Disease relevance of OSM

• Oncostatin M (OSM) is a cytokine of the IL-6 family whose levels are increased in the serum and synovial fluids of patients with rheumatoid arthritis [1].
• Oncostatin M (OSM), a pleiotropic cytokine originally isolated from supernatants of the U937 histiocytic lymphoma cell line, has been shown to have regulatory effects on a wide variety of cultured and tumor cells [2].

High impact information on OSM

• Estrogen significantly and dose-dependently countered CTX-II release from TNFalpha plus OSM-stimulated cartilage explants ex vivo [3].
• The effects of estrogen (1-100 nM) on chondrocytes were investigated in bovine cartilage explants subjected to catabolic cytokines (tumor necrosis factor alpha [TNFalpha] and oncostatin M [OSM]) [3].
• Inhibition of furin-like enzymes blocks interleukin-1alpha/oncostatin M-stimulated cartilage degradation [4].
• OSM induced TIMP-3 mRNA and protein expression in a dose- and time-dependent fashion [1].
• Oncostatin M up-regulates tissue inhibitor of metalloproteinases-3 gene expression in articular chondrocytes via de novo transcription, protein synthesis, and tyrosine kinase- and mitogen-activated protein kinase-dependent mechanisms [1].

Biological context of OSM

• OSM induction of TIMP-3 gene expression was dependent upon de novo protein synthesis and transcription [1].
• RNA decay time-courses suggested that the OSM-mediated increase of TIMP-3 RNA was not due to enhanced message stability and, along with inhibition by actinomycin-D, suggested a transcriptional control [1].
• Phosphorothioate antisense oligonucleotide directed against bFGF inhibited OSM induced BAE cell proliferation and spindle shape formation but had only a minimal effect on migration [2].

Anatomical context of OSM

• We examined responsiveness of the TIMP-3 gene to OSM in articular chondrocytes and studied the regulatory and signaling mechanisms of this response [1].
• In addition, OSM stimulated endothelial cell proliferation and migration as well as acquisition of a spindle shape [2].
• METHODS: Bovine articular cartilage explants were cultured in the presence of interleukin 1a, oncostatin M, and plasminogen to induce cartilage degradation [5].

Associations of OSM with chemical compounds

• OBJECTIVES: Retinoic acid (RetA) and oncostatin M (OSM) have both been shown to mediate potent effects with respect to extracellular matrix integrity [6].
• METHODS: Animal and human cartilage samples were used to assess the ability of RetA + OSM to promote the release of collagen and proteoglycan fragments, which was determined by measuring glycosaminoglycan and hydroxyproline, respectively [6].

Regulatory relationships of OSM

• Oncostatin M induces basic fibroblast growth factor expression in endothelial cells and promotes endothelial cell proliferation, migration and spindle morphology [2].

Other interactions of OSM

• The antibody bound to ovine and bovine submaxillary mucins (OSM and BSM) [7].
• Suboptimal doses of IL17 synergised potently with TNFalpha, IL1, OSM, and IL6 to promote collagen degradation [8].
• Transforming growth factor beta1 blocks the release of collagen fragments from boving nasal cartilage stimulated by oncostatin M in combination with IL-1alpha [9].

Analytical, diagnostic and therapeutic context of OSM

• Western blot analysis demonstrated that OSM stimulated predominantly the synthesis of a 22 kDa form of bFGF [2].
• OSM treatment of BAE cells enhanced the synthesis of bFGF protein as determined by ELISA assays [2].

References