Associations between overweight, obesity, and mental health: a retrospective study among European adults aged 50.

Background: The comorbidities associated with overweight and obesity have been well researched and scientifically proven while their relationship to mental health is still not verified.

Methods: This study is aimed at investigating reciprocal associations between obesity and mental health, and is intended to further analyze possible long-term effects using data from the Survey of Health, Ageing and Retirement in Europe (SHARE). In order to do that, waves 4 and 8, conducted in 2010 and 2019/20 of this survey, were analyzed in a cross-lagged panel approach including 16,184 adult Europeans (50+) using multiple linear regression analysis focusing on the Body Mass Index (BMI), depression status and quality of life (QoL).

First determination of fullerenes in the Austrian market and environment: quantitative analysis and assessment.

This study forms the first report on analyzing fullerenes in the Austrian environment and cosmetic products available on the Austrian market. We developed, optimized, and validated a novel method for the analysis of C and C fullerenes and N-methylfulleropyrrolidine C (NMFP) for measuring sensitivities in the low nanograms per liter range in order to prove their presence in the environment (12 wastewater- and 12 sewage sludge samples) and in 11 selected fullerene-containing cosmetic products from three different brands. The optimized method relies on a liquid-liquid extraction (LLE) or solid-liquid extraction (SLE) and, for the first time, introduced the Carrez-clarification, followed by liquid chromatography (LC) and coupled to a hybrid triple quadrupole mass spectrometry (MS) quantification.

Interleukin 10-coated nanoparticle systems compared for molecular imaging of atherosclerotic lesions.

Atherosclerosis (AS) is one of the leading causes of mortality in high-income countries. Early diagnosis of vulnerable atherosclerotic lesions is one of the biggest challenges currently facing cardiovascular medicine. The present study focuses on developing targeted nanoparticles (NPs) in order to improve the detection of vulnerable atherosclerotic-plaques.

Biophysical analysis of the interaction of the serum protein human β2GPI with bacterial lipopolysaccharide.

There are several human serum proteins for which no clear role is yet known. Among these is the abundant serum protein beta2-glycoprotein-I (β2GPI), which is known to bind to negatively charged phospholipids as well as to bacterial lipopolysaccharides (LPS), and was therefore proposed to play a role in the immune response. To understand the details of these interactions, a biophysical analysis of the binding of β2GPI to LPS and phosphatidylserine (PS) was performed.

Effects of beta2-glycoprotein-I on platelet aggregation in cord versus adult whole blood.

We present a peculiarity of the neonatal hemostatic system that might contribute to establish a procoagulant readiness in neonatal blood by sensitizing neonatal platelets for ADP stimulation. beta2-glycoprotein-I (beta2-GP-I) is a plasma constituent capable of suppressing ADP-induced platelet aggregation. We found significant lower levels of beta2-GP-I in cord vs.

Membrane binding of beta2-glycoprotein I can be described by a two-state reaction model: an atomic force microscopy and surface plasmon resonance study.

Complexes formed between beta2GPI (beta2-glycoprotein I), a human plasma protein, and biological membranes are considered to be targets of macrophages and antiphospholipid autoantibodies involved in autoimmune diseases, such as antiphospholipid syndrome or systemic lupus erythematosus. The positively charged lysine-rich fifth domain of beta2GPI facilitates its interaction with phospholipid membranes containing acidic phospholipids, which normally become exposed by apoptotic processes. In the present study, atomic force microscopy was applied to visualize the binding of beta2GPI to a mixed phospholipid model membrane at physiological ionic strength.

Solution structure of human and bovine beta(2)-glycoprotein I revealed by small-angle X-ray scattering.

beta(2)-Glycoprotein I (beta(2)GPI) is a highly glycosylated phospholipid-binding plasma protein comprised of four complement control protein (CCP) domains and a distinct fifth domain. The structural organisation of human and bovine beta(2)GPI in aqueous solution was studied by small-angle X-ray scattering (SAXS). Low-resolution models that match the SAXS experimental data best were independently constructed by three different ab initio 3D-reconstruction algorithms.