B L Bahr1, M D Price1, D Merrill1, C Mejia1, L Call1, D Bearss1, J Arroyo2. 1. Department of Physiology and Developmental Biology, Brigham Young University, Provo, UT, USA. 2. Department of Physiology and Developmental Biology, Brigham Young University, Provo, UT, USA. Electronic address: jarroyo@byu.edu.
Abstract
INTRODUCTION: Preeclampsia (PE) and intrauterine growth restriction (IUGR) are two diseases that affect pregnant women and their unborn children. These diseases cause low birth weight, pre-term delivery, and neurological and cardiovascular disorders in babies. Combined they account for 20% of preterm deliveries. Pyruvate kinase M2 (PKM2) is a metabolism enzyme found in developing embryonic and cancer tissues. Our objective is to determine the expression of PKM2 in human PE and IUGR compared to normal pregnancies. Understanding expression of PKM2 in PE and IUGR could help us to better understand the mechanisms and find treatments for PE and IUGR. METHODS: Human placental tissues were obtained for PKM2 determination and analyzed by immunohistochemistry, Western blot, and a pyruvate assay. Placental samples were homogenized and cytoplasmic and nuclear proteins were extracted for Western blot analysis. RESULTS: Preeclampsia samples had elevated levels of p-PKM2, p-ERK, and ERK in the cytoplasm. Beta-catenin and lactose dehydrogenase (LDH) were also elevated in preeclampsia placenta samples. DISCUSSION AND CONCLUSION: We conclude that PKM2 is expressed in normal, PE and IUGR pregnancies. Also, that this expression is increased in the PE placenta at delivery. These results suggest placental metabolism through PKM2 could play a role in human preeclampsia.
INTRODUCTION: Preeclampsia (PE) and intrauterine growth restriction (IUGR) are two diseases that affect pregnant women and their unborn children. These diseases cause low birth weight, pre-term delivery, and neurological and cardiovascular disorders in babies. Combined they account for 20% of preterm deliveries. Pyruvate kinase M2 (PKM2) is a metabolism enzyme found in developing embryonic and cancer tissues. Our objective is to determine the expression of PKM2 in human PE and IUGR compared to normal pregnancies. Understanding expression of PKM2 in PE and IUGR could help us to better understand the mechanisms and find treatments for PE and IUGR. METHODS:Human placental tissues were obtained for PKM2 determination and analyzed by immunohistochemistry, Western blot, and a pyruvate assay. Placental samples were homogenized and cytoplasmic and nuclear proteins were extracted for Western blot analysis. RESULTS: Preeclampsia samples had elevated levels of p-PKM2, p-ERK, and ERK in the cytoplasm. Beta-catenin and lactose dehydrogenase (LDH) were also elevated in preeclampsia placenta samples. DISCUSSION AND CONCLUSION: We conclude that PKM2 is expressed in normal, PE and IUGR pregnancies. Also, that this expression is increased in the PE placenta at delivery. These results suggest placental metabolism through PKM2 could play a role in human preeclampsia.
Authors: Emmeli Mikkelsen; Henrik Lauridsen; Per Mose Nielsen; Haiyun Qi; Thomas Nørlinger; Maria Dahl Andersen; Niels Uldbjerg; Christoffer Laustsen; Puk Sandager; Michael Pedersen Journal: R Soc Open Sci Date: 2017-04-26 Impact factor: 2.963
Authors: Kary Y F Tsai; Benton Tullis; Katrina L Breithaupt; Rylan Fowers; Nelson Jones; Samuel Grajeda; Paul R Reynolds; Juan A Arroyo Journal: Cells Date: 2021-04-09 Impact factor: 6.600