Format

Send to

Choose Destination
Am J Clin Nutr. 2015 Aug;102(2):359-67. doi: 10.3945/ajcn.114.104216. Epub 2015 Jun 24.

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

Author information

1
INSERM Unit 1073, Rouen, France; Institute for Research and Innovation in Biomedicine, Rouen University, Rouen, France;
2
Institute for Research and Innovation in Biomedicine, Rouen University, Rouen, France; Platform of Proteomics PISSARO, Mont-Saint-Aignan, France.
3
INSERM Unit 1073, Rouen, France; Institute for Research and Innovation in Biomedicine, Rouen University, Rouen, France; Gastroenterology, Rouen University Hospital, Rouen, France;
4
Pharmacy, and.
5
Institute for Research and Innovation in Biomedicine, Rouen University, Rouen, France; Clinical Investigation Centre CIC 1404-INSERM, Rouen, France;
6
Institute for Research and Innovation in Biomedicine, Rouen University, Rouen, France; INSERM Unit 982, Mont-Saint-Aignan, France; and Platform of Proteomics PISSARO, Mont-Saint-Aignan, France.
7
INSERM Unit 1073, Rouen, France; Institute for Research and Innovation in Biomedicine, Rouen University, Rouen, France; Departments of Nutrition, pierre.dechelotte@inserm.fr.
8
INSERM Unit 1073, Rouen, France; Clinical Investigation Centre CIC 1404-INSERM, 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 · 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.

TRIAL REGISTRATION:

ClinicalTrials.gov NCT01254110.

KEYWORDS:

cytoskeleton; duodenum; enteral nutrition; proteins; proteome

PMID:
26109581
DOI:
10.3945/ajcn.114.104216
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Silverchair Information Systems
Loading ...
Support Center