Changes in concentration, localization and activity of catalase within the human placenta during early gestation.

Using villous tissue from accurately dated gestational age placentae, this study identified significant changes in the protein concentration, enzyme activity and localization of catalase, an enzyme responsible for the intracellular metabolism of hydrogen peroxide, during the first and early second trimester of pregnancy. Enzyme activity was found to increase approximately threefold between weeks 6 and 17, with the greatest increase between 12 and 17 weeks. Immunostaining of tissue sections was supportive of these findings, demonstrating a progressively stronger signal between weeks 6 and 17. Immunostaining also demonstrated that the main cell types expressing catalase were the cytotrophoblast cells as well as a subset of the stromal cells. Between 13-17 weeks gestation, however, it was possible to detect catalase within the syncytiotrophoblast also, although with a much reduced intensity of staining. At the ultrastructural level, immunogold labelling of catalase clearly showed that staining was predominately compartmentalized within peroxisomes, although non-peroxisomal staining was also seen. Immunoreactivity also demonstrated, via morphological identification, that the stromal cells containing detectable levels of catalase were placental macrophages (Hofbauer cells). These results are in agreement with the proposal that the placenta exists in a physiologically low oxygen environment during the early part of gestation. In this environment oxidative activity of the sort resulting in the generation of hydrogen peroxide would presumably be suppressed, thereby limiting the requirement for catalase until oxygen tension begins to rise.