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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.
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.