NDLI: Enteral delivery of proteins enhances the expression of proteins involved in the cytoskeleton and protein biosynthesis in human duodenal mucosa.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Goichon, Alexis Bertrand, Julien Chan, Philippe Lecleire, Stéphane Coquard, Aude Cailleux, Anne-Françoise Vaudry, David Déchelotte, Pierre Coëffier, Moïse
Description	Author Affiliation: Goichon A ( INSERM Unit 1073, Rouen, France); Bertrand J ( INSERM Unit 1073, Rouen, France); Chan P ( Institute for Research and Innovation in Biomedicine, Rouen University, Rouen, France); Lecleire S ( INSERM Unit 1073, Rouen, France); Coquard A ( Pharmacy, and.); Cailleux AF ( Institute for Research and Innovation in Biomedicine, Rouen University, Rouen, France); Vaudry D ( Institute for Research and Innovation in Biomedicine, Rouen University, Rouen, France); Déchelotte P ( INSERM Unit 1073, Rouen, France); Coëffier M ( INSERM Unit 1073, Rouen, France)
Abstract	BACKGROUND: Amino acids are well known to be key effectors of gut protein turnover. We recently reported that enteral delivery of proteins markedly stimulated global duodenal protein synthesis in carbohydrate-fed healthy humans, but specifically affected proteins remain unknown. OBJECTIVE: We aimed to assess the influence of an enteral protein supply on the duodenal mucosal proteome in carbohydrate-fed humans. DESIGN: Six healthy volunteers received for 5 h, on 2 occasions and in random order, either an enteral infusion of maltodextrins alone (0.25 g · kgâ»¹ · hâ»¹) mimicking the fed state or maltodextrins with a protein powder (0.14 g proteins · kgâ»¹ · hâ»¹). Endoscopic duodenal biopsy specimens were then collected and frozen until analysis. A 2-dimensional polyacrylamide gel electrophoresis-based comparative proteomics analysis was then performed, and differentially expressed proteins (at least ±1.5-fold change; Student's t test, P < 0.05) were identified by mass spectrometry. Protein expression changes were confirmed by Western blot analysis. RESULTS: Thirty-two protein spots were differentially expressed after protein delivery compared with maltodextrins alone: 28 and 4 spots were up- or downregulated, respectively. Among the 22 identified proteins, 11 upregulated proteins were involved either in the cytoskeleton (ezrin, moesin, plastin 1, lamin B1, vimentin, and ß-actin) or in protein biosynthesis (glutamyl-prolyl-transfer RNA synthetase, glutaminyl-transfer RNA synthetase, elongation factor 2, elongation factor 1Î´, and eukaryotic translation and initiation factor 3 subunit f). CONCLUSIONS: Enteral delivery of proteins altered the duodenal mucosal proteome and mainly stimulated the expression of proteins involved in cytoskeleton and protein biosynthesis. These results suggest that protein supply may affect intestinal morphology by stimulating actin cytoskeleton remodeling.
File Format	HTM / HTML
ISSN	00029165
e-ISSN	19383207
Journal	American Journal of Clinical Nutrition
Issue Number	2
Volume Number	102
Language	English
Publisher	American Society for Nutrition
Publisher Date	2015-08-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Nutritional Sciences Cytoskeletal Proteins Metabolism Dietary Proteins Administration & Dosage Duodenum Enteral Nutrition Gene Expression Regulation Intestinal Mucosa Protein Biosynthesis Chromatography, High Pressure Liquid Chemistry Genetics Databases, Protein Endoscopy, Gastrointestinal Gene Ontology Intubation, Gastrointestinal Spectrometry, Mass, Electrospray Ionization Tandem Mass Spectrometry Two-dimensional Difference Gel Electrophoresis Randomized Controlled Trial Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Nutrition and Dietetics Medicine

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