolamine, as assessed by phospholipase A2 treatment and trinitrophenylation of aminophospholipids, were, at least partially, responsible for the asymmetrical fluidity of the hemileaflets. Moreover, in vitro addition of benzyl alcohol (final concn 25 mM) preferentially fluidized the exofacial leaflet and concomitantly decreased leucine aminopeptidase activity but did not affect the activities of maltase, sucrase, alkaline phosphatase, or gamma-glutamyltranspeptidase. In vivo addition of the membrane-mobility agent 2-(2-methoxyethoxy)ethyl 8-(cis-2-n-octylcyclopropyl)octanate] (A2C) (final concn 7.5 microM) preferentially fluidized the cytofacial leaflet and increased Na(+)-gradient-dependent D-glucose transport but not Na(+)-gradient-dependent L-leucine transport.

scholarly journals Methodology for the determination of polyphenol bioaccessibility

2020 ◽  
Vol 12 (2) ◽  
pp. 268-279
Author(s):  
Jozo Ištuk ◽  
Drago Šubarić ◽  
Lidija Jakobek
Keyword(s):  
Small Intestine ◽  
Gastrointestinal Tract ◽  
Food Samples ◽  
Human Gastrointestinal Tract ◽  
Gastrointestinal Digestion ◽  
Human Diet ◽  
Wide Range ◽  
Insight Into

Polyphenols are secondary metabolites of plants, commonly present in the human diet. Since they exhibit a wide range of bioactivities, polyphenols are extensively studied in the fields of nutrition and human health. Current studies have shown a high interest in determining the bioaccessibility of polyphenols, the amount of polyphenols that becomes available for absorption in the digestive tract. Bioaccessibility can be determined with the help of in vitro static gastrointestinal (GI) digestion models. In such a methodology, food samples containing polyphenols are subjected to a series of conditions that mimic the human gastrointestinal tract, with associated parameters. A high number of GI models with slightly different parameters were published. The purpose of this paper is to review the literature, focusing on the determination of polyphenol bioaccessibility and the parameters used in these GI digestion models, such as time, temperature, and pH of digestion, as well as enzyme concentrations. Gastrointestinal digestion models consist of oral, gastric and small intestine phases. These models provide a simple and reliable methodology which enables insight into the amount of bioaccessible polyphenols.

Cubilin and megalin expression and their interaction in the rat intestine: effect of thyroidectomy

2001 ◽  
Vol 281 (5) ◽  
pp. E900-E907 ◽  
Author(s):  
Raghunatha R. Yammani ◽  
Shakuntla Seetharam ◽  
Bellur Seetharam
Keyword(s):  
Brush Border ◽  
Intrinsic Factor ◽  
Immunoblot Analysis ◽  
Rat Intestine ◽  
Complement Components ◽  
Protein Levels ◽  
Intestinal Brush Border ◽  
Molecular Masses ◽  
Epidermal Growth

Cubilin is a 460-kDa multipurpose, multidomain receptor that contains an NH2-terminal 110-residue segment followed by 8 epidermal growth factor (EGF)-like repeats and a contiguous stretch (representing nearly 88% of its mass) of 27 CUB (initially found in complement components C1r/C1s, Uegf, and bone morphogenic protein-1) domains. Cubilin binds to intrinsic factor (IF)-cobalamin (cbl, vitamin B12) complex and promotes the ileal transport of cbl. The 460-kDa form of cubilin is the predominant form present in the apical brush-border membranes of rat intestine, kidney, and yolk sac, but a 230-kDa form of cubilin is also noted in the intestinal membranes. In thyroidectomized (TDX) rats, levels of intestinal brush-border IF-[57Co]-labeled cbl binding, 460-kDa cubilin protein levels and tissue (kidney) accumulation of cbl were reduced by ∼70%. Immunoblot analysis using cubilin antiserum of intestinal total membranes from TDX rats revealed cubilin fragments with molecular masses of 200 and 300 kDa. Both of these bands, along with the 230-kDa band detected in the total membranes of control rats and unlike the 460-kDa form, failed to react with antiserum to EGF. Mucosal membrane cubilin associated with megalin was reduced from ∼12% in control to ∼4% in TDX rats, and this decreased association was not due to altered megalin levels. Thyroxine treatment of TDX rats resulted in reversal of all of these effects, including an increase to nearly 24% of cubilin associated with megalin. In vitro, megalin binding to cubilin occurred with the NH2-terminal region that contained the EGF-like repeats and CUB domains 1 and 2 but not with a downstream region that contained CUB domains 2–10. These studies indicate that thyroxine deficiency in rats results in decreased uptake and tissue accumulation of cbl caused mainly by destabilization and deficit of cubilin in the intestinal brush border.

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