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Increased oxidative stress in pre-eclamptic placenta is associated with altered proteasome activity and protein
1Department of Biochemistry and Tumor Biology, Clinic of Obstetrics and Gynecology (OE6410), Medical School, Podbielskistr. 380, 30659 Hannover, Germany. hass.ralf@mh-hannover.de
Insights
Pre-eclampsia is linked to a 30% increase in damaged placental proteins and a 30% decrease in proteasome function. This suggests impaired protein metabolism contributes to pre-eclampsia development.
Area of Science:
- Biochemistry
- Obstetrics
- Proteomics
Background:
- Oxidatively damaged proteins accumulate in pre-eclampsia.
- The 20S proteasome metabolizes these damaged proteins.
- Reduced proteasome function is implicated in pre-eclampsia.
Purpose of the Study:
- To investigate the role of proteasome function and damaged protein levels in pre-eclampsia.
- To explore molecular alterations in the proteasomal complex in pre-eclamptic placentas.
Main Methods:
- Analysis of oxidatively damaged proteins in normal and pre-eclamptic placentas.
- Evaluation of proteasome activity.
- Two-dimensional SDS-PAGE and Western blotting for proteasome subunits and PP14.
- Silver staining for differentially expressed proteins.
Main Results:
- Pre-eclamptic placentas showed a 30% increase in damaged proteins and a 30% decrease in proteasome function.
- Specific proteasome subunits (approx. 20 kDa and 30 kDa) were underexpressed in pre-eclamptic placentas.
- Differential expression of acidic proteins (20-45 kDa) was observed between normal and pre-eclamptic placentas.
Conclusions:
- Reduced proteasome activity contributes to the accumulation of damaged proteins in pre-eclampsia.
- Alterations in the proteasomal complex and differential protein expression may underlie metabolic interference in pre-eclampsia.
- These findings highlight potential molecular mechanisms contributing to pre-eclampsia pathogenesis.
Abstract:
Analysis of the amount of oxidatively damaged proteins in placenta proteins from normal pregnancies and pre-eclampsia revealed a relative increase of about 30 per cent of damaged proteins in pre-eclamptic placenta. Previous work has demonstrated that these cell- and tissue-damaging oxidatively stressed proteins are metabolized particularly by the 20S proteasome. Evaluation of the proteasomal activity revealed a significantly reduced proteasome function in pre-eclamptic placenta by about 30 per cent, suggesting that the accumulation of oxidatively damaged proteins in pre-eclampsia is associated with reduced proteasomal activity. To investigate these effects at molecular levels, separation of placental proteins by two-dimensional SDS-PAGE and subsequent anti-proteasome Western blot revealed several sets of approximately 20 kDa and 30 kDa protein subunits in normal placenta which appear at low or undetectable expression levels in pre-eclamptic placenta. Control Western blots against the placenta protein 14 (PP14) demonstrated equal loading and no significant differences in the PP14 protein patterns. These data suggested that alteration of the multifactorial proteasomal protein complex in pre-eclamptic placenta is accompanied by reduced metabolization of oxidatively damaged proteins. Consequently, the accumulation of these damaged proteins in the placenta may be associated with metabolic interference and thus contribute to certain developments of pre-eclampsia. Silver staining of the two-dimensional SDS-PAGE revealed a variety of acidic proteins in the range of 20 kDa and 45 kDa, respectively, which are differentially expressed in normal and pre-eclamptic placenta and thus provide further analytic potential for metabolic interference.
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