Enteral Delivery of Proteins Enhances the Expression of Proteins Involved in the Cytoskeleton and Protein Biosynthesis in Human Duodenal Mucosa

Alexis Goichon (1, 2, 3) , Julien Bertrand (1, 2, 3) , Philippe Chan (4, 2, 3) , Stéphane Lecleire (5, 1, 2, 3) , Aude Coquard (6) , Anne-Françoise Cailleux (7, 2, 3) , David Vaudry (8, 2, 3, 4) , Pierre Déchelotte (1, 2, 3, 9) , Moïse Coëffier (1, 2, 3, 9)

1 ADEN - Nutrition, inflammation et dysfonctionnement de l'axe intestin-cerveau
2 UNIROUEN - Université de Rouen Normandie
3 IRIB - Institute for Research and Innovation in Biomedicine
4 Plate-forme de Protéomique PISSARO
5 Service d'Hépato-Gastroentérologie [CHU Rouen]
6 Pharmacie [CHU Rouen]
7 CIC Rouen - Centre d'Investigation Clinique [CHU Rouen]
8 DC2N - Différenciation et communication neuronale et neuroendocrine
9 Service de Nutrition [CHU Rouen]

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 · kg^-1 · h^-1) mimicking the fed state or maltodextrins with a protein powder (0.14 g proteins · kg^-1 · h^-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 β-actin) or in protein biosynthesis (glutamyl-prolyl-transfer RNA synthetase, glutaminyl-transfer RNA synthetase, elongation factor 2, elongation factor 1δ, 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.

Mots clés: Young Adult; Adult; Chromatography; High Pressure Liquid; Cytoskeletal Proteins; cytoskeleton; Databases; Protein; Dietary Proteins; Duodenum; Endoscopy; Gastrointestinal; Enteral Nutrition; Gene Expression Regulation; Gene Ontology; Humans; Intestinal Mucosa; Intubation; Male; Protein Biosynthesis; proteins; proteome; Spectrometry; Mass; Electrospray Ionization; Tandem Mass Spectrometry; Two-Dimensional Difference Gel Electrophoresis

Domaines: Alimentation et Nutrition

Alexis Goichon, Julien Bertrand, Philippe Chan, Stéphane Lecleire, Aude Coquard, et al.. Enteral Delivery of Proteins Enhances the Expression of Proteins Involved in the Cytoskeleton and Protein Biosynthesis in Human Duodenal Mucosa. The American Journal of Clinical Nutrition, 2015, 102 (2), pp.359-367. ⟨10.3945/ajcn.114.104216⟩. ⟨hal-02305176⟩