Presence of low-grade inflammation impaired postprandial stimulation of muscle protein synthesis in old rats.
Aging is characterized by a decline in muscle mass that could be explained by a defect in the regulation of postprandial muscle protein metabolism. This study was undertaken to examine a possible link between the development of low-grade inflammation (LGI) in elderly and the resistance of muscle protein synthesis and degradation pathways to food intake. Fifty-five 20-month-old-rats were studied for 5 months; blood was withdrawn once a month to assess plasma fibrinogen and alpha2-macroglobulin. Animals were then separated into two groups at 25 months old according to their inflammation status: a control non-inflamed (NI, n=24) and a low-grade inflamed group (LGI, n=23). The day of the experiment, rats received no food or a meal. Muscle protein synthesis was assessed in vivo using the flooding dose method ([1-(13)C]phenylalanine) and muscle phosphorylation of protein S6 kinase, and protein S6 was measured in gastrocnemius muscle. Muscle proteolysis was assessed in vitro using the epitrochlearis muscle. Postabsorptive muscle protein synthesis and proteolysis were similar in NI and LGI. After food intake, muscle protein synthesis was significantly stimulated in NI but remained unresponsive in LGI. Muscle proteolysis was similar in both groups whatever the inflammation and/or the nutritional status. In conclusion, we showed that development of LGI during aging may be responsible, at least in part, for the defect in muscle protein synthesis stimulation induced by food intake in rats. Our results suggested that the control of LGI development in elderly improve meal effect on muscle protein synthesis and consequently slow down sarcopenia.
INRA, UMR 1019 Nutrition Humaine, F-63122 Saint Genès Champanelle, France.
Michèle
M
Balage
Julien
J
Averous
Didier
D
Rémond
Cécile
C
Bos
Estelle
E
Pujos-Guillot
Isabelle
I
Papet
Laurent
L
Mosoni
Lydie
L
Combaret
Dominique
D
Dardevet
D000209:Acute-Phase Proteins / Q000032:analysis; D000375:Aging / Q000378:metabolism*; D000596:Amino Acids / Q000097:blood; D000818:Animals; D045163:Antibodies, Phospho-Specific; D016207:Cytokines / Q000097:blood; D005508:Food Deprivation / Q000502:physiology; D007249:Inflammation / Q000150:complications / Q000378:metabolism*; D009124:Muscle Proteins / Q000096:biosynthesis*; D018482:Muscle, Skeletal / Q000378:metabolism*; D010766:Phosphorylation; D019518:Postprandial Period / Q000502:physiology*; D011499:Protein Processing, Post-Translational; D051381:Rats; D017208:Rats, Wistar; D038601:Ribosomal Protein S6 / Q000378:metabolism; D019893:Ribosomal Protein S6 Kinases / Q000378:metabolism; D055948:Sarcopenia / Q000150:complications / Q000378:metabolism*; D012720:Severity of Illness Index
D000209:Acute-Phase Proteins; D000596:Amino Acids; D045163:Antibodies, Phospho-Specific; D016207:Cytokines; D009124:Muscle Proteins; D038601:Ribosomal Protein S6; D019893:Ribosomal Protein S6 Kinases; C526901:Rps6kb1 protein, rat