NPIF

Spis deg frisk!

 Forum 

Svikt i tarmbarrieren og opptak i blodbanen av peptider

Peptides. 2008 Jun;29(6):1042-7. Epub 2008 Feb 6.
Transport of micro-opioid receptor agonists and antagonist peptides across Caco-2 monolayer.
Iwan M, Jarmołowska B, Bielikowicz K, Kostyra E, Kostyra H, Kaczmarski M.
Faculty of Biology, University of Warmia and Mazury, Oczapowskiego 1A, 10-19 Olsztyn, Poland.

Milk is the source of beta-casomorphins--biologically active peptides with opioid activity--which are suspected to play various roles in the human body. The local influence of exogenous opioid peptides on gastrointestinal functions has been widely reported. After passing the gut barrier, beta-casomorphins may affect the functions of immunological system, as well as dopaminergic, serotoninergic and GABA-ergic systems in brain, regulate the opioid receptor development and elicit behavioral effects. However, possibilities and mechanisms of the intestinal transport of beta-casomorphins in human body in vivo have not been reported so far. In our research, the transepithelial transport of micro-opioid receptor agonists--human beta-casomorphin-5 and 7(BCM5, BCM7) and antagonist--lactoferroxin A (LCF A) have been investigated using Caco-2 monolayer. In order to determine the pathway of investigated peptide transport across Caco-2 monolayer, two directions of the transport (apical to basolateral and basolateral to apical) have been studied. All investigated peptides were transported across the human intestinal cell line Caco-2 and the curves of cumulative amount of transported peptides in time were linear in each case. In addition, the hydrolysis of beta-casomorphins during 60 min of experiment by dipeptidyl peptidase IV was observed. The data suggest the possibility of transport of opioid peptides derived from food across human intestinal mucosa.

PMID: 18355944 [PubMed - in process]



J Pept Sci. 2007 Jul;13(7):468-74. Links
Transport of a tripeptide, Gly-Pro-Hyp, across the porcine intestinal brush-border membrane.
Aito-Inoue M, Lackeyram D, Fan MZ, Sato K, Mine Y.
Department of Food Sciences and Nutritional Health, Kyoto Prefectural University, 1-5 Nakaragi-cho, Shimogamo, Kyoto 606-8522, Japan.

The transcellular transport of oligopeptides across intestinal epithelial cells has attracted considerable interest in investigations into how biologically active peptides express diverse physiological functions in the body. It has been postulated that the tripeptide, Gly-Pro-Hyp, which is frequently found in collagen sequences, exhibits bioactivity. However, the mechanism of uptake of dietary di- and tripeptides by intestinal epithelial cells is not well understood. In this study, we used porcine brush-border membrane (BBM) vesicles to assess Gly-Pro-Hyp uptake, because these vesicles can structurally and functionally mimic in vivo conditions of human intestinal apical membranes. The present study demonstrated the time-dependent degradation of this tripeptide into the free-form Gly and a dipeptide, Pro-Hyp, on the apical side of the BBM vesicles. In parallel with the hydrolysis of the tripeptide, the dipeptide Pro-Hyp was identified in the BBM intravesicular space environment. We found that the transcellular transport of Pro-Hyp across the BBM was inhibited by the addition of a competitive substrate (Gly-Pro) for peptide transporter (PEPT1) and was pH-dependent. These results indicate that Gly-Pro-Hyp can be partially hydrolyzed by the brush-border membrane-bound aminopeptidase N to remove Gly, and that the resulting Pro-Hyp is, in part, transported into the small intestinal epithelial cells via the H(+)-coupled PEPT1. Gly-Pro-Hyp cannot cross the epithelial apical membrane in an intact form, and Pro-Hyp is highly resistant to hydrolysis by intestinal mucosal apical proteases. Copyright (c) 2007 European Peptide Society and John Wiley & Sons, Ltd.

PMID: 17554807 [PubMed - in process]



2007 The American Society for Nutrition J. Nutr. 137:953-958, April 2007
Nutrient Physiology, Metabolism, and Nutrient-Nutrient Interactions
Angiotensin Converting Enzyme Inhibitory Peptides from a Lactotripeptide-Enriched Milk Beverage Are Absorbed Intact into the Circulation1
Unilever Food and Health Research Institute, 3133 AR Vlaardingen, The Netherlands
Martin Foltz*, Evelyne E. Meynen, Veronique Bianco, Chris van Platerink, Thea M. M. G. Koning and Joris Kloek

* To whom correspondence should be addressed. E-mail: Denne e-postadressen er beskyttet mot programmer som samler e-postadresser. Du må aktivere javaskript for å kunne se den. .

