Differential Proteomic Analysis of Highly Purified Placental Cytotrophoblasts in Pre-Eclampsia Demonstrates a State of Increased Oxidative Stress and Reduced Cytotrophoblast Antioxidant Defense

Proteomics. 2011 Oct;11(20):4077-84. doi: 10.1002/pmic.201000505. Epub 2011 Aug 30.

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.

MeSH terms

  • Blotting, Western
  • Electrophoresis, Gel, Two-Dimensional
  • Female
  • Fetuins / chemistry
  • Fetuins / metabolism
  • Humans
  • Oxidative Stress*
  • Placenta / metabolism*
  • Pre-Eclampsia / metabolism*
  • Pregnancy
  • Proteomics*
  • Trophoblasts / chemistry
  • Trophoblasts / metabolism*
  • Up-Regulation

Substances

  • Fetuins