[Determining factors of survival in patients with severe coronavirus infection admitted to intensive care unit in the third and fourth waves of COVID-19 pandemic].

Introduction: During COVID-19 pandemic, a high mortality rate (20-60%) of patients admitted to intensive care unit has been observed. Identification of risk factors can support the understanding of disease pathophysiology and the recognition of vulnerable patients, prognostication and selection of appropriate treatment.

Objective: Beyond characterisation of a local, critically ill COVID-19 population, analysis of the associations between demographic/clinical data and patient survival were investigated.

Hospitals with and without neurosurgery: a comparative study evaluating the outcome of patients with traumatic brain injury.

Background: We leveraged the data of the international CREACTIVE consortium to investigate whether the outcome of traumatic brain injury (TBI) patients admitted to intensive care units (ICU) in hospitals without on-site neurosurgical capabilities (no-NSH) would differ had the same patients been admitted to ICUs in hospitals with neurosurgical capabilities (NSH).

Methods: The CREACTIVE observational study enrolled more than 8000 patients from 83 ICUs. Adult TBI patients admitted to no-NSH ICUs within 48 h of trauma were propensity-score matched 1:3 with patients admitted to NSH ICUs.

Institutionally Adopted Perioperative Blood Management Program Significantly Decreased the Transfusion Rate of Patients Having Primary Total Hip Replacement Surgery.

Perioperative transfusion in patients undergoing orthopedic surgery increases the number of postoperative complications. Thus, we have introduced an institution-tailored perioperative blood management program (PBM) to decrease the amount of blood transfused in patients going through primary total hip replacement (THR) surgery. We have conducted a before-after observational cohort study in two predetermined observational periods.

Fibrinogen level at hospital admission after multiple injury correlates with BMI and is negatively associated with the need for transfusion and early multiple organ failure.

Introduction: Bleeding and coagulopathy are leading causes of morbidity and lethal outcome after multiple injuries. The pathophysiology of traumatic coagulopathy is under extensive investigations and recent results highlighted the central role of fibrinogen and the fibrin polymerisation process. Our goal was to investigate the factors influencing fibrinogen level and the consequences of hypofibrinogenaemia with clinical importance.

Variations and obstacles in the use of coagulation factor concentrates for major trauma bleeding across Europe: outcomes from a European expert meeting.

Purpose: Trauma is a leading cause of mortality, with major bleeding and trauma-induced coagulopathy (TIC) contributing to negative patient outcomes. Treatments for TIC include tranexamic acid (TXA), fresh frozen plasma (FFP), and coagulation factor concentrates (CFCs, e.g.

Advanced Trauma Life Support (ATLS) in Hungary; The First 10 Years.

Advanced Trauma Life Support (ATLS) programs are recognized as the standard educational trauma program worldwide. Data suggest that ATLS has a positive impact on the value of trauma care. The ATLS Hungary program has been started in 2005, celebrating its 10-year anniversary this year.

Chaperone-related immune dysfunction: an emergent property of distorted chaperone networks.

Molecular chaperones (heat shock proteins) are important components of cellular networks, such as protein-protein and gene regulatory networks. Chaperones participate in the folding of immunologically important proteins, presentation of antigens and activation of the immune system. Here, we propose that chaperone-related immune dysfunction might be more general than was previously thought.

FAD oxidizes the ERO1-PDI electron transfer chain: the role of membrane integrity.

The molecular steps of the electron transfer in the endoplasmic reticulum from the secreted proteins during their oxidation are relatively unknown. We present here that flavine adenine dinucleotide (FAD) is a powerful oxidizer of the oxidoreductase system, Ero1 and PDI, besides the proteins of rat liver microsomes and HepG2 hepatoma cells. Inhibition of FAD transport hindered the action of FAD.

Diabetic changes in the redox status of the microsomal protein folding machinery.

Changes in assisted protein folding are largely unexplored in diabetes. In the present studies, we have identified a reductive shift in the redox status of rat liver microsomes after 4 weeks of streptozotocin-induced diabetes. This change was reflected by a significant increase in the total- and protein-sulfhydryl content, as well as in the free sulfhydryl groups of the major protein disulfide isomerases (PDIs), the 58 kDa PDI and the 57 kDa ERp57 but not other chaperones.

DUK114, the Drosophila orthologue of bovine brain calpain activator protein, is a molecular chaperone.

UK114, the goat liver tumour antigen, is a member of a widely distributed family of conserved low-molecular-mass proteins (YER057c/YjgF/UK114), the function of which is ill understood. To the various orthologues diverse functions have been ascribed, such as translation inhibition, regulation of purine repressor or calpain activation. Owing to a limited sequence similarity to Hsp90 (heat-shock protein 90), they have also been proposed to be molecular chaperones; however, this has never been tested.

Enhancement of complement-induced cell lysis: a novel mechanism for the anticancer effects of Hsp90 inhibitors.

Molecular chaperones (heat shock proteins, Hsp-s) play a pleiotropic role in immunological functions. Hsp-s participate in the presentation of peptide antigens, folding of several immunologically important proteins, such as the MHC, and in the maintenance of the activation-competent conformation of key signaling molecules (mostly serine/threonine and tyrosine kinases) of B and T cells activation. The most abundant cytoplasmic chaperone, Hsp90, is in the center of these processes.

FAD transport and FAD-dependent protein thiol oxidation in rat liver microsomes.

The transport of FAD and its effect on disulfide bond formation was investigated in rat liver microsomal vesicles. By measuring the intravesicular FAD-accessible space, we observed that FAD permeates across the microsomal membrane and accumulates in the lumen. Rapid filtration experiments also demonstrated the uptake and efflux of the compound, which could be inhibited by atractyloside and 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid.

Reduction of the endoplasmic reticulum accompanies the oxidative damage of diabetes mellitus.

The endoplasmic reticulum (ER), similary to other subcompartments of the eukaryotic cell possesses a relatively oxidizing environment. The special milieu of ER lumen is important for many ER-specific processes (redox protein folding, glycoprotein synthesis, quality control of secreted proteins, antigen presentation, etc.).

Molecular chaperones, stress proteins and redox homeostasis.

Protection against oxidative stress is highly interrelated with the function of the most ancient cellular defense system, the network of molecular chaperones, heat shock, or stress-proteins. These ubiquitous, conserved proteins help other proteins and macromolecules to fold or re-fold and reach their final, native conformation. Redox regulation of protein folding becomes especially important during the preparation of extracellular proteins to the outside oxidative milieu, which should take place in a gradual and step-by-step controlled manner in the endoplasmic reticulum or in the periplasm.

[Stress proteins in medicine].

Stress proteins or in other words heat shock proteins form an ancient defense system of our cells. They are necessary to prevent the aggregation of damaged proteins and to help their refolding after stress. Stress protein-assisted remodeling of protein structure is an important step of many cellular processes, such as protein transport, signaling and protein degradation.

Chaperone function and chaperone overload in the aged. A preliminary analysis.

Chaperones have an important role in the repair of proteotoxic damage, which is greatly increased in aged subjects. Chaperone levels and expression were subject of numerous studies in aged organisms. However, there were only very few attempts to measure chaperone activity in aged animals.