Effectiveness of Soluble CTLA-4-Fc in the Inhibition of Bone Marrow T-Cell Activation in Context of Indoleamine 2.3-Dioxygenase (IDO) and CD4Foxp3 Treg Induction.

Background: Rheumatoid arthritis (RA) is a chronic autoimmune disease with systemic inflammation finally resulting in damaged joints. One of the RA development models suggests bone marrow (BM) as a place of inflammation development further leading to disease progression. We aimed to investigate the potential of CTLA-4-Fc molecule in inducing tolerogenic milieu in BM measured as indoleamine 2,3-dioxygenase (IDO) expression, CD4Foxp3 Treg induction, and T cell activation control.

Diminished presentation of complement regulatory protein CD55 on red blood cells from patients with hereditary haemolytic anaemias.

Introduction: Hereditary haemolytic anaemias (HHA) encompass a heterogeneous group of anaemias characterized by decreased red blood cell survival. The aim of this study was to evaluate the status of red blood cell (RBC) surface molecules known or previously proposed to participate in preventing premature RBC clearance, analysing erythrocytes from patients with two types of HHA: hereditary spherocytosis (HS) and microcytosis.

Material/methods: Relative binding of five monoclonal antibodies (mAbs), anti-CD55, anti-CD59, anti-CD44, anti-CD47 and anti-CD58, was evaluated in erythrocytes of patients with HS and hereditary microcytosis, using flow cytometry.

In vivo evidence for cooperation of Mia40 and Erv1 in the oxidation of mitochondrial proteins.

The intermembrane space of mitochondria accommodates the essential mitochondrial intermembrane space assembly (MIA) machinery that catalyzes oxidative folding of proteins. The disulfide bond formation pathway is based on a relay of reactions involving disulfide transfer from the sulfhydryl oxidase Erv1 to Mia40 and from Mia40 to substrate proteins. However, the substrates of the MIA typically contain two disulfide bonds.

Elements regulating Potato leafroll virus sgRNA1 translation are located within the coding sequences of the coat protein and read-through domain.

Translation of viral proteins from subgenomic RNAs (sgRNAs) is a common strategy among positive-stranded RNA viruses. Unlike host mRNA, sgRNA of Potato leafroll virus (PLRV) does not possess a cap at its 5' end nor a poly(A) tail at the 3' terminus, both of which are known to be crucial for translation of RNA in eukaryotic cells. Here, we demonstrate, that in wheat germ extract (WGE) truncation of the sgRNA1 5' UTR increases translation efficiency, as it has previously been observed in rabbit reticulocyte lysate (RRL), whereas removal of the 3' UTR does not affect translation.