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Formation of high-molecular weight angiotensinogen during pregnancy is a result of competing redox reactions with proform of eosinophil major basic protein.
MedLine Citation:
PMID:  23033876     Owner:  NLM     Status:  Publisher    
The plasma concentration of placentally derived proform of eosinophil major basic protein (proMBP) increases in pregnancy, and three different complexes containing proMBP have been isolated from pregnancy plasma and serum: A 2:2 complex with the metalloproteinase, pregnancy-associated plasma protein-A (PAPP-A), a 2:2 complex with angiotensinogen (AGT), and a 2:2:2 complex with AGT and complement C3dg. We show that during human pregnancy, all of circulating proMBP exists in covalent complexes, bound to either PAPP-A or AGT. We also show that the proMBP/AGT complex constitutes the major fraction of circulating high-molecular weight (HMW) AGT in late pregnancy, and that this complex is able to further associate with complement C3 derivatives post-sampling. Clearance experiments in mice suggest that complement C3-based complexes are removed faster from the circulation compared to monomeric AGT and the proMBP/AGT complex. Furthermore, we have used recombinant proteins to analyze formation of the proMBP/PAPP-A and the proMBP/AGT complexes, and we demonstrate that they are competing reactions, depending on the same cysteine residue of proMBP, but differentially on the redox potential, potentially important for the relative amounts of the complexes in vivo. These findings may be important physiologically, since the biochemical properties of the proteins change as a consequence of complex formation.
Søren Kløverpris; Louise Lind Skov; Simon Glerup; Kasper Pihl; Michael Christiansen; Claus Oxvig
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-10-4
Journal Detail:
Title:  The Biochemical journal     Volume:  -     ISSN:  1470-8728     ISO Abbreviation:  Biochem. J.     Publication Date:  2012 Oct 
Date Detail:
Created Date:  2012-10-4     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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