Main individual and product characteristics influencing in-mouth flavour release during eating masticated food products with different textures: mechanistic modelling and experimental validation.

A mechanistic model predicting flavour release during oral processing of masticated foods was developed. The description of main physiological steps (product mastication and swallowing) and physical mechanisms (mass transfer, product breakdown and dissolution) occurring while eating allowed satisfactory simulation of in vivo release profiles of ethyl propanoate and 2-nonanone, measured by Atmospheric Pressure Chemical Ionization Mass Spectrometry on ten representative subjects during the consumption of four cheeses with different textures. Model sensitivity analysis showed that the main parameters affecting release intensity were the product dissolution rate in the mouth, the mass transfer coefficient in the bolus, the air-bolus contact area in the mouth and the respiratory frequency. Parameters furthermore affecting release dynamics were the mastication phase duration, the velopharynx opening and the rate of saliva incorporation into the bolus. Specific retention of 2-nonanone on mucosa was assumed to explain aroma release kinetics and confirmed when gaseous samples were consumed.

Mechanisms explaining the role of viscosity and post-deglutitive pharyngeal residue on in vivo aroma release: A combined experimental and modeling study.

The objective of this study was to analyse the viscosity effect of liquid Newtonian products on aroma release, taking human physiological characteristics into account. In vivo release of diacetyl from glucose syrup solutions varying widely in viscosity (from 0.7 to 405mPas) was assessed by five panelists using Proton Transfer Reaction Mass Spectrometry (PTR-MS). The physicochemical properties of the solutions and the physiological parameters of subjects were experimentally measured. In parallel, a mechanistic model describing aroma release while eating a liquid food was developed. Model predictions based on the characteristics of the glucose syrup solution were invalidated when compared to in vivo measurements. Therefore, the assumption that the post-deglutitive pharyngeal residue was considerably diluted with saliva was introduced into the model. Under this hypothesis, the model gives a satisfactory prediction of the in vivo data. Thus, relevant properties to be considered for in vivo release were those of product-saliva mixes.

Thrombin receptor induction by injury-related factors in human skeletal muscle cells.

Thrombin is involved in tissue repair through its proteolytic activation of a specific thrombin receptor (PAR-1). Previous studies have shown that serine proteases and their inhibitors are involved in neuromuscular junction plasticity. We hypothesized that thrombin could also be involved during skeletal muscle inflammation. Thus we investigated the expression of PAR-1 in human myoblasts and myotubes in vitro and its regulation by injury-related factors. The functionality of this receptor was tested by measuring thrombin's ability to elicit Ca2+ signals. Western blot analysis and immunocytochemistry demonstrated the presence of PAR-1 in myoblasts but not in myotubes unless they were treated by tumor necrosis factor-alpha (10 ng/ml), interleukin-1beta (5 ng/ml), or transforming growth factor-beta(1) (10 ng/ml). The addition of 10 nM alpha-thrombin evoked a strong Ca2+ signal in myoblasts while a limited response in myotubes was observed. However, in the additional presence of injury-related factors, the amplitude of the Ca2+ response was significantly enhanced, representing 88, 65, 48% of their respective basal level, compared to 27% of that obtained in controls. Moreover, immunochemical studies on human skeletal muscle biopsies of patients suffering from inflammatory myopathies showed an overexpression of PAR-1. These results suggest that PAR-1 synthesis may be induced in response to muscle injury, thereby implicating thrombin signaling in certain muscle inflammatory diseases.

Protease nexin I expression is up-regulated in human skeletal muscle by injury-related factors.

Protease nexin I is a 43-50 kDa glycoprotein capable of inhibiting a number of serine proteases. In cultured differentiated human skeletal muscle (myotubes), we previously found that protease nexin I was localized in patches at their surface where it was active and able to inhibit thrombin. To understand the role of skeletal muscle protease nexin I after injury or in inflammatory conditions where thrombin might be extravasated by blood vessels, we examined the role of inflammatory factors on protease nexin I synthesis and secretion by myotubes in culture. By enzyme-linked immunosorbent assay (ELISA) and Western blotting, we found that this serine protease inhibitor is secreted by cultured human myotubes. Protease nexin I secretion is stimulated by tumor necrosis factor-alpha, transforming growth factor-beta and interleukin-1. Complex formation experiments with labeled thrombin reveal active protease nexin I bound to the surface of the treated cells. Secreted protease nexin I-thrombin complex was enhanced in the presence of transforming growth factor-beta and tumor necrosis factor-alpha. Protease nexin I mRNA was detected by reverse transcription-polymerase chain reaction (RT-PCR) and Northern blot analysis. Whatever the conditions, no significantly different levels were observed, indicating that the changes in cell and media protease nexin I concentration are elicited at the translational/posttranslational levels. Immunocytochemical studies on human skeletal muscle biopsies of patients suffering from inflammatory myopathies showed an overexpression of protease nexin I together with the above inflammatory factors. These findings suggest that skeletal muscle protease nexin I might play a role after injury or inflammatory pathologies.