Document Detail


Iron transfer between the purple phosphatase uteroferrin and transferrin and its possible role in iron metabolism of the fetal pig.
MedLine Citation:
PMID:  7056739     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Uteroferrin, a purple-colored, iron-containing phosphatase which is induced by progesterone in the porcine uterus, has been proposed to be an intermediary in iron transfer between the mother and conceptus in the pig. Along with a number of other uterine proteins of maternal origin, it accumulates in the allantoic fluid during mid-pregnancy. When [59Fe]uteroferrin was introduced into the allantoic sacs of five fetuses at Day 60 of pregnancy, its iron was transferred to another protein, identified as transferrin. The half-life of iron loss from uteroferrin was approximately 24 h and the kinetics suggested an approximately second order process. 59Fe was also distributed to the fetus and was recovered at high specific activity in the fetal red blood cells (as hemoglobin), liver, and spleen. Introduction of [59Fe] transferrin to allantoic fluid resulted in an almost identical distribution of isotope in the fetus as was observed with [59Fe]uteroferrin. Whereas [125I]transferrin has been shown to be capable of leaving the allantoic sac in intact form, [125I]uteroferrin either has only a limited capacity to exit or else is almost immediately degraded upon entering the fetal circulation. Following loss of its iron to transferrin in allantoic fluid, uteroferrin rapidly loses immunological reactivity and is cleaved proteolytically into small peptides. The transfer of iron between uteroferrin and transferrin has also been followed in vitro. Iron on uteroferrin is relatively stable to pH and is not readily lost to transferrin at around neutral pH unless low molecular iron chelators such as citrate, pyrophosphate, ATP, or ascorbate are present. Iron transfer was promoted at ascorbate concentrations (approximately 50 microM) and at pH values (approximately 6.8) approximating those found in allantoic fluid. Results are consistent with a model in which maternal uteroferrin can transfer its iron to fetal transferrin via a low molecular weight intermediary in the allantoic sac. Transferrin is then responsible for iron distribution to the fetus.
Authors:
W C Buhi; C A Ducsay; F W Bazer; R M Roberts
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  257     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1982 Feb 
Date Detail:
Created Date:  1982-04-12     Completed Date:  1982-04-12     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1712-23     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Acid Phosphatase
Allantois / metabolism
Animals
Electrophoresis, Polyacrylamide Gel
Female
Fetus / metabolism*
Hydrogen-Ion Concentration
Iron / metabolism*
Isoenzymes
Kinetics
Maternal-Fetal Exchange
Metalloproteins / metabolism*
Pregnancy
Swine
Tissue Distribution
Transferrin / isolation & purification,  metabolism*
Grant Support
ID/Acronym/Agency:
HD 10436/HD/NICHD NIH HHS; HD-08560/HD/NICHD NIH HHS
Chemical
Reg. No./Substance:
0/Isoenzymes; 0/Metalloproteins; 11096-37-0/Transferrin; 7439-89-6/Iron; EC 3.1.3.-/tartrate-resistant acid phosphatase; EC 3.1.3.2/Acid Phosphatase

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


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