32 results match your criteria: "The Netherlands l.vanloon@maastrichtuniversity.nl.[Affiliation]"
J Nutr
July 2015
Department of Human Movement Sciences, NUTRIM School of Nutrition and Translational Research in Metabolism, Maastricht University Medical Centre+ (MUMC+), Maastricht, The Netherlands
Background: The slow digestion and amino acid absorption kinetics of isolated micellar casein have been held responsible for its relatively lower postprandial muscle protein synthetic response compared with rapidly digested proteins such as isolated whey. However, casein is normally consumed within a milk matrix. We hypothesized that protein digestion and absorption kinetics and the subsequent muscle protein synthetic response after micellar casein ingestion are modulated by the milk matrix.
View Article and Find Full Text PDFCrit Care
March 2015
Division of Anesthesia and Intensive Care, Department of Clinical Sciences, Intervention and Technology (CLINTEC), Karolinska Institutet and Karolinska University Hospital, Hälsovägen 13, Huddinge, 14186, Sweden.
Introduction: Evidence behind the recommendations for protein feeding during critical illness is weak. Mechanistic studies are needed to elucidate the effects of amino acid and/or protein supplementation on protein metabolism before larger clinical trials with higher levels of protein feeding are initiated.
Methods: We studied the effects of parenteral amino acid supplementation (equivalent to 1 g/kg/day) over the course of 3 hours on whole-body protein turnover in critically ill patients in the intensive care unit (ICU) during the first week after admission.
Eur J Endocrinol
July 2015
Department of Human Movement SciencesFaculty of Health, Medicine and Life Sciences, NUTRIM School for Nutrition, Toxicology and Metabolism, Maastricht University, PO Box 616, 6200 MD Maastricht, The NetherlandsDivision of Human NutritionWageningen University, Wageningen, The Netherlands
Background: Though it is well appreciated that insulin plays an important role in the regulation of muscle protein metabolism, there is much discrepancy in the literature on the capacity of exogenous insulin administration to increase muscle protein synthesis rates in vivo in humans.
Objective: To assess whether exogenous insulin administration increases muscle protein synthesis rates in young and older adults.
Design: A systematic review of clinical trials was performed and the presence or absence of an increase in muscle protein synthesis rate was reported for each individual study arm.
J Appl Physiol (1985)
December 2014
NUTRIM School for Nutrition, Toxicology and Metabolism, Maastricht University, Maastricht, The Netherlands
We aimed to determine the impact of precursor pool dilution on the assessment of postprandial myofibrillar protein synthesis rates (MPS). A Holstein dairy cow was infused with large amounts of L-[1-(13)C]phenylalanine and L-[1-(13)C]leucine, and the milk was collected and fractionated. The enrichment levels in the casein were 38.
View Article and Find Full Text PDFJ Clin Endocrinol Metab
December 2013
PhD, Department of Human Movement Sciences, Maastricht University Medical Center, Maastricht 6200 MD, The Netherlands.
Background: Disuse leads to rapid skeletal muscle atrophy, which brings about numerous negative health consequences. Muscle disuse atrophy is, at least in part, attributed to a decline in basal (postabsorptive) muscle protein synthesis rates. However, it remains to be determined whether muscle disuse also impairs the muscle protein synthetic response to dietary protein ingestion.
View Article and Find Full Text PDFNutr Metab (Lond)
January 2013
Department of Human Movement Sciences, Maastricht University Medical Centre, PO Box 616, Maastricht, MD, 6200, The Netherlands.
Background: A blunted muscle protein synthetic response to protein ingestion may contribute to the age related loss of muscle tissue. We hypothesized that the greater endogenous insulin release following co-ingestion of carbohydrate facilitates post-prandial muscle protein accretion after ingesting a meal-like bolus of protein in older males.
Methods: Twenty-four healthy older men (75±1 y) were randomly assigned to ingest 20 g intrinsically L-[1-13C] phenylalanine-labeled casein protein with (PRO-CHO) or without (PRO) 40 g carbohydrate.
Curr Opin Clin Nutr Metab Care
January 2012
Department of Human Movement Sciences, NUTRIM School for Nutrition, Toxicology and Metabolism, Maastricht University Medical Centre, Maastricht, The Netherlands.
Purpose Of Review: Amino acids do not merely represent precursors for de-novo protein synthesis, but also function as nutritional signals regulating various metabolic processes. In fact, ample evidence has been generated to show that various tissues respond to changes in amino acid availability via signal transduction pathways that are also regulated by hormones such as insulin, glucagon, and insulin-like growth factor 1.
Recent Findings: Amino acids, and leucine in particular, can act as strong insulin secretagogues when administered in combination with carbohydrate.