View clinical trials related to Protein Malabsorption.
Filter by:Rationale: Aging is accompanied by a blunted muscle protein synthetic response to protein ingestion.This anabolic resistance may be related to decreased postprandial amino acid release in the circulation, due to greater amino acid extraction by splanchnic tissues in older individuals. It has been suggested that extracted amino acids are utilized by intestinal epithelial cells for cell proliferation, generating new cells to maintain healthy mucosa. So far, there is no evidence that dietary protein-derived amino acids are taken up and incorporated in intestinal mucosal protein in vivo in humans. Furthermore, there is no evidence that this process is impacted by age. Objective: To assess the postprandial incorporation of dietary protein-derived amino acids in intestinal mucosal protein in healthy young and older males. Study design: Cross-sectional, non-therapeutic intervention study design Study population: 5 healthy, non-obese (BMI 18.5-30kg/m2) young adult males (age: 18-35y inclusive) and 5 community dwelling older males (age: 67+y). Intervention: Continuous intravenous stable isotope amino acid tracer infusion will be applied, in combination with oral ingestion of 20g intrinsically labelled milk protein, with plasma, muscle and duodenal mucosa biopsy samples collected at different time points throughout the experimental test day. Main study parameters/endpoints: The primary study outcome is the postprandial (0-5h) incorporation of dietary protein-derived amino acids in duodenal mucosal protein following the ingestion of 20g intrinsically labelled milk protein. Secondary study parameters include postprandial plasma availability of dietary protein-derived amino acids and fractional duodenal mucosal protein synthetic rate.
The retrospective cohort study will compare the prevalence of sarcopenia and associated factors between older patients who have undergone bariatric surgery and older patients with obesity without previous bariatric surgery.
Inflammatory bowel disease (IBD) includes two idiopathic chronic relapsing and remitting inflammatory conditions affecting the gastrointestinal (GI) tract: Crohn's disease (CD) and ulcerative colitis (UC)Malnutrition and significant alteration of body composition are common in inflammatory bowel disease patients, whereby the prevalence of malnutrition may be up to 82.8% in CD patients with active disease, and up to 38.9% in CD patients in remission. Many CD patients have low muscle mass and function (sarcopenia) with drivers of such pathophysiology unknown. 41.6% of CD patients with sarcopenia require surgery, with the surgical trauma and resulting inactivity leading to further muscle mass loss such that the chronic inflammatory insult associated with refractory disease may be linked to advanced muscle mass depletion. The majority of adult CD patients have low muscle mass even in clinical remission indicating the poorly reversible nature of this phenomenon. Chronic disease burden may therefore be important in the accentuation of muscle loss. Muscle mass is maintained through the daily balance of MPS and muscle protein breakdown (MPB), with the essential amino acid (EAA) components of a meal and muscle contraction being the primary stimulators of MPS. Patients with active CD show a significant decrease in the expression of proteins in hypertrophic signalling pathways (Akt, P70S6K1) with no change in the expression of atrophic signalling (MAFbx, MuRF1). Also, adult CD patients with established disease consume less protein compared to matched healthy volunteers (HV). Furthermore, the intestinal motility, measured using cine-MRI, is reduced in active CD, possibly further decreasing intestinal digestion and absorption of dietary peptides. In general, the malabsorption is a major contributing factor to malnourishment in CD. It has been shown that in male paediatric patients with long-term CD, muscle metabolism is perturbed by a negative branched-chain amino acid balance in the forearm, with this variable linked to lower appendicular muscle mass, higher muscle fatigue and reduced protein intake, CD may have a significant effect on protein digestion and absorption, and blunt the MPS response to feeding, leading to a chronic muscle mass reduction that may persist even when in remission. The EAA components of a protein meal are crucial for the stimulation of muscle protein synthesis (MPS), and all the EAA/leucine play a key role in driving MPS. Low serum levels EAA/leucine have been reported in CD but their role in the aetiology of sarcopenia in CD is unknown. Further, how CD affects the protein digestion/absorption and how this contributes to low EAA/leucine unclear. Recent advances in stable isotope tracer techniques using a dual tracer methodology now enable a more accurate determination of protein digestibility. By following the appearance of intrinsically labelled AAs into the blood upon digestion of the intrinsically labelled protein, alongside the appearance of label-free AAs, protein digestibility can be accurately determined. Further, by collecting a muscle biopsy postprandially, the direct incorporation of AA from the digested protein into the muscle can be determined- providing a gold standard method for investigating anabolic resistance. Project aim is to use an intrinsically labelled casein to investigate protein digestion, absorption and MPS responses in CD patients. To achieve this, investigators will investigate protein digestion, absorption and muscle protein synthesis responses in Crohn's disease patients and healthy volunteers by utilising intrinsically labelled protein.
