BCM-7 regulates the secretion and expression of gastrointestinal mucins through μ-opioid pathway

A1 cow milk works for my digestion

  • yeah, great

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  • nah, it's lousy

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  • after my thyroid started picking up

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PeskyPeater

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β-Casomorphin-7 regulates the secretion and expression of gastrointestinal mucins through a μ-opioid pathway


Abstract

We have recently shown that β-casomorphin-7, a milk opioid peptide, strongly stimulates mucin secretion in the rat jejunum through a nervous pathway and opioid receptor activation. In this study, the hypothesis that β-casomorphin-7 may also act directly on intestinal goblet cells was investigated in vitro in rat and human intestinal mucin-producing cells (DHE and HT29-MTX) using quantitative and semiquantitative RT-PCR and ELISA. The presence of μ-opioid receptors was demonstrated in rat goblet cells in the upper half of the colonic crypt and in the two cell lines by immunohistochemistry and RT-PCR. In rat DHE cells, β-casomorphin-7 increased the expression of rat mucin (rMuc)2 and rMuc3 but not rMuc1, rMuc4, and rMuc5AC. This effect was time and dose dependent, with the maximum of increase in transcripts being noticed for a concentration of 10−4 M after 2 h of stimulation for rMuc2 (225% of controls) and 4 h of stimulation for rMuc3 (208% of controls). Mucin secretion was maximally increased after 8 h of stimulation. Interestingly, these effects were prevented by pretreatment of the cells with the μ-opioid antagonist cyprodime. In human HT29-MTX cells, β-casomorphin-7 (10−4 M) also increased MUC5AC mRNA levels (219% after 24 h of stimulation) and the secretion of this mucin (169% of controls). In conclusion, β-casomorphin-7 may contribute significantly to mucin production via a direct effect on intestinal goblet cells and the activation of μ-opioid receptors. Because intestinal mucins have a crucial mucosal protective function, dairy products containing β-casomorphin-7 may improve intestinal protection and could have dietary and health applications.
 
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PeskyPeater

PeskyPeater

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Wondering which products actually contain these BCM-7 or don't and how processing and digestion of dairy is affected?
Let's take look at this study,

direct link PDF:

Occurrence of β-casomorphins 5 and 7 in commercial dairy products and in their digests following in vitro simulated gastro-intestinal digestion
Ivano De Noni *, Stefano Cattaneo
Dipartimento di Scienze e Tecnologie Alimentari e Microbiologiche, Università degli Studi di Milano, via G. Celoria 2, Milano 20133, Italy
ABSTRACT
The occurrence of b-casomorphin-5 (BCM5) and b-casomorphin-7 (BCM7) was investigated in commercial dairy products and in their digests, following in vitro simulated gastro-intestinal digestion (SGID), by means of HPLC–MS.
The analysed dairy products were as follows:
10 cheeses (Gorgonzola, Caprino, Brie, Taleggio, Gouda, Fontina, Cheddar and Grana Padano 10-, 15- or 25-m ripened);
4 samples of drinking milk (unprocessed, pasteurised, UHT and in bottle-sterilised);
2 yoghurts and 4 fermented milks containing probiotics;
7 infant formulas; and 4 dried milk-derivatives (skim milk powder, calcium caseinate and milk protein concentrates).
b-Casomorphin-5 was not detected in dairy products, either prior to or after SGID.
b-Casomorphin-7 was detected only in cheeses with the exception of Taleggio, Caprino and Grana Padano samples.
Peptide amount was in the range 0.01–0.15 mg kg1 the highest level being recovered in Brie sample. Following SGID, BCM7 formed in all dairy samples or increased up to 21.77 mg kg1 in digests of cheeses.
The peptide level ranged from 0.29 to 1.23 mg kg1 in fermented milks and from 3.46 to 22.18 mg kg1 in dried milk-derivatives.

Digests of commercial infant formulas contained BCM7 at concentrations of 0.04–0.21 mg l1 .
For the first time, this work reports quantitative values for BCM5 and BCM7 in a range of dairy products providing evidence that, during processing, only
proteolytic systems involved in manufacturing and ripening of cheese can potentially hydrolyse b-CN to BCM7.
Nevertheless, formation or further release of BCM7 is mainly promoted by the action of gastrointestinal proteinases during in vitro digestion irrespective of the type of dairy product.
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PeskyPeater

PeskyPeater

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You might ask yourself, aren't these casomorphins detrimental by activating the same receptor as endotoxin LPS in our gut?
Can these caseine opioids protect us from endotoxin or what?
Let's take a look:

Interaction of Opioids with TLR4—Mechanisms and Ramifications
Abstract:
The innate immune receptor toll-like receptor 4 (TLR4) is known as a sensor for the gramnegative bacterial cell wall component lipopolysaccharide (LPS). TLR4 activation leads to a strong pro-inflammatory response in macrophages; however, it is also recognised to play a key role in cancer. Recent studies of the opioid receptor (OR)-independent actions of opioids have identified that TLR4 can respond to opioids. Opioids are reported to weakly activate TLR4, but to significantly inhibit LPS-induced TLR4 activation. The action of opioids at TLR4 is suggested to be non-stereoselective, this is because OR-inactive (+)-isomers of opioids have been shown to activate or to inhibit TLR4 signalling, although there is some controversy in the literature. While some opioids can bind to the lipopolysaccharide (LPS)-binding cleft of the Myeloid Differentiation factor 2 (MD-2) co-receptor, pharmacological characterisation of the inhibition of opioids on LPS activation of TLR4 indicates a noncompetitive mechanism. In addition to a direct interaction at the receptor, opioids affect NF-κB activation downstream of both TLR4 and opioid receptors and modulate TLR4 expression, leading to a range of in vivo outcomes. Here, we review the literature reporting the activity of opioids at TLR4, its proposed mechanism(s), and the complex functional consequences of this interaction.
 

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