Food products containing angiotensin converting enzyme (ACE) inhibitory peptides reportedly play a role in treatment of mild hypertension. The aim of this placebo-controlled crossover study was to assess the bioavailability of Ile-Pro-Pro and 7 other ACE-inhibiting peptides present in a lactotripeptide (LTP)-enriched yogurt beverage and whether meal intake affects Ile-Pro-Pro bioavailability. Six male and female subjects randomly consumed an LTP-enriched yogurt beverage or a placebo in the fasted state and an LTP-enriched yogurt beverage in the fed or fasted state. The area under the curve (AUC) of Ile-Pro-Pro after the LTP treatment in the fasted state was 2.1-fold of that after the placebo treatment (P < 0.001). The maximum peptide plasma concentration (Cmax) value was greater after consumption of the LTP-enriched beverage (897 ± 157 pmol/L) than after the placebo treatment (555 ± 0.09 pmol/L; P < 0.001) with a greater time after ingestion when reaching Cmax (Tmax) in the placebo treatment. Plasma concentrations of the peptides Leu-Trp, Phe-Tyr, Ile-Tyr, and Leu-Pro-Pro increased compared with baseline (P < 0.05) in the LTP-enriched and placebo treatment when consumed in the fasted state. However, Cmax values differed significantly between the placebo and LTP-enriched treatment only for Leu-Pro-Pro. Meal intake affected Ile-Pro-Pro concentrations. When the beverage was consumed after a meal, the AUC of Ile-Pro-Pro was 1.3-fold (P < 0.05) of the AUC derived from premeal intake. This was due to an increase in the plasma elimination half-life (P < 0.05); Cmax and Tmax were not affected by meal intake. In summary, this is the first demonstration, to our knowledge, that the tripeptide Ile-Pro-Pro selectively escapes from intestinal degradation and reaches the circulation undegraded.

[link til publikasjonen]

Kommentar: Påvisning av tripeptid som går gjennom tarm-blodbarrieren uspaltet


 
Scand J Gastroenterol. 2006 Apr;41(4):408-19.Links
Gliadin, zonulin and gut permeability: Effects on celiac and non-celiac intestinal mucosa and intestinal cell lines.
Drago S, El Asmar R, Di Pierro M, Grazia Clemente M, Tripathi A, Sapone A, Thakar M, Iacono G, Carroccio A, D'Agate C, Not T, Zampini L, Catassi C, Fasano A.
Mucosal Biology Research Center, Center for Celiac Research and Division of Pediatric Gastroenterology and Nutrition, University of Maryland, School of Medicine, Baltimore, MD 21201, USA.

OBJECTIVE: Little is known about the interaction of gliadin with intestinal epithelial cells and the mechanism(s) through which gliadin crosses the intestinal epithelial barrier. We investigated whether gliadin has any immediate effect on zonulin release and signaling. MATERIAL AND METHODS: Both ex vivo human small intestines and intestinal cell monolayers were exposed to gliadin, and zonulin release and changes in paracellular permeability were monitored in the presence and absence of zonulin antagonism. Zonulin binding, cytoskeletal rearrangement, and zonula occludens-1 (ZO-1) redistribution were evaluated by immunofluorescence microscopy. Tight junction occludin and ZO-1 gene expression was evaluated by real-time polymerase chain reaction (PCR). RESULTS: When exposed to gliadin, zonulin receptor-positive IEC6 and Caco2 cells released zonulin in the cell medium with subsequent zonulin binding to the cell surface, rearrangement of the cell cytoskeleton, loss of occludin-ZO1 protein-protein interaction, and increased monolayer permeability. Pretreatment with the zonulin antagonist FZI/0 blocked these changes without affecting zonulin release. When exposed to luminal gliadin, intestinal biopsies from celiac patients in remission expressed a sustained luminal zonulin release and increase in intestinal permeability that was blocked by FZI/0 pretreatment. Conversely, biopsies from non-celiac patients demonstrated a limited, transient zonulin release which was paralleled by an increase in intestinal permeability that never reached the level of permeability seen in celiac disease (CD) tissues. Chronic gliadin exposure caused down-regulation of both ZO-1 and occludin gene expression. CONCLUSIONS: Based on our results, we concluded that gliadin activates zonulin signaling irrespective of the genetic expression of autoimmunity, leading to increased intestinal permeability to macromolecules.

PMID: 16635908 [PubMed - indexed for MEDLINE]


J Agric Food Chem. 2006 Jul 26;54(15):5261-6.Links
Improvement in isolation and identification of food-derived peptides in human plasma based on precolumn derivatization of peptides with phenyl isothiocyanate.
Aito-Inoue M, Ohtsuki K, Nakamura Y, Park EY, Iwai K, Morimatsu F, Sato K.
Department of Food Sciences and Nutritional Health, Kyoto Prefectural University, Shimogamo, Kyoto 606-8522, Japan.

