Document Detail

Reduced expression of intestinal N-acetylglutamate synthase in suckling piglets: a novel molecular mechanism for arginine as a nutritionally essential amino acid for neonates.
MedLine Citation:
PMID:  20931344     Owner:  NLM     Status:  In-Data-Review    
The objective of this study was to determine developmental changes in mRNA and protein levels for N-acetylglutamate synthase (NAGS; a key enzyme in synthesis of citrulline and arginine from glutamine/glutamate and proline) in the small intestine of suckling piglets. The porcine NAGS gene was cloned using the real-time polymerase-chain reaction (RT-PCR) method. The porcine NAGS gene encoded 368 amino acid residues and had a high degree of sequence similarity to the "conserved domain" of human and mouse NAGS genes. The porcine NAGS gene was expressed in E. coli BL21 and a polyclonal antibody against the porcine NAGS protein was developed. Real-time RT-PCR and western-blot analyses were performed to quantify NAGS mRNA and protein, respectively, in the jejunum and ileum of 1- to 28-day-old pigs. Results indicated that intestinal NAGS mRNA levels were lower in 7- to 28-day-old than in 1-day-old pigs. Immunochemical analysis revealed that NAGS protein was localized in enterocytes of the gut. Notably, intestinal NAGS protein abundance declined progressively during the 28-day suckling period. The postnatal decrease in NAGS protein levels was consistent with the previous report of reduced NAGS enzymatic activity as well as reduced synthesis of citrulline and arginine in the small intestine of 7- to 28-day-old pigs. Collectively, these results suggest that intestinal NAGS expression is regulated primarily at the post-transcriptional level. The findings also provide a new molecular basis to explain that endogenous synthesis of arginine is impaired in sow-reared piglets and arginine is a nutritionally essential amino acid for the neonates.
Meimei Geng; Tiejun Li; Xiangfeng Kong; Xiaoyan Song; Wuying Chu; Ruilin Huang; Yulong Yin; Guoyao Wu
Related Documents :
1322354 - The human beta-subunit of rod photoreceptor cgmp phosphodiesterase: complete retinal cd...
8138024 - Comparative structural analysis of human and rat 65 kda tumor-associated phosphoproteins.
8357834 - Molecular and biochemical characterization of a recombinant human pkc-delta family member.
21564134 - The electrophoretic separation of spermatozoa: an analysis of genotype, surface carbohy...
12242034 - Cdna cloning and expression of human activin betae subunit.
9109654 - Electron transfer proteins from the haloalkaliphilic archaeon natronobacterium pharaoni...
Publication Detail:
Type:  Journal Article     Date:  2010-10-08
Journal Detail:
Title:  Amino acids     Volume:  40     ISSN:  1438-2199     ISO Abbreviation:  Amino Acids     Publication Date:  2011 May 
Date Detail:
Created Date:  2011-04-21     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9200312     Medline TA:  Amino Acids     Country:  Austria    
Other Details:
Languages:  eng     Pagination:  1513-22     Citation Subset:  IM    
Key Laboratory for Agro-ecological Processes in Subtropical Region, Institute of Subtropical Agriculture, The Chinese Academy of Sciences, Changsha, Hunan, 410125, China.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms

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

Previous Document:  Superoxide dismutase type 1 in monocytes of chronic kidney disease patients.
Next Document:  Liver autoantibodies in patients with scleroderma.