Phosphorylation and carbonylation of placental proteins in normal pregnancy and gestosis.
Study of posttranslational changes in placental proteins revealed disorders in the intensity of their phosphorylation and carbonylation in patients with placental failure. Phosphorylation was reduced for the majority of endogenous placental proteins, substrates for cAMP- and cGMP-dependent protein kinases. An opposite dynamics was noted for oxidative modification of proteins. The content of carbonyl derivatives evaluated in spontaneous and metal-catalyzed oxidation of placental proteins was elevated in gestosis in comparison with the normal level.
Pogorelova
T N
TN
Department of Biomedical Problems, Rostov Institute of Obstetrics and Pediatrics, Federal Agency for High-Technological Medical Care, Rostov-on-Don, Russia. biochem@rniiap.ru
Orlov
V I
VI
Krukier
I I
II
Drukker
N A
NA
D000328:Adult; D002843:Chromatin / Q000201:enzymology / Q000378:metabolism; D017868:Cyclic AMP-Dependent Protein Kinases / Q000378:metabolism; D017869:Cyclic GMP-Dependent Protein Kinases / Q000378:metabolism; D003593:Cytoplasm / Q000201:enzymology / Q000378:metabolism; D005260:Female; D006801:Humans; D008928:Mitochondria / Q000201:enzymology / Q000378:metabolism; D010766:Phosphorylation; D010922:Placenta Diseases / Q000201:enzymology / Q000378:metabolism*; D011247:Pregnancy; D011257:Pregnancy Proteins / Q000378:metabolism*; D050050:Protein Carbonylation; D055815:Young Adult
D002843:Chromatin; D011257:Pregnancy Proteins; D017868:Cyclic AMP-Dependent Protein Kinases; D017869:Cyclic GMP-Dependent Protein Kinases