RT journal article
T1 Characterization of NO-induced Nitrosative Status in Human Placenta from Pregnant Women with Gestational Diabetes Mellitus
A1 Visiedo García, Francisco Manuel
A1 Santos Rosendo, Celeste
A1 Mateos Bernal, Rosa María
A1 Gil Sánchez, María del Mar
A1 Bugatto González, Fernando
A1 Aguilar Diosdado, Manuel
A1 Segundo Iglesias, Maria del Carmen
A1 López Tinoco, Cristina
A2 Anatomía y Embriología Humana
K1 pregnancy, nitrosative and oxidative stress, gestational diabetes mellitus, placenta
K1 pregnancy
K1 nitrosative and oxidative stress
K1 gestational diabetes mellitus
K1 placenta
AB Dysregulation of NO production is implicated in pregnancy-related diseases, including gestational diabetes mellitus (GDM). The role of NO and its placental targets in GDM pregnancies has yet to be determined. S-Nitrosylation is the NO-derived posttranslational protein modification that can modulate biological functions by forming NO-derived complexes with longer half- life, termed S-nitrosothiol (SNO). Our aim was to examine the presence of endogenous S-nitrosylated proteins in cysteine residuesin relation to antioxidant defense, apoptosis, and cellular signal transduction in placental tissue from control (𝑛������= 8) and GDM (𝑛������= 8) pregnancies. S-Nitrosylation was measured using the biotin-switch assay, while the expression and protein activity were assessed by immunoblotting and colorimetric methods, respectively. Results indicated that catalase and peroxiredoxin nitrosylation levels were greater in GDM placentas, and that was accompanied by reduced catalase activity. S-Nitrosylation of ERK1/2 and AKTwas increased in GDM placentas, and their activities were inhibited. Activities of caspase-3 and caspase-9 were increased, with the latter also showing diminished nitrosylation levels. These findings suggest that S-nitrosylation is a little-known, but critical, mechanism by which NO directly modulates key placental proteins in women with GDM and, as a consequence, maternal and fetalanomalies during pregnancy can occur.
PB HINDAWI LTD
SN 1942-0900
YR 2017
FD 2017-03-16
LK http://hdl.handle.net/10498/35070
UL http://hdl.handle.net/10498/35070
LA eng
DS Repositorio Institucional de la Universidad de Cádiz
RD 08-nov-2026