Deciphering the protein digestion of meat products for the elderly by in vitro food oral processing and gastric dynamic digestion, peptidome analysis and modeling.

The elderly population will increase sharply in the future, along with an emerging range of specific nutritional needs that include adapted food. We aimed to develop a workflow to study the fate of a food, objectify the bioavailability of nutrients in the case of the digestive physiology of the elderly, and model the fate of proteins in the stomach. Pork frankfurters were subjected to in vitro normal and deficient mastication and gastric digestion, mimicking adult and elderly food oral and digestive processing. Swallowable food boluses were characterized for granulometric and rheological properties. Biochemical analyses were conducted on the bolus and on the digesta. Macronutrients, label-free peptide quantification and identification were performed, and modeling was applied to protein digestion kinetics. After deficient mastication, the food bolus was harder with more large particles, lower free iron release and more protein oxidation. The amount of peptides released in the stomach progressively increased, but to a lower extent for the elderly digestive condition and irrespective of masticatory efficiency. 592 peptides were identified from 67 proteins. Different trajectories were observed for adult and elderly digestive conditions, and two groups of meat proteins were identified based on the rate of hydrolysis. Designing suitable foods requires in vitro tools to evaluate the possible benefit for the elderly. Besides the well-known notion of Food Oral Processing (FOP), our work broadens the concept by extending oral activity to digestion when working in a nutritional context. This new concept is named Food Oral and Digestive Processing, FODP.

Determination of irinotecan and SN38 in human plasma by TurboFlow™ liquid chromatography-tandem mass spectrometry.

Irinotecan is a cytotoxic agent used in the treatment of metastatic colorectal cancer. Irinotecan is a prodrug when is converted in vivo to an active metabolite SN38, which has potent pharmacological activity. SN38 is then inactivated and excreted as SN38-glucuronide. High-performance liquid chromatography-mass spectrometry is a widely used bioanalysis technique that can be coupled to the turbulent-flow extraction line to shorten preparation time. A technique was developed to quantify irinotecan and its metabolite by liquid chromatography-tandem mass spectrometry coupled with a turbulent-flow online extraction method. Assays were performed on 100 µL of plasma after protein precipitation. The supernatant is injected directly into the extraction column, transferred to the chromatographic column, and analyzed by tandem mass spectrometry. Linearity, reproducibility and repeatability of the method were validated on a concentration range of 25-2500 ng/mL for irinotecan and 5-500 ng/mL for SN38. For the low limit of quantification of irinotecan and SN38, precision is 6.31% and 8.73%, and accuracy is 84.0% and 91.8%, respectively. The SN38-glucuronide determination protocol included a hydrolyzation step. This method was successfully used to quantify irinotecan, SN38 and SN38-G in human plasma in a clinical trial.

Forces created by mandibular advancement devices in OSAS patients: a pilot study during sleep.

BACKGROUND: The aim of this study was to measure forces created by progressive mandibular advancement with an oral device, during natural sleep, in a sample of adult patients with obstructive sleep apnea syndrome (OSAS). METHODS: A pressure transducer system was placed on the acrylic arms of a two-piece oral appliance (Herbst type) used by nine moderate to severe OSAS patients, in addition to all captors routinely used for polysomnography. Strains on the left and right sides were collected, during stable sleep stages without arousal, for each step of 1 mm advancement. RESULTS: The mean force in this sample was 1.18 N/mm and showed an almost linear evolution. Measurements showed intra- and inter-individual variability. CONCLUSION: The force values recorded in this study may explain the occlusal and skeletal side effects associated with long-term use of these oral appliances. They illustrate the influence of the extent of mandibular advancement, and indicate a possible dose-dependent effect.

Functional genomics of the muscle response to restraint and transport in chickens.

In the present study, we used global approaches (proteomics, transcriptomics, and metabolomics) to assess the molecular basis of the muscle response to stress in chickens. A restraint test, combined with transport for 2 h (RT test) was chosen as the potentially stressful situation. Chickens (6 wk old) were either nontreated (control chickens) or submitted to the RT test (treated chickens). The RT test induced a 6-fold increase in corticosterone concentrations, suggesting hypothalamic-pituitary-adrenal axis activation. The RT test decreased the relative abundance of several hexose phosphates [glucose-1-P (G1P), glucose-6-P (G6P), fructose-6-P (F6P), and mannose-6-P (M6P)] in thigh muscle. In addition, 55 transcripts, among which 39 corresponded to unique annotated genes, were significantly up- (12 genes) or downregulated (27 genes) by treatment. Similarly, 45 proteic spots, among which 29 corresponded to unique annotated proteins, were overexpressed (11 proteins), underexpressed (14 proteins), or only expressed in treated chickens. Integrative analysis of differentially expressed genes and proteins showed that most transcripts and proteins belong to 2 networks whose genes were mainly related with cytoskeleton structure or carbohydrate metabolism. Whereas the decrease in energetic metabolites suggested an activation of glycogenolysis and glycolysis in response to the RT test, the reduced expression of genes and proteins involved in these pathways suggested the opposite. We hypothesized that the prolonged RT test resulted in a repression of glycogenolysis and glycolysis in thigh muscle of chickens. The down-expression of genes and proteins involved in the formation of fiber stress after the RT test suggests a reinforcement of myofibrils in response to stress.