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Differential proteomic analysis of highly purified placental cytotrophoblasts in pre‐eclampsia demonstrates a state of increased oxidative stress and reduced cytotrophoblast antioxidant defense
Author(s) -
Johnstone Edward D.,
Sawicki Grzgorz,
Guilbert Larry,
WinklerLowen Bonnie,
Cadete Virgilio J. J.,
Morrish Donald W.
Publication year - 2011
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201000505
Subject(s) - syncytiotrophoblast , cytotrophoblast , hsp70 , oxidative stress , glutathione , heat shock protein , protein disulfide isomerase , placenta , biochemistry , phosphoglycerate mutase , biology , gpx1 , triosephosphate isomerase , chemistry , glutathione peroxidase , superoxide dismutase , enzyme , glycolysis , fetus , pregnancy , genetics , gene
Abstract Proteomics were performed using highly (99.99%) purified cytotrophoblasts from six normal and six pre‐eclamptic placentas. Eleven proteins were found which decreased in pre‐eclampsia (actin, glutathione S ‐transferase, peroxiredoxin 6, aldose reductase, heat shock protein 60 (Hsp60), two molecular forms of heat shock protein 70 (Hsp70) β‐tubulin, subunit proteasome, ezrin, protein disulfide isomerase, and phosphoglycerate mutase 1). Only one protein, α‐2‐HS‐glycoprotein (fetuin), was found to increase its expression. Western blots of actin, Hsp70, ezrin, and glutatione S ‐transferase confirmed decrease in protein expression. Many of the proteins that decreased are consistent with a state of oxidative stress in the pre‐eclamptic placenta and a decreased cytotrophoblast defense against and response to oxidative stress.