RMD Open
January 2017
Introduction: Structural damage progression is a major outcome in rheumatoid arthritis (RA). Its evaluation and follow-up in trials should involve radiographic scoring by 1 or 2 readers (reference assessment), which is challenging in large longitudinal cohorts with multiple assessments.
Objectives: To compare the reproducibility of multireader and reference assessment to improve the feasibility of detecting radiographic progression in a large cohort of patients with early arthritis (ESPOIR).
Double-stranded RNA-binding proteins (DRBPs) are known to regulate many processes of RNA metabolism due, among others, to the presence of double-stranded RNA (dsRNA)-binding motifs (dsRBMs). Among these DRBPs, Interleukin enhancer-binding factor 3 (Ilf3) and Nuclear Factor 90 (NF90) are two ubiquitous proteins generated by mutually exclusive and alternative splicings of the Ilf3 gene. They share common N-terminal and central sequences but display specific C-terminal regions.
View Article and Find Full Text PDFOsteoarthritis, a disease characterized by cartilage degradation, abnormal subchondral bone remodelling and some grade of inflammation, and sarcopenia, a condition of pathological muscle weakness associated with altered muscle mass, strength, and function, are prevalent disorders in elderly people. There is increasing evidence that decline in lower limb muscle strength is associated with knee or hip osteoarthritis in a context of pain, altered joint stability, maladapted postures and defective neuromuscular communication. At the cellular and molecular levels, chondrocytes and myoblasts share common pathological targets and pathways, and the close anatomical location of both cell types suggest a possibility of paracrine communication.
View Article and Find Full Text PDFInterleukin enhancer binding factor 3 (Ilf3) and Nuclear Factor 90 (NF90) are two ubiquitous proteins generated by alternative splicing from the ILF3 gene that provides each protein with a long and identical N-terminal domain of 701 amino acids and a specific C-terminal domain of 210 and 15 amino acids, respectively. They exhibit a high polymorphism due to their posttranscriptional and posttranslational modifications. Ilf3 and NF90 functions remain unclear although they have been described as RNA binding proteins but have been implicated in a large scale of cellular phenomena depending on the nature of their interacting partners, the composition of their protein complexes and their subcellular localization.
View Article and Find Full Text PDFObjective: To examine the effects of agonists of peroxisome proliferator-activated receptor (PPAR) gamma on proteoglycan degradation induced by interleukin (IL)-1beta or tumor necrosis factor (TNF)alpha in cartilage in vitro.
Design: Proteoglycan degradation was measured as release of radioactivity from rat cartilage explants previously labeled with (35)SO2-4. Western blots were used to examine tissue levels of aggrecan neoepitopes NITEGE and VDIPEN, generated by aggrecanases and matrix metalloproteinases (MMP), respectively.