For the isolation and detection of food-derived peptides in blood, an approach based on the derivatization of peptides with phenyl isothiocyanate (PITC) was developed. This approach allows hydrophilic peptides to be resolved and specifically detected by reversed-phase (RP) HPLC. For the rapid capturing and clarification of peptides in human plasma, solid-phase extraction by using a mini spin column (5 mmx5 mm) packed with a strong cation exchanger was used. The clarified peptide fraction was further fractionated by size-exclusion chromatography (SEC). The peptides in the SEC fractions were derivatized with PITC, and the derivatives were resolved by RP-HPLC by using an ammonium acetate buffer or a trifluoroacetic acid system. An automatic peptide sequencer based on Edman degradation with a modified program can directly analyze the resolved derivatives. Some synthetic peptides and food-derived peptides in human plasma were successfully isolated and identified by this approach.

PMID: 16848504 [PubMed - indexed for MEDLINE]



FEBS Lett. 2005 Aug 29;579(21):4851-5.Links
Rapid disruption of intestinal barrier function by gliadin involves altered expression of apical junctional proteins
.Sander GR, Cummins AG, Henshall T, Powell BC.
Tissue Development and Repair, Epithelial Biology Laboratory, Child Health Research Institute, 72 King William Road, North Adelaide, SA 5006, Australia. Denne e-postadressen er beskyttet mot programmer som samler e-postadresser. Du må aktivere javaskript for å kunne se den.

Coeliac disease is a chronic enteropathy caused by the ingestion of wheat gliadin and other cereal prolamines derived from rye and barley. In the present work, we investigated the mechanisms underlying altered barrier function properties exerted by gliadin-derived peptides in human Caco-2 intestinal epithelial cells. We demonstrate that gliadin alters barrier function almost immediately by decreasing transepithelial resistance and increasing permeability to small molecules (4 kDa). Gliadin caused a reorganisation of actin filaments and altered expression of the tight junction proteins occludin, claudin-3 and claudin-4, the TJ-associated protein ZO-1 and the adherens junction protein E-cadherin.

PMID: 16099460 [PubMed - indexed for MEDLINE]


Rapid disruption of intestinal barrier function by gliadin involves altered expression of apical junctional proteins
Guy R. Sandera, b, Adrian G. Cumminsc, d and Barry C. Powella, b
a) Tissue Development and Repair, Epithelial Biology Laboratory, Child Health Research Institute, 72 King William Road, North Adelaide, SA 5006, Australia
b) Department of Paediatrics, University of Adelaide, South Australia, Australia
c) Department of Gastroenterology and Hepatology, The Queen Elizabeth Hospital, Adelaide, South Australia, Australia
d) Department of Medicine, University of Adelaide, South Australia, Australia

Received 14 July 2005;  accepted 19 July 2005.  Available online 8 August 2005.

Referred to by:  Corrigendum to “Rapid disruption of intestinal barrier function by gliadin involves altered expression of apical junctional proteins FEBS (29865)” [FEBS Letters 579 (2005) 4851–4855] FEBS Letters, Volume 579, Issue 22, 12 September 2005, Page 5111
Guy R. Sander, Adrian G. Cummins, Tanya Henshall and Barry C. Powell

Abstract

Coeliac disease is a chronic enteropathy caused by the ingestion of wheat gliadin and other cereal prolamines derived from rye and barley. In the present work, we investigated the mechanisms underlying altered barrier function properties exerted by gliadin-derived peptides in human Caco-2 intestinal epithelial cells. We demonstrate that gliadin alters barrier function almost immediately by decreasing transepithelial resistance and increasing permeability to small molecules (4 kDa). Gliadin caused a reorganisation of actin filaments and altered expression of the tight junction proteins occludin, claudin-3 and claudin-4, the TJ-associated protein ZO-1 and the adherens junction protein E-cadherin.

[url til artikkel]



Biochimie. 1998 Feb;80(2):155-65. Related Articles, Links
Casein peptide release and passage to the blood in humans during digestion of milk or yogurt.
Chabance B, Marteau P, Rambaud JC, Migliore-Samour D, Boynard M, Perrotin P, Guillet R, Jollès P, Fiat AM.
CNRS-URA 1188, Université de Paris V, France.

In adult humans, after milk or yogurt ingestion, many peptides derived from alpha s1-, beta- or kappa-caseins were detected in stomach, including the kappa-caseinoglycopeptide, an inhibitor of platelet aggregation. Smaller peptides derived from casein and lactoferrin were recovered from duodenum. Two long peptides, the kappacaseinoglycopeptide and the N-terminal peptide of alpha s1-casein, were absorbed and detected in plasma. These results support the concept that food-born peptides could have physiological activities in man.

