Document Detail


Sepsis and development impede muscle protein synthesis in neonatal pigs by different ribosomal mechanisms.
MedLine Citation:
PMID:  21364490     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In muscle, sepsis reduces protein synthesis (MPS) by restraining translation in neonates and adults. Even though protein accretion decreases with development as neonatal MPS rapidly declines by maturation, the changes imposed by development on the sepsis-associated decrease in MPS have not been described. Pigs at 7 and 26 d of age were infused for 8 h with lipopolysaccharide (LPS, endotoxin, 0 and 10 μg · kg⁻¹ · h⁻¹). Fractional MPS rates and translation eukaryotic initiation factor (eIF) activation in muscle were examined (n = 5-7/group). The LPS-induced decrease in MPS was associated with reduced ribosomal and translational efficiency, whereas the age-induced decrease in MPS occurred by decreasing ribosome number. Abundances of mammalian target of rapamycin (mTOR) and S6 decreased, and that of the repressor eIF4E · 4E-binding protein 1 (4EBP1) association increased in 26-d-old pigs--compared with 7-d-old pigs. LPS decreased the abundance of the active eIF4E ·eIF4G association and the phosphorylation of eIF4G across ages, whereas the abundance of eIF4G declined and eIF2α phosphorylation increased with age. Therefore, when lacking anabolic stimulation, the decrease in MPS induced by LPS is associated with reduced ribosomal efficiency and decreased eIF4E ·eIF4G assembly, whereas that induced by development involves reduced ribosomal number, translation factor abundance, and increased eIF2α phosphorylation.
Authors:
Renán A Orellana; Fiona A Wilson; María C Gazzaneo; Agus Suryawan; Teresa A Davis; Hanh V Nguyen
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Pediatric research     Volume:  69     ISSN:  1530-0447     ISO Abbreviation:  Pediatr. Res.     Publication Date:  2011 Jun 
Date Detail:
Created Date:  2011-05-09     Completed Date:  2011-08-22     Revised Date:  2012-09-19    
Medline Journal Info:
Nlm Unique ID:  0100714     Medline TA:  Pediatr Res     Country:  United States    
Other Details:
Languages:  eng     Pagination:  473-8     Citation Subset:  IM    
Affiliation:
Department of Pediatrics, Baylor College of Medicine, Houston, Texas 77030, USA. orellana@bcm.edu
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Animals
Animals, Newborn / metabolism
Blood Glucose / metabolism
Elongation Factor 2 Kinase / metabolism
Eukaryotic Initiation Factor-2 / metabolism
Eukaryotic Initiation Factor-4E / metabolism
Eukaryotic Initiation Factor-4G / metabolism
Female
Insulin / metabolism
Lipopolysaccharides / pharmacology
Muscle Development / physiology*
Muscle Proteins / biosynthesis*
Muscle, Skeletal / drug effects,  physiology
Pregnancy
Protein Biosynthesis*
Random Allocation
Ribosomes / metabolism*
Sepsis / physiopathology*
Signal Transduction / physiology
Swine
Grant Support
ID/Acronym/Agency:
AR-44474/AR/NIAMS NIH HHS; K08 AR-51563/AR/NIAMS NIH HHS; K08 AR051563-05/AR/NIAMS NIH HHS; R01 AR044474-15/AR/NIAMS NIH HHS
Chemical
Reg. No./Substance:
0/Blood Glucose; 0/Eukaryotic Initiation Factor-2; 0/Eukaryotic Initiation Factor-4E; 0/Eukaryotic Initiation Factor-4G; 0/Insulin; 0/Lipopolysaccharides; 0/Muscle Proteins; EC 2.7.1.17/Elongation Factor 2 Kinase
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Determinants of expiratory flow limitation in healthy women during exercise.
Next Document:  Cerebral tissue oxygenation and regional oxygen saturation can be used to study cerebral autoregulat...