The purpose of this study is to examine the pattern of plasma amino acid appearance after a two-week daily regimen of milk protein concentrate supplementation with and without the addition of Bacillus coagulans GBI-30, 6086 among older women.
Proteins play an important role as structural and functional components for the human body and prevent stunting. Protein quality has a great importance in meeting the nutritional needs of populations across the world throughout the life course, particularly during pregnancy and early childhood. Dietary protein deficiency is mainly due to protein indigestibility limiting indispensable amino acids (IAAs) bioavailability. In Morocco, as it's the case in many developing countries, diet is mainly based on a large consumption of cereals, fruits, vegetables and pulses, and is generally low in meat, which is the main source of protein and IAA. The general objective of this study is to evaluate the digestibility of Fava bean proteins and bioavailability of IAA using a dual-tracer method with stable isotopes.
Objective of Clinical Trial: To test, in a blinded study the bioavailability of Genepro Generation 3 (GEN3) Protein as compared to whey protein. This study is intended to show the equivalent value of Genepro Gen3 as compared to whey protein (1scoop (12g) Genepro Generation 3 (GEN3) compared to 30g serving of whey protein). Total Serum Protein levels will be tested every other week to evaluate blood protein levels in each participant
The quality of protein intake has an important role within the nutritional needs of people throughout their lives around the world, particularly in developing countries and in particular during pregnancy and early childhood. It is likely that adequate protein reduce by 40% the prevalence of stunting (low height for age) in children under five years, according to World Health Organization data. Uncertainty about the quality of the diet, specifically with reference to quality proteins has potential impacts on health, economy, agriculture, and food security of a nation. The amino acid digestibility estimates based on stool analysis do not represent the amount of absorbed amino acid. Ideally, the bioavailable amino acid should be measured by methods that assess the difference between consumed and absorbed amino acids. However, the uptake of amino acids is not readily non-invasively measured in healthy humans. The use of vegetable protein intrinsically labeled by stable isotopes offers a solution to this problem. The deuterated water (2H2O), with relatively low cost, is suitable for labeling plant proteins such as those of beans. The labeled amino acids are present in the test meal ingested and incorporated into the blood, representing a single measure of bioavailability. This study aims to develop and apply a new methodology, using stable isotopes, to evaluate the bioavailability of bean protein, a very important food in the Brazilian diet, according to cooking procedures, through the use of deuterium. The project will be divided into two parts: a human nutrition and an agriculture part, the latter by planting/harvesting deuterium-labeled Phaseolus vulgaris L. After two weeks of blooming, deuterium water will be added to the bean crop, which will be subsequently dried. Chemical analysis and assessment of incorporation of deuterium in the beans will be done. Concurrent with the cultivation of beans, there will be a protein absorption test with 15 healthy volunteers for validation of the methods. For comparison purposes, milk protein labeled with deuterium and C13 will be used. The volunteers will consume the test meals. Blood, urine and saliva samples will be collected at baseline (before food ingestion), and in different times after the meal. In the next phase of this research, labeled beans produced by the agriculture experiment will be used to measure the protein absorption of volunteers of different groups (older persons, and stunting and non-stunting children). The samples will analyzed by isotope-ratio mass spectrometry. This methodology may promote a better understanding of the absorption of proteins and amino acids using less invasive methods in different age groups and clinical conditions. This work will have an important impact for the general population as well as for agriculture and health-related professionals.