Publication Types:
Research Support, Non-U.S. Gov't

PMID: 9587673 [PubMed - indexed for MEDLINE]



FEBS Lett. 1997 Aug 4;412(3):475-9.Links
Release of opioid peptides, gluten exorphins by the action of pancreatic elastase.

Fukudome S, Jinsmaa Y, Matsukawa T, Sasaki R, Yoshikawa M.
Food Research Laboratory, Nisshin Flour Milling Co. Ltd., Saitama, Japan.

The release of opioid peptides, gluten exorphins A, which have been isolated from the pepsin-thermolysin digest of wheat gluten, with gastrointestinal proteases was examined. High levels of gluten exorphin A5 (Gly-Tyr-Tyr-Pro-Thr) immunoreactive materials were detected in the pepsin-pancreatic elastase digest by a competitive ELISA. From this digest, gluten exorphin A5, B5 and B4 were isolated. This means that these peptides are released in the gastrointestinal tracts after ingestion of wheat gluten. The yield of gluten exorphin A5 in the pepsin-elastase digest was larger than that in the pepsin-thermolysin digest. The gluten exorphin A5 sequence is found 15 times in the primary structure of the high molecular weight glutenin. The region from which gluten exorphin A5 was released by the action of pancreatic elastase was identified using synthetic fragment peptides.

PMID: 9276449 [PubMed - indexed for MEDLINE]



Gut. 1985 November; 26(11): 1214–1219.
Copyright notice
Intestinal permeability in patients with coeliac disease and dermatitis herpetiformis.
I Bjarnason, M N Marsh, A Price, A J Levi, and T J Peters

AbstractIntestinal permeability was investigated in patients with coeliac disease and dermatitis herpetiformis by a 51Chromium-labelled ethylenediaminetetraacetate (51Cr-EDTA) absorption test and the results correlated with histomorphometric analysis and intraepithelial lymphocyte counts of jejunal biopsies. The mean (+/- SD) 24 hour urine excretion of 51Cr-EDTA in 34 healthy volunteers was 1.9 +/- 0.5% of the orally administered test dose. Patients with untreated coeliac disease (19) or untreated dermatitis herpetiformis (five) excreted significantly more 51Cr-EDTA than controls (5.9 +/- 2.7% and 4.6 +/- 2.1%, respectively, p less than 0.001) and all were outside the normal range of 1.0-2.6%. Patients with coeliac disease (42) treated for 6 months-23 years (mean 5 years) and patients with dermatitis herpetiformis (11) treated for 6 months-8 years (mean 3 years) excreted significantly more 51Cr-EDTA than controls, 4.2 +/- 2.4% p less than 0.0001 and 3.0 +/- 0.9% p less than 0.003 respectively. Eleven of 14 (79%) treated patients with coeliac disease with an entirely normal jejunal mucosae demonstrated abnormal intestinal permeability. Intestinal permeability did not correlate significantly with either the mucosal height/crypt depth ratio or intraepithelial lymphocyte counts in jejunal biopsies from patients with untreated or treated coeliac disease. The demonstration of a persistent increase in intestinal permeability in patients with both coeliac disease and dermatitis herpetiformis may suggest a common pathogenetic mechanism in both disorders. It is postulated that altered permeability may facilitate the entry of gluten or a fraction thereof into the lamina propria where it causes a cascade of immunological events.

[Url til artikkel]

Kostholdsendringer

Kan hjelpe ved: 

ADHD
Aggresjon
Asperger
Autisme

Depresjon
Diabetes
Dysleksi
Epilepsi
Konsentrasjonsvansker
Magetrøbbel
Multippel Sklerose
Muskelsmerter
Opioide peptider
Parkinson
Psoriasis
Schizofreni
Sengevæting
Stoffskifteproblemer
Utslett

 

Listet alfabetisk.


 

Nytt PIF-nytt

PIF-nytt-nr-4-2016-Liten-for-web 


Alle medlemmene våre får PIF-nytt 4 ganger i året. Mangler du noen utgaver? Bestill dem hos: Denne e-postadressen er beskyttet mot programmer som samler e-postadresser. Du må aktivere javaskript for å kunne se den.

 

Frist for artikler etc til neste
PIF-nytt: 30. jan. 2017!

      2013 © NPIF | Drøbakgate 10b | 0463 OSLO | Tlf: 94 81 86 05 | Org.nr 980.252.256 | Bankgiro 5083.06.02795 | Denne e-postadressen er beskyttet mot programmer som samler e-postadresser. Du må aktivere javaskript for å kunne se den.