Ricerc@Sapienza

We analyzed whether serum albumin is independently associated with portal vein thrombosis (PVT) in liver cirrhosis (LC) and if a biologic plausibility exists. This study was divided into three parts. In part 1 (retrospective analysis), 753 consecutive patients with LC with ultrasound-detected PVT were retrospectively analyzed. In part 2, 112 patients with LC and 56 matched controls were entered in the cross-sectional study.

Background: Malnutrition-inflammation complex syndrome (MICS) is a common and usually concurrent condition occurring in patients undergoing hemodialysis (HD), with a pathogenesis linked to biological and in situ environmental traditional risk factors. Periodontitis, one of the major types of infection-driven inflammation, often co-occurs in the in the hemodialysis population and correlates with markers of malnutrition and inflammation, such as albumin, creatinine, and C-reactive protein.

The most abundant plasma protein, human serum albumin (HSA), plays a key part in the body’s antioxidant defense against reactive species [1]. This study was aimed at correlating oxidant-induced chemical and structural effects on HSA [2].

Human Serum Albumin (HSA), the most abundant protein of body fluids, has a “modular” three-domain structure potentially responding to stress by means of changes of conformation (1). Besides acting as the main carrier protein of the circulation, HSA is also an obvious target of extracellular reactive oxidant species due to its high abundance in plasma. It is for this reason considered the main anti-oxidant defense in blood (2).

The most abundant plasma protein, Human Serum Albumin (HSA), is known to undergo conformational transitions in acidic environment [1]. To avoid buffer effects and correlate global and local structural changes, we developed a continuous acidification method and simultaneously monitored the protein changes by both small-angle scattering (SAXS) and fluorescence [2], using a dedicated instrumental platform [3].

The use of UV-C light as a means to inactivate pathogens in biological media containing blood components or plasma derivatives has recently been rediscovered. Although highly effective, these treatments may have deleterious effects on plasma proteins such as albumin, fibrinogen and immunoglobulins. Here we investigate the use of three natural antioxidants, gallic acid, nicotinic acid and ascorbic acid, as potential stabilizers of human albumin (HA) during irradiation by UV at 254 nm.