Abstract

RationaleIn elderly subjects, splanchnic extraction of amino acids (AA) increases during meals in a process known as splanchnic sequestration of amino acids (SSAA). This process potentially contributes to the age-related progressive decline in muscle mass via reduced peripheral availability of dietary AA. SSAA mechanisms are unknown but may involve an increased net utilization of ingested AA in the splanchnic area.ObjectivesUsing stable isotope methodology in fed adult and old rats to provide insight into age-related SSAA using three hypotheses: 1) an increase in protein synthesis in the gut and/or the liver, 2) an increase in AA oxidation related to an increased ureagenesis, and 3) Kupffer cell (KC) activation consequently to age-related low-grade inflammation.FindingsSplanchnic extraction of Leu (SPELeu) was doubled in old rats compared to adult rats and was not changed after KC inactivation. No age-related effects on gut and liver protein synthesis were observed, but urea synthesis was lower in old rats and negatively correlated to liver Arg utilization. Net whole-body protein synthesis and arterial AA levels were lower in old rats and correlated negatively with SPELeu.ConclusionSSAA is not the consequence of age-related alterations in ureagenesis, gut or liver protein synthesis or of KC activity. However, SSAA may be related to reduced net whole-body protein synthesis and consequently to the reduced lean body mass that occurs during aging.

Highlights

  • Aging is characterized by a progressive decline in muscle protein stores [1]

  • sequestration of amino acids (SSAA) may be related to reduced net whole-body protein synthesis and to the reduced lean body mass that occurs during aging

  • Studies conducted in the fed state showed that aging results in a blunted stimulation of muscle protein synthesis [4]–[][6] that may be related to the progressive loss of muscle mass characterizing sarcopenia [7], [8]

Read more

Summary

Introduction

Aging is characterized by a progressive decline in muscle protein stores [1]. This could be the consequence of a number of factors, including deregulation of protein turnover. Studies conducted in patients in the postabsorptive state did not show any effect of aging on protein kinetics when the results were adjusted for lean body mass [2], [3]. Studies conducted in the fed state showed that aging results in a blunted stimulation of muscle protein synthesis [4]–[][6] that may be related to the progressive loss of muscle mass characterizing sarcopenia [7], [8]. The contribution of muscle to whole-body protein turnover appears diminished in elderly subjects [9]. The inability of elderly people to maintain body protein stores could be attributed to an impaired anabolic response to meals

Objectives
Methods
Results
Conclusion
Full Text
Published version (Free)

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call