Document Detail


Oxidized transthyretin in amniotic fluid as an early marker of preeclampsia.
MedLine Citation:
PMID:  17203960     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Preeclampsia is a pregnancy-specific hypertensive syndrome and a major cause of maternal and fetal morbidity and mortality. At the present time, no reliable screening tests to identify women at risk are available. We have compared the amniotic fluids (AF) proteomic maps of five preeclamptic patients with those of five controls. The analysis was carried out by two-dimensional electrophoresis followed by peptide mapping and tandem mass spectrometric analysis. Besides the implementation of the previously published AF proteomic maps, our results show that transthyretin (TTR), the protein responsible for transporting both the thyroid hormone tyroxine and the retinol binding protein, is present in the AF of both preeclamptic and control women as a mixture of dimeric and post-translationally modified monomeric forms. Although the nature of these forms is similar in both groups, the preeclamptic women showed a significant increase in the amount of monomeric proteins with respect to the control group. Since the TTR monomeric forms are the results of different oxidizing reactions, we hypothesize that the higher oxidative stress in preeclampsia is the major destabilizing factor of the TTR functional dimeric form in the preeclamptic women.
Authors:
Carlo Vascotto; Anna Maria Salzano; Chiara D'Ambrosio; Arrigo Fruscalzo; Diego Marchesoni; Carla di Loreto; Andrea Scaloni; Gianluca Tell; Franco Quadrifoglio
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of proteome research     Volume:  6     ISSN:  1535-3893     ISO Abbreviation:  J. Proteome Res.     Publication Date:  2007 Jan 
Date Detail:
Created Date:  2007-01-05     Completed Date:  2007-07-24     Revised Date:  2007-08-17    
Medline Journal Info:
Nlm Unique ID:  101128775     Medline TA:  J Proteome Res     Country:  United States    
Other Details:
Languages:  eng     Pagination:  160-70     Citation Subset:  IM    
Affiliation:
Department of Biomedical Sciences and Technologies, University of Udine, 33100 Udine, Italy.
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MeSH Terms
Descriptor/Qualifier:
Amniocentesis
Amniotic Fluid / metabolism*
Electrophoresis, Gel, Two-Dimensional
Electrophoresis, Polyacrylamide Gel
Female
Humans
Immunohistochemistry
Mass Spectrometry
Oxygen / chemistry*,  metabolism
Pre-Eclampsia / metabolism*
Prealbumin / metabolism*
Pregnancy
Protein Processing, Post-Translational
Proteomics / methods*
Spectrometry, Mass, Electrospray Ionization
Chemical
Reg. No./Substance:
0/Prealbumin; 7782-44-7/Oxygen

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


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