| Sepsis and development impede muscle protein synthesis in neonatal pigs by different ribosomal mechanisms. | |
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MedLine Citation:
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PMID: 21364490 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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Renán A Orellana; Fiona A Wilson; María C Gazzaneo; Agus Suryawan; Teresa A Davis; Hanh V Nguyen |
Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S. |
Journal Detail:
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Title: Pediatric research Volume: 69 ISSN: 1530-0447 ISO Abbreviation: Pediatr. Res. Publication Date: 2011 Jun |
Date Detail:
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Created Date: 2011-05-09 Completed Date: 2011-08-22 Revised Date: 2012-09-19 |
Medline Journal Info:
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Nlm Unique ID: 0100714 Medline TA: Pediatr Res Country: United States |
Other Details:
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Languages: eng Pagination: 473-8 Citation Subset: IM |
Affiliation:
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Department of Pediatrics, Baylor College of Medicine, Houston, Texas 77030, USA. orellana@bcm.edu |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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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:
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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:
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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
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