The Correlation Between Neutrophil Elastase and Neutrophil-Lymphocyte Ratio in Endothelial Dysfunction of Preeclampsia.

BACKGROUND: Preeclampsia (PE) is a serious inflammatory process that is unique to pregnancy, occurring at or after the 20th week of pregnancy, and leading to maternal and neonatal illness and systemic disruptions. Placental hypoxia leads to increased levels of cytokines and inflammatory syncytiotrophoblast microvillus membrane microparticles (STBM) which activates neutrophils leading to oxidative stress and endothelial dysfunction in preeclampsia. The mechanisms that cause PE in people remain unknown. To understand the pathophysiology of PE, numerous theories have been given. There is currently no proven treatment or early detecting marker for PE available so far. METHODS: The present study includes 40 patients (20 controls and 20 PE patients) aged 20-45 years hospitalized at the Department of Obstetrics and Gynecology, Hamdard Institute of Medical Sciences and Research (HIMSR) and Hakeem Abdul Hameed Centenary (HAHC) Hospital, Jamia Hamdard, New Delhi. Nitric oxide (NO), neutrophil elastase (NE), and the neutrophil-to-lymphocyte ratio were measured. The blood and biochemical parameters in PE patients were also analyzed. RESULTS: The neutrophil-to-lymphocyte ratio (NLR) was significantly increased in PE patients as compared to healthy pregnant. All the biochemical and hemodynamic parameters were assessed. The serum NO concentrations were lower in PE patients and endothelial dysfunction markers (NE and von Willebrand factor {vWF}) were markedly increased in PE patients. The difference was statistically significant with a p-value <0.05. CONCLUSIONS: NLR is greatly increased in PE patients. An increase in NLR in PE patients occurs due to an increase in inflammatory markers and endothelial damage. Hence, the NLR could act as a novel diagnostic biomarker for depicting PE progression.

Structural evidence that MOAP1 and PEG10 are derived from retrovirus/retrotransposon Gag proteins.

The Gag proteins of retroviruses play an essential role in virus particle assembly by forming a protein shell or capsid and thus generating the virion compartment. A variety of human proteins have now been identified with structural similarity to one or more of the major Gag domains. These human proteins are thought to have been evolved or "domesticated" from ancient integrations due to retroviral infections or retrotransposons. Here, we report that X-ray crystal structures of stably folded domains of MOAP1 (modulator of apoptosis 1) and PEG10 (paternally expressed gene 10) are highly similar to the C-terminal capsid (CA) domains of cognate Gag proteins. The structures confirm classification of MOAP1 and PEG10 as domesticated Gags, and suggest that these proteins may have preserved some of the key interactions that facilitated assembly of their ancestral Gags into capsids.