Document Detail


Polyamine synthesis from proline in the developing porcine placenta.
MedLine Citation:
PMID:  15576824     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Polyamines (putrescine, spermidine, and spermine) are essential for placental growth and angiogenesis. However, little is known about polyamine synthesis in the porcine placenta during conceptus development. The present study was conducted to test the hypothesis that arginine and proline are the major sources of ornithine for placental polyamine production in pigs. Placentae, amniotic fluid, and allantoic fluid were obtained from gilts on Days 20, 30, 35, 40, 45, 50, 60, 90, and 110 of the 114-day gestation (n = 6 per day). Placentae as well as amniotic and allantoic fluids were analyzed for arginase, proline oxidase, ornithine aminotransferase (OAT), ornithine decarboxylase (ODC), proline transport, concentrations of amino acids and polyamines, and polyamine synthesis using established radiochemical and chromatographic methods. Neither arginase activity nor conversion of arginine into polyamines was detected in the porcine placenta. In contrast, both proline and ornithine were converted into putrescine, spermidine, and spermine in placental tissue throughout pregnancy. The activities of proline oxidase, OAT, and ODC as well as proline transport, polyamine synthesis from proline, and polyamine concentrations increased markedly between Days 20 and 40 of gestation, declined between Days 40 and 90 of gestation, and remained at the reduced level through Day 110 of gestation. Proline oxidase and OAT, but not arginase, were present in allantoic and amniotic fluids for the production of ornithine (the immediate substrate for polyamine synthesis). The activities of these two enzymes as well as the concentrations of ornithine and total polyamines in fetal fluids were highest at Day 40 but lowest at Days 20, 90, and 110 of gestation. These results indicate that proline is the major amino acid for polyamine synthesis in the porcine placenta and that the activity of this synthetic pathway is maximal during early pregnancy, when placental growth is most rapid. Our novel findings provide a new base of information for future studies to define the role of proline in fetoplacental growth and development.
Authors:
Guoyao Wu; Fuller W Bazer; Jianbo Hu; Greg A Johnson; Thomas E Spencer
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2004-12-01
Journal Detail:
Title:  Biology of reproduction     Volume:  72     ISSN:  0006-3363     ISO Abbreviation:  Biol. Reprod.     Publication Date:  2005 Apr 
Date Detail:
Created Date:  2005-03-22     Completed Date:  2005-08-30     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0207224     Medline TA:  Biol Reprod     Country:  United States    
Other Details:
Languages:  eng     Pagination:  842-50     Citation Subset:  IM    
Affiliation:
Department of Animal Science, Texas A&M University, College Station, Texas 77843-2471, USA. g-wu@tamu.edu
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MeSH Terms
Descriptor/Qualifier:
1-Pyrroline-5-Carboxylate Dehydrogenase
Amniotic Fluid / metabolism
Animals
Arginase / metabolism
Carbon Radioisotopes / diagnostic use
Female
Fetal Development / physiology*
Male
Methionine / metabolism
Ornithine / metabolism
Oxidoreductases Acting on CH-NH Group Donors / metabolism
Placenta / growth & development*,  metabolism*
Polyamines / metabolism*
Pregnancy
Proline / metabolism*
Putrescine / metabolism
S-Adenosylmethionine / metabolism
Spermidine / metabolism
Spermine / metabolism
Sus scrofa
Chemical
Reg. No./Substance:
0/Carbon Radioisotopes; 0/Polyamines; 110-60-1/Putrescine; 124-20-9/Spermidine; 147-85-3/Proline; 29908-03-0/S-Adenosylmethionine; 63-68-3/Methionine; 7006-33-9/Ornithine; 71-44-3/Spermine; EC 1.5.-/Oxidoreductases Acting on CH-NH Group Donors; EC 1.5.1.12/1-Pyrroline-5-Carboxylate Dehydrogenase; EC 3.5.3.1/Arginase

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


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